AU2013201343A1

AU2013201343A1 - Peptide vaccines for cancers expressing tumor-associated antigens

Info

Publication number: AU2013201343A1
Application number: AU2013201343A
Authority: AU
Inventors: Ryuji Ohsawa; Takuya Tsunoda
Original assignee: Oncotherapy Science Inc
Current assignee: Oncotherapy Science Inc
Priority date: 2007-02-21
Filing date: 2013-03-07
Publication date: 2013-03-28
Anticipated expiration: 2028-02-21
Also published as: AU2013201340B2; AU2013201340A1; AU2013201338B2; AU2013201338A1; AU2013201343B2

Abstract

C:\NRPortbl\DCC\AARW308539_ ,DOC-12/122012 -85 The present invention provides peptides having an amino acid sequence as set forth in SEQ ID NOs:19, 22, 30, 34, 344, 358, 41, 44, 46, 48, 78, 376, 379, 80, 100, 101, 110, 111, 387, 112, 394, 114, 116, 117, 121, 395, 133, 135, 137, 426, 174, 178, 186, 194, 196, 202, 210, 213, 214, 217, 223, 227, 228, 233, 254, 271, 272 or 288, as well as peptides having the above-mentioned amino acid sequences in which 1, 2, or several (e.g. up to 5) amino acids are substituted, deleted, or added, provided the peptides posses cytotoxic T cell inducibility. The present invention also provides drugs for treating or preventing a disease associated with over-expression of the CDH3, EPHA4, ECT2, HIG2, INHBB, KIF20A, TTK and/or URLC10, e.g. cancers containing as an active ingredient one or more of these peptides. The peptides of the present invention find further utility as vaccines.

Description

1 Description PEPTIDE VACCINES FOR CANCERS EXPRESSING TUMOR-ASSOCIATED ANTIGENS This application is a divisional of Australian Application No. 2012261725, the entire contents of which are incorporated herein by reference. Tehnical Field 100013 The present applicaion claims the beneit of U.S. PAisional Application No. 6002,949, filed February 21,2007, the entire disclosure of which is hmreby in corprtcdheremin by ref&nce for all pmposes. [0002] The pmsent invention latest to the field of biological science, more specifically to the field of cancer therapy. In particular, thepxescnt invention plates in novel im mnimogenic peptides thatserve as extremely effective as cancer vaccines, and drags for treating and preventing tumom containing such peptides. Background Art [0003] It has been demonstraed that CD8+ cytotoidc T lymphocyteas (CTs) recognize eptope peptides dived from tumor-assocaied antigens (TAAs) pzsented on MHC class Imolecules, and subsequently lyse the tumor cells. Since the discovery of the MAGE family as the ftat example of TAM, many other TAAs have been discovered using immunological approaches (Boon T.. (1993) Int JCancer 54:177-80.; Boon T. at at, (1996) 1&Ep Med 183: 725-9.; van der Brggen P et al., (1991) Science 254: 1643-7.; BrichardV et al., (1993)J xp Med 178:489-95.; Kawakami Yet al., (1994) J &ip Med 18O:'347-52.). Some of thea now in clinical developmentas targets of imrmmnotheapy. TAAs discovered t datB include MAGE (van der Brvggen P et aL, (1991) Science 254:1643-7.), gp100 (Kawakami Y et al., (1994) JEp Med 180 347-52.), SART (Skichijo S at at, (1998) JExp Med 187:277-88.), and NY-ESO-I (Chm Y.T. et at, (1997) Proc. Nat Acd. Sci. USA, 94: 1914-8.). On the ohe hand, certain gen products demonstrated to be somewhat specifically over-expmssed in tumor cells have been shown to be recognized as targets for inducing cellular immune responses Such gene products include p53 (Umano Y et HL, (2001) Br JCancer, 84:1052-7.), FE2/nen (Tanaka H et al, (2001)Br J Cancer, 84: 94-9.), CEA (Nukaya I et al., (1999) Int. J. Cancer 80, 92-7.) and the likA. [0004] Despite significant progress in basic and clunial research concerning TAAs (Rosenberg SA et al, (1998) Nature Med, 4:321-7.; Mukherji B. et al., (1995) Proc Nati Acad Sci USA, 92: 8078-82.: Hu X et al, (1996) Cancer Res, 56:2479-83.), ouly a veay limited number of candidate TAAs suitable for treatment of cancers are presently available. TAAs that are abundantly expressed in cancer cells, and whose ex pression is restricted to cancer cells, would be prondsing candidates as immuno therapeutic targets.

2 WO 2008/102557 PCT/JPZOOS/000290 [00051 Both HILA-A24 and BLA-A0201 are common HLA alleles in the Japanese and Caucasian populations (Date Y et al., (1996) Tissue Antigens 47: 93-10L.; Kondo A et aL, (1995) J Imunol 155: 4307-12,; Kubo RT et al., (1994) J Inimunol 152: 3913-24. Imanishi et al., Proceeding of the eleventh International Histocompatibility Workshop and Conference Oxford University Press, Oxford, 1065 (1992); Williams F et a, (1997) Tissue Antigen 49: 129-33.). Thus, antigenic peptides of cancers presented by these HlLA alleles may find particular utility in the treatment of cancers among Japanese and Caucasian patients. Further, it is known that the induction of low-affinity CTL in vitro usually results from exposure to high concentrations of peptides, generating a high level of specific peptide/MHC complexes on antigen-presenting cells (APCs), which will effectively activate these CTL (Alexander-Miller et al., (1996) Proc Natd Acad Sci USA 93: 4102-7.). [0006] Recently, HLA class I-binding peptide sequence can be expected using algorithms (Jounal of Immunological Methods, (1995), Vol.185, pp.181-190, J.Immunol., (1994), Vol. 152, pp.163-175, protein science, (2000), Vol.9, pp.1838-1846). However, it is hard to say that the expected epitope peptide can be cut to the size and expressed on the target cell surface with HLA molecule and recognized by CTL. Moreover, the algorithm, for example BIMAS (http://binas.dcrt.nih.gov/cgi-bin/molbio/kertparker_comboforn) (Parker KC, et al, (1994) J ImmunoL;152(1):163-75.; Kuzushima K, et al., (2001) Blood;98(6):1872-81.)) can suggest the HLA molecule-binding peputide, but the suggested peptide is not so rigorous (BachinskyMM, et al., Cancerbnmiun. 2005 Mar 22;5:6.). Thus TAA screening still remains alot of challenges and difficulties. [00071 Recent developments in cDNA microarray technologies have enabled the con struction of comprehensive profiles of gene expression in malignant cells as compared to normal cells (Okabe, H. et al,, (2001) Cancer Res., 61, 2129-37.; Lin YM. et al, (2002) Oncogene, 21;4120-8.; Hasegawa S. et al., (2002) Cancer Res 62:7012-7.). This approach enables a more thorough understanding of the complex nature of cancer cells and the mechanisms of carcinogenesis and facilitates the identification of genes whose expression is deregulated in tumors (Bienz M. et al., (2000) Cell 103, 311-20.). Among the transcripts identified as np-regulated in cancers, CDH3 (GenHank Accession No. NM_001793; SEQ ID Nos.1, 2), EPIA4 (GenBank Accession No. L36645; SEQ ID Nos.3, 4), ECT2 (GenBank Accession No. AY376439; SEQ ID Nos.5, 6), HIG2 (GenBank Accession No. NM_013332; SEQ ID Nos.7, 8)INHIBB (GenBank Accession No. NM_002193; SEQ ID Nos.9, 10), KIF20A (GenBank Accession No. NM005733; SEQ ID Nos.1 1, 12), KNTC2 (GenBank Accession No. AF017790; SEQ ID Nos. 13, 14), TTK (GenBank Accession No. NM_003318; SEQ ID Nos. 15, 16) and URLCI0 (GenBank Accession No. NVL017527; SEQ ID Nos.17, 18) have been 3 WO 20081102557 PCT/JP2001/000290 recently discovered. The entire contents of the references are incorporated by reference berein. These genes are of particular interest to the present inventors, being specifically up-regulated in tumor cells of the various cancer tissues of the cases analyzed (see below). Thus, immunogenic peptides derived from CDH3, EPHA4, ECT2, HIGZ INHBB, KIF20A, KNTC2; TTK and URLCIO may find utility in selectively killing tumor cells that express such antigens. The present invention addresses these and other needs. [0008] Since cytotoxic drugs, such as M-VAC, often cause severe adverse reactions, it is clear that thoughtful selection of novel target molecules on the basis of well characterized mechanisms of action should be very helpful in the development of effective anti-cancer drugs having a minimized risk of side effects. Toward this goal, expression profile analyses were previously performed on various cancers and normal human tissue. Such studies led to the discovery of multiple genes that am specifically over-expressed in cancer (Lin YM, et al., Oncogene. 2002 Jun 13;21:4120-8,; Kitahara 0, et al., Cancer Res. 2001 May 1;61:3544-9.; Suzuli C, et al., Cancer Res. 2003 Nov 1;63:7038-41.; Ashida S, Cancer Res. 2004 Sep 1;64:5963-72.; Ochi K, et al, Int J OncoL 2004 Mar24(3):647-55.; Kaneta Y, et al., Int J Oncol. 2003 Sep;23:681-9L; Obama K, Hepatology. 2005 Jun;41:1339-48.; Kato T, et al., Cancer Res. 2005 Jul 1;65;5638-46.; Kitahara 0, et aL, Neoplasia. 2002 Jul-Aug;4:295-303.; Saito lisaminato A et al., DNA Res 2002, 9: 35-45.). Examples of such genes identified as over-expressed in various cancers include, but are not limited to, CDH3, EPHA4, ECT2, HI02, INHBB, KIP20A, KNTC2, TIK and URLC10. CDH3 has been previously identified as over-expressed in bladder cancer, cervical cancer, cholangin cellular carcinoma, colorectal cancer, endometriosis, gastric cancer, diffuse-type gastric cancer, ron-srnall cell lung cancer (NSCLC), pancreatic cancer, soft tissue tumor and testicular tumor. EPHA4 has been identified in bladder cancer, cervical cancer, cholangincellular carcinoma, endometriosis, diffuse-type gastric cancer, ovarian cancer, pancreatic cancer, prostate cancer and soft tissue tumor. ECF2 has been identified in bladder cancer, breast cancer, cervical cancer, cholangincellular carcinoma, chronic myeloid leukemia (CML), colorectal cancer, esophageal cancer, NSCLC, lymphoma, prostate cancer, renal carcinoma and small cell lung cancer (SCLC). HIG2 has been identified in renal carcinoma and SCLC. INHBB has been identified in cholangincellular carcinoma, esophageal cancer, NSCLC, renal carcinoma, SCLC and soft tissue rumor. KIF20A has been identified in bladder cancer, breast cancer, cholangincellular carcinoma, esophageal cancer, NSCLC, pancreatic cancer, prostate cancer, renal carcinoma and SCLC. KNTC2 has been identified in bladder cancer, breast cancer, cervical cancer, cholangincellular carcinoma, CML, colorectal cancer, esophageal cancer, NSCLC, lymphoma, osteosarcoma, ovarian 4 WO 2098/102557 PCT/JP2008/000290 cancer, pancreatic cancer, prostate cancer, renal carcinoma, SCLC and soft tissue turmor.' TK has been identified in bladder cancer, breast cancer, cervical cancer, cholangincellular carcinoma, CML, colorectal cancer, esophageal cancer, liver cancer, NSCLC, lymphoma, osteosarcoma, prostate cancer, SCLC and soft tissue tumor. URLC10 has been identified in bladder cancer, cervical cancer, cholangincellular carcinoma, esophageal cancer, gastric cancer, NSCLC, osteosarooma, pancreatic cancer and SCLC. [0009] Summary of the Invention The present invention is based in part on the discovery of the applicable targets of immunotherapy. Because TAAs have often no immunogenioity, the discovery of ap propriate targets is of extreme importance. As noted above, CDH3, EPHA4, ECT2, IG22NHBB, KIF20A, KNTC2, ITIK and URLC1O have been identified as up regulated in various cancers. More particularly, these genes were identified using gene expression profiling with a genome-wide cDNA microanray. As discussed above, ex pression of CDH3, EPHA4, ECT2, HIG2, INHBB, KIF20A, KNTC2, TTK and URLC10 has been shown to be specifically up-regulated in various tumor colls, from pancreatic cancer cells to renal cell carcinomas. As described in Table 1, CDH3 ex pression is validly elevated in 26 out of 34 bladder cancer, 17 out of 19 cervical cancer, all of 19 cholangincellular carcinoma, 30 out of 34 colorectal cancer, 20 oui of 21 en dometriosis, 13 out of 20 gastric cancer, 7 out of 8 diffuse-type gastric cancer, 36 out of 37 NSCLC, all of 16 pancreatic cancer, all of 21 soft tissue tumor and all of 10 testicular tumor. [0010] Table 1 further demonstrates that: EPHA4 expression isvalidly elevated in 14 out of 34 bladder cancer, 8 out of 14 cervical cancer, 10 out of 25 cholangincellular carcinoma, 5 out of 15 endometriosis, 5 out of 8 diffuse-type gastric cancer, all of 5 ovarian cancer, all 14 pancreatic cancer, ,20 out of 51 prostate cancer and 14 out of 23 soft tissue tumor. FCT2 expression is validly elevated in 17 out of 19 bladder cancer, 5 out of 12 breast cancer, all of 14 cervical cancer, all of 13 cholangiocellular carcinoma, all of 5 CML, 7 out of 8 colorectal cancer, 12 out of 16 esophageal cancer, 6 out of 16 NSCLC, 8 out of 10 lymphoma, 1 out of 1 pancreatic cancer, 10 out of 13 prostate cancer, 3 out of 6 renal-carcinoma and 12 out of 13 SCLC cancer. HIG2 expression is validly elevated in 19 out of 20 renal cancer and 7 out of 9 soft tissue tumor. JNHBB expression is validly elevated in 10 out of 21 cholangiocellular carcinoma, all of 12 esophageal cancer,- 10 out of 13 NSCLC, 22 out of 24 renal carcinoma, 8 out of 14 SCLC cancer and 45 out of 49 soft tissue tumor. KIP20A expression is validly elevated in all of 31 bladder cancer, 38 out of 61 breast 5 WO 2008/102557 PCT/JP2008/000290 cancer, 10 out of 11 cholangiacellular carcinoma, 7 out of 19 esophageal cancer, 21 out of 22 NSCLC, all of 6 ovarian cancer, 17 out of 36 prostate cancer, 6 out of 11 renal carcinoma and all of 15 SCLC . KNTC2 expression is validly elevated in 30 out of 32 bladder cancer, 47 out of 56 breast cancer, all of 10 cervical cancer, 16 out of 22 cholangioncellular carcinoma, 17 out of 37 CML, 3 out of 10 colorectal cancer, 11 out of 46 esophagus cancer, 15 out of 19 NSCLC, 7 out of 8 lymphoma, 20 out of 24 osteosarcoma, 3 out of 5 ovarian cancer, all of 2 pancreatic cancer, 15 out of 37 prostate cancer, 14 out of 19 renal carcinoma, all of 15 SCLC and 40 out of 59 soft tissue tumor. TTK expression is validly elevated in all of 27 bladder cancer, 25 out of 30 breast cancer, 15 out of 16 cervical cancer, all of 10 cholangiocellular carcinoma, 5 out of 7 CML, 6 out of 10 colorectal cancer, 24 out of 44 esophageal cancer, 8 out of -15 liver cancer, all of 12 NSCLC, all of 6 lymphoma, 13 out of 16 osteoblastoma, 12 out of 17 prostate cancer, all of 15 SCLC and 16 out of 33 soft tissue tumor. URLC10 expression is validly elevated in all of 29 bladder cancer, 15 out of 16 cervical cancer, all of 7 cholangiocellular carcinoma, 7 out of 19 esophageal cancer, all of 3 gastric cancer, 24 out of 27 NSCLC, 15 out of 19 osteosarcoma, 4 out of 5 pancreatic cancer, 33 out of 43 soft tissue tumor. [00111 The present invention is based, at least in part, on the identification of specific epitope peptides of the gene products of these genes (CDH3, EPHA4, ECT2, HIG2, INHBB, KIF20A, KNTC2, TTK and URLC10) which possess the ability to induce cytotoxic T lymphocytes (CTLs) specific to the conesponding molecules. As discussed in detail below, Peripheral Blood Mononuclear Cells (PBMC) of healthy donor were stimulated using HLA-A*2402 or HLA-A*0201 binding candidate peptides derived from CDH3, EPHA4, ECT2, HIG2, IBB, KIF20A, KNTC2, TTK or URLC 10. CTL clones and/or lines were then established with specific cytotoxicity against the HLA-A24 or HLA-A2 positive target cells pulsed with each of the candidate peptides. These results demonstrate that these peptides ar HLA-A24 or HLA-A2 restricted epitope peptides that can induce potent and specific immune responses against cells ex pressing CDH3, EPHA4, ECT2, MG2, INHBB, KIF20A, KNTC2, TTK or URLC10. [0012] Accordingly, the present invention provides methods for treating or preventing a disease associated with the over-expression of CDHI3, EPHA4, ECT2, HI02, INHBB, KIP20A, KNTC2, TTK or URLC10, e.g. cancer. Such methods involve the step of ad ministering to a subject in need thereof a CDH3, EPHA4, ECT2, IG2, INHBB, KIF20A, KNTC2, TfK and/or URLCIO polypeptides of the invention. Administration of such peptide(s) results in the inducdtion of anti-tumor immunity is induced by the ad ministration of these polypeptides. Thus, the present invention provides methods for inducing anti-tumor immunity in a subject, such methods involving the step of admin- -6 istering to a subject in need thereof a CDH3, EPHA4, ECT2, H11G2, NHB, KIF20A, KNTC2, TTK and/or URLCI0 polypeptides of the invention. Administration ofsuch peptide(s) results in the induction of anti-tumor immunity is induced by the administration of these polypeptides. Thus, the present invention provides methods for inducing anti-tumor immunity in a subject, such methods involving the step of administering to the subject the CDH3, EPHA4, ECT2, 1HG2, INHBB, KIF20A, KNTC2, T7K and/or URLC10 polypeptides, as well as pharmacentical compositions for treating or preventing a disease associated with the over-expression of CDH3, EPHA4, ECT2, HIG2, INHBB, KIF20A, KNTC2, ITK and/or URLC10, e.g. cancer, that include the CDH3, EPHA4, ECT2, HIG2, INHBB, KIF20A, KNTC2, TTK and URLCIO polypeptides. Examples of such cancers include, but are not limited to., bladder cancer, breast cancer, cervical cancer, cholangincellular carcinoma, CML, colorectal cancer, endometriosis, esophageal cancer, gastric cancer, diffused type gastric cancer, liver cancer, NSCLC, lymphoma, osteosarcoma, ovarian cancer, pancreatic cancer, prostate cancer, renal carcinoma, SCLC, soft tissue tumor and testicular tumor. [0013] The present invention further provides methods for preventing post-surgery recurrence of the disease mentioned above. Regarding the specific aims and objectives recited above, it will be understood by those skilled in the art that one or more aspects of this invention can meet certain objectives, while one or more other aspects can meet certain other objectives. Each objective may not apply equally, in all its respects, to every aspect of this invention. As such, the objects herein can be viewed in the alternative with respect to any one aspect of this invention. [0014] Additional objects and featurs of the invention will become more fully apparent when the following detailed description is read in conjunction with the accompanying figures and examples. However, it is to be understood that both the foregoing summary of the invention and the following detailed description are of preferred embodiments, and not restrictive of the invention or other alternate embodiments of the invention. In particular, while the invention is described herein with reference to a number of specific embodiments, it will be appreciated that the description is illustrative of the invention and is not constructed as limiting of the invention. Various modifications and applications may occur to those who are skilled in the art, without departing from the spirit and the scope of the invention, as described by the appended claims. Likewise, other objects, features, benefits and advantages of the present invention will be apparent from this summary and certain embodiments described below, and will be readily apparent to those skilled in the art, Such objects, features, benefits and advantages will be apparent from the above in conjunction with the accompanying examples, data, figures and all reasonable inferences to be drawn therefrom, alone or with consideration of the references incorporated herein. [Brief Description of Drawings] [0015] Various aspects and applications of the present invention will become apparent to the skilled artisan upon consideration of the brief description of the figures and the 7 WO I/102557 PCT/JP2,00/000290 detailed description of the present invention and its preferred embodiments which follows: [fig. 1-1Figure 1 depicts the results of the screening of epitope peptides,'bich, in turn, demonstrate that CDH3-A24-10-332 (SEQ ID NO: 34), CDH3-A24-10-470 (SEQ ID NO: 358), CDH3-A24-9-513 (SEQ ID NO: 19), CDH3-A24-9-406 (SEQ ID NO: 22), CDH3-A24-10-807 (SEQ ID NO: 30) and CDH3-A24-10-655 (SEQ ID NO: 344) , show potent IFN-gamma production. "a" depicts the example of negative peptides which could not be detected CThiinducing ability despite possible binding activity with HLA-A*2402. "b" depicts the CTh-inducing ability of CDH3-A24-10-332 (SEQ ID NO: 34). CDH3-A24-10-332 (SEQ ID NO: 34) demonstrated potent IFN-gammfa production as compared to the control by IFN-gamma ELISPOT assay, and CTL line that was established from the positive well #4 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide. "c" depicts the CTL-inducing ability of CDH3-A24-10-470 (SEQ ID NO: 358). CDH3-A24-10-470 (SEQ ID NO: 358) demonstrated potent IFN-gamma production as compared to the control by IPN-gamma ELISPOT assay, and CTL line that was es tablished from the positive well #4 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide. "d" depicts the CTL inducing ability of CDH3-A24-9-513 (SEQ ID NO: 19). CDH3-A24-9-513 (SEQ ID NO: 19) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay. The well #6 shown in boxed wells in left panel demonstrated the specific response against the target cells pulsed with the epitope peptide. Moreover, CT line that was established from the positive well #5 shown in boxed wells in middle panel, demonstrated the specific response against the target cells pulsed with the epitope peptide. "e" depicts the CTL-inducing ability of CDH3-A24-9-406 (SEQ ID NO: 22). CDH3-A24-9-406 (SEQ ID NO: 22) demonstrated potent lFN-gamma production as compared to the control by IFN gamma ELISPOT assay, and CTL line that was established from the positive well #2 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide. [fig. l-2]Figure I depicts the results of the screening of epitope peptides, which, in turn, demonstrate that CDH3-A24-10-332 (SEQ ID NO: 34), CDH3-A24-10-470 (SEQ ID NO: 358), CDH3-A24-9-513 (SEQ ID NO: 19), CDH3-A24-9-406 (SEQ ID NO: 22), CDH3-A24-10-807 (SEQ ID NO: 30) and CDH3-A24-10-655 (SEQ ID NO: 344) show potent IFN-gamma production. N' depicts the CTL-inducing ability of CDH3-A24-l0-807 (SEQ ID NO: 30). CDH3-A24-10-807 (SEQ ID NO: 30) demonstrated potent LFN-gamma production as compared to the control by IFN gamma ELISPOT assay, and CTL line and the clone were established from the positive B WO 2008/102557 PCT/JP200/00290 well #5 shown in boxed wells. The established CTL clone raised against the peptide demonstraed the specific CTL activity against COS7 transfected both full length of CDH3 gene and HLA-A24 molecule (lower right graph). On the other hand, COS7 transfected full length of CDH3 but not BLA-A24 and COS7 transfected HLA-A24 but not full length of CDH3 were prepared for the negative control. The CTL clone showed high specific CTL activity against COS7 that transfected both CDH3 and HLA-A24. "g" depicts the CTL-inducing ability of CDH3-A24-10-655 (SEQ ID NO; 344). CDH3-A24-10-655 (SEQ ID NO; 344) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CTL line and the clone were established from the positive well #1 shown in boxed wells. The es tablished CTL clone raised against the peptide demonstrated the specific CTL activity against COS7 transfected both full length of CDH3 gene and HLA-A24 molecule (lower right graph). On the other hand, COS7 transfected fell length of CDH3 but not HLA-A24 and COS7 transfected HLA-A24 but not full length of CDH3 were prepared for the negative control. The CTL clone showed high specific CTL activity against COS7 that transfected both CDH3 and HLA-A24. [fig.2]Figure 2 depicts the results of the screening of epitope peptides, which, in turn, demonstrate that Epha4-A24-9-453 (SEQ ID NO: 41), Epha4-A24-9-5 (SEQ ID NO: 44), Epha4-A24-9-420 (SEQ ID NO: 48), Epha4-A24-9-869 (SEQ ID NO: 46), Epha4-A24-10-24 (SEQ ID NO: 78) Epha4-A02-9-501 (SEQ ID NO; 376) and Epha4-A02-9-165 (SEQ ID NO: 379) show potent IFN-gamma production. "a" depicts the example of negative peptides which could not be detected CTE-inducing ability despite possible binding activity with HLA. "b" depicts the CTL-inducing ability of Epha4-A24-9-453 (SEQ ID NO: 41). Epha4-A24-9-453 (SEQ ID NO: 41) demonstrated potent IFN-gamma production as compared to the control by WN gamma ELISPOT assay, and CTL line that was established from the positiVe well #3 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide. "c' depicts the CTL-inducing ability of Epha4-A24-9-5 (SEQ ID NO: 44). Epha4-A24-9-5 (SEQ ID NO: 44) demonstrated potent IFN-ganma production as compared to the control by IFN-gamma ELISPOT assay, and CTL line, that was established from the positive well #2 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide. "d" depicts the CTL-inducing ability of Epha4-A24-9-420 (SEQ ID NO: 48). Epha4-A24-9-420 (SEQ ID NO: 48) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay. The well #6 shown in boxed wells in upper panel demonstrated the specific response against the target cells pulsed with the epitope peptide. Moreover CTL line that was established from the positive well #6 shown in boxed wells in middle panel, demonstrated the 9 WO 20G8/102557 PCT/JP2008/000290 specific response against the target cells pulsed with the epitope peptide. "e" depicts the CTL-inducing ability of Epha4-A24-9-869 (SEQ ID NO: 46). Epba4-A24-9-869 (SEQ ID NO: 46) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CITL line that was established from the positive wel #5 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide. '"' depicts the CIL-inducing ability of Epha4-A24-10-24 (SEQ ID NO: 78). Epha4-A24-10-24 (SEQ ID NO: 78) demonstrated potent lFN-gamma production as compared to the control by IPN gamma ELISPOT assay, and CTL line that was established from the positive well #4 shown in boxed wels, demonstrated the specific response against the target cells pulsed with the egitope peptide. "g' depicts the CTL-inducing ability of Epha4-A02-9-501 (SEQ ID NO: 376). Epha4-A02-9-501 (SEQ ID NO: 376) demonstrated potent IFN-gamma production as compared to the control by IPN gamma BLISPOT assay, and CTL line and clone was established from the positive well #8 shown in boxed wells. Cytotoxic activity of the established CTL line against the target cells pulsed with the peptide was measured by Cr-release assay (CRA) (lower graph), and the CTL line had very potent specific cytotoxic activity against the target cells pulsed with the peptides. "h" depicts the CTL-inducing ability of Epha4-A02-9-165 (SEQ ID NO: 379). Epha4-A02-9-165 (SEQ ID NO: 379) demonstrated potent IFN-gamma production as compared to the control by IFN gamma EUSPOT assay, and CTL line was established from the positive well #3 shown in boxed wells. Cytotoxic activity of the established CTL line against target cells pulsed with peptide was measured by Cr-elease assay (CRA) (right graph), and the CL line had very potent specific cytotoxic activity against the target cells pulsed with the peptides. [fig.3]Figure 3 depicts. the results of the screening of epitope peptides, which, in tum, demonstrate that ECT2-A24-9-5 15 (SEQ ID NO: 80), ECT2-A24-10-40 (SEQ ID NO: 100) and ECT2-A24-10-101 (SEQ ID NO: 101) show potent IFN-gamma production. "a" depicts the example of negative peptides which cold not be detected CTL inducing ability despite possible binding activity with HLA. "b" depicts the CTL inducing ability of ECT2-A24-9-515 (SEQ ID NO; 80). ECT2-A24-9-515 (SEQ ID NO: 80) demonstrated potent IFN-gamma production as compared to the contrl by IFN-gamma ELISPOT assay. The well #5 and #7 shown in boxed wells in left panel demonstrated the specific response against the target cells pulsed with the epitope peptide. Moreover, CTL line that was established from the positive well #7 shown in boxed wells in second panel, demonstrated the specific response against the target cells pulsed with the epitope peptide. Cytotoxic activity of the CTL line against cancer cell line, TE6 endogenously expressing ECT2 and HLA-A24 was measured by Cr-release 10 WO 20081102557 pCT/JP2M0S/000290 assay (CRA), and the CTL clone had very potent cytotoxic activity against TE6. On the other hand, the effector cells did not demonstrate the cytotoxic activity of the CTL line against cancer cell line, TE5 expressing only ECT2 was not detected. "c" depicts the CTL-inducing ability of ECT2-A24-10-40 (SEQ ID NO: 100). ECT2-A24-10-40 (SEQ ID NO: 100) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CTL line and the clone were established from the positive well #2 shown in boxed wells. The established CIL clone raised against the peptide demonstrated specific CIL activity against COS7 transfected both full length of ECT2 gene and HLA-A24 molecule. On the other hand, COS7 transfected full length of ECT2 but riot HLA-A24, COS7 transfected HLA-A24 and URLC1O gene as a substitute for full length of ECT2 and COS7 transfected HLA-A24 and pulsed with ECT2-10-101 were prepared for the negative control The CIL clone showed high specific CMT activity against COS7 that transfected both ECT2 and H4LA A24. "d" depicts the CTL-inducing ability of ECT2-A24-10-101 (SEQ ID NO: 101). ECT2-A24-10-101 (SEQ ID NO: 101) demonstrated potent IFN-gammaproduction as compared to the control by IFN-gamma ELISPOT assay, and CIL line were es tablished from the positive well #1 shown in boxed wells. The established CTL line raised against the peptide demonstrated specific CTL activity against COS7 transfected both fnll length of ECT2 gene and HLA-A24 molecule. COS7 transfected full length of ECT2 but not HLA-A24, COS7 transfected HLA-A24 and URLC 10 gene as substitute for full length of ECT2 and COS7 transfected HLA-A24 and pulsed with ECT2-10-40 were prepared for the negative control. The CTL clone showed high specific CTL activity against COS7 that transfected both ECT2 and HLA-A24. [fig.4- iFIgure 4 depicts the results of the screening of epitope peptides, which, in turn, demonstrate that HIG2-A24-9-19 (SEQ ID NO: 110), HIG2-A24-9-22(SEQ D NO: 111), HIG2-A24-9-8-(SEQ M NO: 387), IG2-A24-10-7 (SEQ ID NO: 112), HI02-A24-10-18 (SEQ ID NO: 394), HIG2-A02-9-15 (SEQ ID NO: 116), HG2-A02-9-4 (SEQ ID NO: 117) and HIG2-A02-10-8 (SEQ ID NO: 121) show potent IFN-gamma production. "a" depicts the example of negative peptides which could not be detected CTL-inducing ability despite possible binding activity with HLA. "b" depicts the CiT-inducing ability of fHG2-A24-9-19 (SEQ ID NO: 110). HIG2-A24-9-19 (SEQ ID NO: 110) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CTL line, that was es tablished from the positive well #6 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide. "c" depicts the CTL inducing ability of H102-A24-9-22 (SEQ ID NO: 111). HIG2-A24-9-22 (SEQ ID NO: 111) demonstrated potent IFN-gamma production as compared to the control by IFN gamma ELISPOT assay, and CTL line and clone, that was established from the 11 WO 200&1102557 PCT/JP200/000290 positive wefl #7 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide. "d" depicts the CTL-inducing ability of HIG2-A24-9-8 (SEQ ID NO: 387). 1IG02-A24-9-8 (SEQ ID NO: 387) demonstrated potent IFN-ganma production as compared to the control by IFN-gamma EUSPOT assay, and CTL line and clone, that were established from the positive well #5 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide. "e" depicts the CTL-inducing ability of HIG2-A02-9-8 (SEQ IID NO: 114). H1G2-A02-9-8 (SEQ ID NO: 114) demonstrated potent ]FN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CTL line was established from the positive well #10 shown in boxed wells. The established CTL line raised against the peptide demonstrate. specific CTL activity against 293T transfected both full length of HIG2 gene and HLA-AO2 molecule. 293T -transfected full length of HIG2 but not HLA-A02, 293Ts transfected HLA-A02 and FoxP3 gene as substitute dor full length of IG2 and 293Ts transfected HLA-A02 and pulsed with HIG2-9-15 were prepared for the negative control. The CTL line showed high specific CTL activity against 293T that transfected both HIG2 and HLA-A02. [fig.4-2JFigure 4 depicts the results of the screening of epitope peptides, which, in tUrn, demonstrate that HIG2-A24-9-19 (SEQ ID NO: 110), IIG2-A24-9-22 (SEQ ID NO: 111), HIG2-A24-9-8 (SEQ ID NO: 387), HIG2-A24-10-7 (SEQ ID NO: 112), HIG2-A24-10-18 (SEQ ID NO: 394), IG2-A02-9-15 (SEQ ID NO: 116), -HG2-A02-9-4 (SEQ ID NO: 117) and HIG2-A02-10-8 (SEQ ID NO: 121) show potent FN-gamma production. "f Pdepicts the CTL-indacing ability of HIG2-A24-10-7 (SEQ ID NO: 112); I02-A24-10-7 (SEQ ID NO: 112) demonstrated potent FN-ganmna production as compared to the control by IFN-gamma ELISPOT assay, and CTL lines or clone, that were established from the positive well #1 and #7 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide. "g" depicts the CTL-inducing ability of HIG2-A24-10-18 (SEQ ID NO: 394). H102-A24-10-18 (SEQ ID NO: 394) demonstrated potent IFN-gamma production as compared to the control by IFN gamma ELISPOT assay, and CTL line and clone, that were established from the positive well #7 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide. "h" depicts the CTL-inducing ability of HI02-AO2-9-15 (SEQ ID NO: 116). HIG2-A02-9-15 (SEQ ID NO: 116) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CTL line was established from the positive well#10 shown in boxed wells. The established CIL line raised against the peptide demonstrated specific CTL activity against COS7 transfected both full length of HG2 gene and HLA-AOZ molecule. COS7 transfected full length of HG2 but not HLA-A02 and COS7s transfected HLA- WO 200/102557 PCT/JP2008/000290 A02 and pulsed with 1G2-9-8 peputide were prepared for the negative control. The CTh line showed high specific CTL activity against COS7 that transfected both HIG2 and BLA-A02. [fig.4-3JFigurs 4 depicts the results of the screening of epitope peptides, which, in turn, demonstrate that HIG2-A24-9-19 (SEQ ID NO: 110), HIG2-A24-9-22 (SEQ ID NO: 111), IG2-A24-9-8 (SEQ ID. NO: 387), IG2-A24-10-7 (SEQ ID NO: 112), HIG2-A24-10-18 (SEQ ID NO: 394), HIG2-A02-9-15 (SEQ ID NO: 116), HIG2-A02-9-4 (SEQ ID NO: 117) aid I02-A02-10-8 (SEQ ID NO: 121) show potent IFN-ganmaproduction. " depicts the CTL-inducing ability of HIG2-A02-9-4 (SEQ ID NO: 117). HIG2-A02-9-4 (SEQ ID NO: 117) demonstrated potent IFN gamma production as compared to the control by IFN-gamma ELISPOT assay, and CTL line and clone were established from the positive well #10 shown in boxed wells. The established CTL line raised against the peptide demonstrated specific CTL activity against COS7 transfected both fll length of I02 gene and HLA-A02 molecule (middle graph). Also, COS7 transfected full length of HIG2 but not HLA-A02, COS7s transfected HLA-A02 and TTlC gene as substitute for full length of HIG2 and COS7s transfected HLA-A02 and pulsed with H02-9-8 were prepared for the negative control. Cytotoxic activity of the CTL clone against 293T, transfected both full length of IG2 gene and HLA-A02 molecule, and cancer cell line, Cald-1 endogenously ex pressing -HG2 and HLA-A02 was measured by Cr-release assay (CRA) (lower graphs), and the CTL clone had very potent cytotaxic activity against the transfectant with both of HIG2 gene and HLA-A02, and Caki-1. On the other hand, the effector cells did not demonstrate the cytotoxic activity of the CTL line against 293T, transfected only HIG2 or only HLA-A02, and cancer cell line, A498 expressing only HIG2 was not detected. 'j" depicts the CTL-inducing ability of HG2-A02-10- (SEQ ID NO: 121). HIG2-A02-10-8 (SEQ ID NO: 121) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CT line, that was established from thepositive well #9 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide. [fig.5-1]Figure 5 depicts the results of the screening of epitope peptides, which, in turn, demonstrate that INHBB-A24-9-180 (SEQ ID NO: 395), INHBB-A24-10-180 (SEQ ID NO: 133), INHBB-A24-10-305 (SEQ ID NO: 135), INHBB-A24-l0-7 (SEQ ID NO: 137) and IBB-A24-10-212 (SEQ ID NO: 426) show potent JFN-gnimma production. "a" depicts the example of negative peptides which could not be detected CTL-inducing ability despite possible binding activity with HLA. "b" depicts the CTL inducing ability of INHBB-A24-9-180 (SEQ ID NO: 395). INHEB-A24-9-1 80 (SEQ ID NO: 395) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CTL line and clone was established from the 13 WO 2008/102557 PCT/JP2008/000290 positive well #7 shown in boxed wells. Cytotoxic activity of the established CTL clone against tumor cells, Miapaca2 expressing both of INHBB and HLA-A02 was measured by Cr-release assay (CRA), and the effector cells showed high specific cytotoxic activity against Miapaca2. On the other hand, it did not show significant specific cytotoxic activity against Caki-1 expressing INHBB but not HLA-A02. "c" depicts the CTL-inducing ability of INHBB-A24-10-180 (SEQ ID NO: 133). INHBB-A24-10-1 80 (SEQ ID NO: 133) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CTL line was established from the positive well #3 shown in boxed wells. The established CTL line raised against the peptide demonstrated high specific CTL activity against 293T transfected both of full length of INHBB gene and BLA-A24 molecule. Also, 293T transfected full length of INHB but not HLA-A24 and 293Ts transfected HILA-A24 andpulsed with INHEBB 10-305 peptide were prepared for the negative control. [fig.5-2]Figure 5 depicts the results of the screening of epitope peptides, which, in turn, demonstrate that INHBB-A24-9-180 (SEQ ID NO: 395), INHBB-A24-10-180 (SEQ ID NO: 133), INHBB-A24-10-305 (SEQ ID NO: 135), IHBB-A24-10-7 (SEQ ID NO: 137) and INHBB-A24-10-212 (SEQ ID NO: 426) show potent IFN-gamma production. "d" depicts the CTL-inducing ability of INBB-A24-10-305 (SEQ ID NO: 135). ]NBB-A24-10-305 (SEQ ID NO: 135) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CTL line and clone were established from the positive well #2 shown in boxed wells. The es tablished CTL clone raised against the peptide demonstrated high specific CTL activity against 293T transfected both full length of INHBB gene and HLA-A24 molecule. Also, 293T transfected full length of INHBB but HLA-A24 and 293Ts transfected HLA-A24 and pulsed with INHBB-10-180 peptide were prepared for the negative controL "e" depicts the CTL-inducing ability of INHBB-A24-10-7 (SEQ ID) NO: 137)). INHBB-A24-10-7 (SEQ ID NO: 137) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CTL lines were es tablished from the positive well #8 shown in boxed wells in upper panel and #2 shown in boxed wells in lower panel. The CTL line from #8 well demonstrated specific CTL activity against 293T transfected both full length of INMB gene and HLA-A24 molecule. Also, 293T transfected full length of INHBB but not HLA-A24 and 293Ts transfected HLA-A24 and pulsed with INHBB-l0-40 peptide were prepared for the negative control. "f depicts the CTL-inducing ability of INHBB-A24-10-212 (SEQ ID NO: 426). INHBB-A24- 10-212 (SEQ ID NO: 426) demonstrated potent IFN-gaznma production as compared to the control by IFN-gamma ELISPOT assay, and CTL line, that was established from the positive well #1 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide.

14 WO 2008/102557 PCT/JP2008/000290 [fig.6-1]Figore 6 depicts the results of the screening of epitope peptides, which, in turn, demonstrate that IGF20A-A24.-10-304 (SEQ ID NO; 186), KIF20A-A24-9-383 (SEQ ID NO: 178), KIP20A-A24-10-66 (SEQ ID NO: 194) and KF20A-A24-9-305 (SEQ ID NO: 174) show potent IFN-gamrnma production. "a" depicts the example of negative peptides which could not be detected CM-inducing ability despite possible binding activity with HLA. "b" depicts the CTL-inducing ability of CF20A-A24-10-304 (SEQ ID NO: 1S6). KIF20A-A24-10-304 (SEQ ID NO: 186) demonstrated potent LFN gamma production as compared to the control by IFN-gamma ELISPOT assay. The well #5 shown in boxed wells in lower right panel demonstrated the specific response against the target cells pulsed with the epitope peptide. Moreover, CTL line and clone, that were established from the positive well #5 shown in boxed wells in upper left panel, also demonstrated the specific response against the target cells pulsed with the epitope peptide. The established CTL clone raised against the peptide demonstrated specific CTL activity against 24-LCL transfected full length of KF20A gene. Also, A24-LCL transfected mock vector was prepared for the negative control. Cytotoxic activity of the CTL clone against tumor cells, Miapaca2 expressing both of KIF20A and HLA-A24 was measured by Cr-release assay (CRA), and the CTL clone had very potent specific cytotoxic activity against Miapaca2 (lower right graph). On the other hand, it did not show significant specific cytotoxic activity against PK59 expressing KIP20A but not HLA-A24. "c" depicts the CTL-inducing ability of KIF20A-A24-9-383 (SEQ ID NO: 178). KTF20A-A24-9-383 (SEQ ID NO: 178) demonstrated potent IFN-gamma production as compared to the control by IFN gamma ELISPOT assay. The well #3 and 4 shown in boxed wells in right panel demonstrated the specific response against the target cells pulsed with the epitope peptide. Moreover, CTL line, that was established from the positive well #3 shown in boxed wells in left panel, also demonstrated the specific response against the target cells pulsed with the epitope peptide. The established CTL line demonstrated high specific CTL activity against COS7 transfected both full length of KIF20A gene and HLA-A24 molecule. Also, COS7 transfected full length of KCF20A but not HLA-A24 and COS7s transfected HLA-A24 and pulsed with KIF20A-9-621 peptide were prepared for the negative control. [fig.6-2JFigure 6 depicts the results of the screening of epitope peptides, which, in turn, demonstrate that KIF20A-A24-10-304 (SEQ IID NO: 186), KIF20A-A24-9-383 (SEQ ID NO: 178), KlF20A-A24-10-66 (SEQ ID NO: 194) and KIF20A-A24-9-305 (SEQ ID NO: 174) show potent IFN-gamma production. "d" depicts the CTL-inducing ability of KIF20A-A24-10-66 (SEQ ID NO: 194). KIF2OA-A24-10-66 (SEQ ID NO: 194) demonstrated potent IFN-ganma production as compared to the control by IFN gamma ELISPOT assay, and CTL lines, that were established from the positive well CINRmrlDCOAAMW65IW C-M19/OLI - 15 #6 shown in boxed wells in upper left panel and #3 shown in boxed wells in lower middle panel demonstrated the specific response against the target cells pulsed with the epitope peptide. Moreover, CTL clone selected from CIL line from #6 well by limiting dilution demonstrated specific CT activity against the target cells. The established CTL cone showed specific CTL activity against COS7 transfected both full length of KIF20A gene and HLA-A24 molecule. Also, COS7 transfected full length of KIF20A but not HLA-A24, COS7s transfected HLA-A24 and URLC10 gene as substitute for full length of KIF20A and COS7 transfected HLA-A24 and pulsed with KIF20A-10-308 peptide were prepared for the negative control. "e" depicts the CTL-inducing ability ofKIF20A-A24-9-305 (SEQ ID NO: 174). KIF2OA-A24-9-305 (SEQ ID NO: 174) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CTL lines, that were established from the positive well #2 shown in boxed wells in upper left panel and #6 shown in boxed wells in lower middle panel, demonstrated the specific response against the target cells pulsed with the epitope peptide. Moreover, CTL clone selected from CTL line from #2 well by limiting dilution demonstrated specific CTL activity against the target cells. Cytotoxic activity of the CTL clone against tumor cells, PK45P expressing both of KIF20A and HLA-A24 was measured by Cr-rease assay (CRA), and the CTL clone had very potent cytotoxic activity against PK45P. On the other hand, it did not show significant specific cytotoxic activity against PK59 expressing KIF2OA but not HLA-A24. [Fig. 7-]]Figure 7 depicts the results of the screening of epitope peptides, which, in turn, demonstrate that KNTC2-A24-9-309 (SEQ ID NO: 196), KNTC2-A24-9-124 (SEQ ID NO: 202), KNTC2-A24-9-154 (SEQ ID NO: 210) KNTC2-A24-9-150 (SEQ ID NO: 213), KNTC2-A24-10-452 (SEQ ID NO: 214), KNTC2-A24-10-227 (SEQ ID NO: 217) and KNTC2-A24-10-273 (SEQ ID NO: 223) show potent IFN-gamma production. "a" depicts the example of negative peptides which could not be detected CTL-inducing ability despite possible binding activity with HLA. "b" depicts the CTL-inducing ability of KNTC2-A24 9-309 (SEQ ID NO: 196). KNTC2-A24-9-309 (SEQ ID NO: 196) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CTL line, that was established from the positive well #8 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide.. "c" depicts the CTL-inducing ability of KNTC2-A24-9-124 (SEQ ID NO: 202). KNTC2 A24-9-124 (SEQ ID NO: 202) demonstrated potent lFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CIL line, that was established from the positive well #5 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide. "d" depicts the CTL-inducing ability of - 16 KNTC2-A24-9-154 (SEQ ID NO: 210). KIF20A-A24-9-154 (SEQ ID NO: 210) demonstrated potent IN-gammaproduction as compared to the control by IFN-gamma ELISPOT assay, and CTL line and clone, that were established from the positive well #5 shown in boxed wells demonstrated the specific response against the target cells pulsed with the epitope peptide. "e"l depicts the CTL-inducing ability of KNTC2-A24-9-150 (SEQ ID NO: 213). KNTC2-A24-9-150 (SEQ ID NO: 213) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CTL line, that was established from the positive well #7 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide. [Fig. 7-2]Figure 7 depicts the results of the screening of epitope peptides, which, in turn, demonstrate that KNTC2-A24-9-309 (SEQ ID NO: 196), KNTC2-A24-9-124 (SEQ ID NO: 202) KNTC2-A24-9-154 (SEQ ID NO: 210) KNTC2-A24-9-150 (SEQ ID NO: 213), KNTC2-A24-10-452 (SEQ ID NO: 214), KNTC2-A24-10-227 (SEQ ID NO: 217) and KNTC2-A24-10-273 (SEQ ID NO: 223) show potent IFN-gamma production. "' depicts the CTL-inducing ability of KNTC2-A24-10-452 (SEQ ID NO: 214). KNTC2-A24-10-452 (SEQ ID NO: 214) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CTL lines and clone, that were established from the positive well #4 shown in boxed wells in upper left panel and #5 shown in boxed wells in middle panel, demonstrated the specific response against the target cells pulsed with the epitope peptide. Moreover, CTL clone selected from CTL line from #5 well by limiting dilution demonstrated specific CTL activity against the target cells. The established CTL line from #4 well showed specific CTL activity against HEK293 transfected both full length of KNTC2 gene and HLA-A24 molecule. Also, HEK293 transfected full length of KNTC2 but not HLA-A24, HEK293 transfected HLA-A24 but full length of KNTC2 and HEK293 transfected HLA-A24 pulsed with KNTC-9-309 peptide were prepared for the negative control. "g" depicts the CTL-inducing ability of KNTC2-A24-10-227 (SEQ ID NO: 217). KNTC2-A24-10-227 (SEQ ID NO: 217) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CTL line, that was established from the positive well #1 shown in boxed well s, demonstrated the specific response against the target cells pulsed with the epitope peptide. "h" depicts the CTL inducing ability of KNTC2-A24-10-273 (SEQ ID NO: 223). KNTC2-A24-10-273 (SEQ ID NO: 223) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CTL line, that was established from the positive well #8 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide. [Fig. 8-1)Figure 8 depicts the results of the screening of epitope peptides, which, in turn, 17 WO 2008/102557 PCT/JPZOS/000290 demonstrate that TTK-A02-9-462 (SEQ ID NO: 227), TTK-A2-9-719 (SEQ ID NO: 233), TTK-A02-9-547 (SEQ ID NO: 228) and TTK-A02-10-462 (SEQ ID NO: 254), show potent IFN-gamrna production. "a" depicts the example of negative peptides which could not be detected CTL-inducing ability despite possible binding activity with ELA. "b" depicts the CTL-inducing ability of TTK-A02-9-462 (SEQ ID NO: 227). TTK-A02-9-462 (SEQ ID NO: 227) demonstrated potent IFN-gamma production as compared to the control by IPN-gamma ELISPOT assay, and CTL line and two clones, that were established from the positive well #4 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide. The established CTL clone showed high specific CTL activity against COS7 transfected both full length of TTK gene and HLA-A02 molecule. Also, COS7 transfected fall length of TTK but not HLA-A02, COS7s transfected HLA-A02 but not full length of TTK and COS7s transfected HLA-A02 pulsed with TTK-9-547 peptide were prepared for the negative controL "c" depicts the CTL-inducing ability of TTK A02-9-719 (SEQ ID NO: 233). TTK-A02-9-719 (SEQ I) NO: 233) demonstrated potent TN-gamma production as 'compared to the control by IEN-gamma ELISPOT assay, and CT line and clones were established from the positive well #1 shown in boxed wells. The established CTL line showed high specific CTL activity against COS7 transfected both fall length of TTK gene and HLA-A02 molecule. Also, COS7 fransfected full length of TTK but not HILA-A02 and COS7s transfected HLA-A02 and HIG2 gene as substitute for full length of TTK were prepared for the negative control. [fig. 8-2]Figure 8 depicts the results of the screening of epitope peptides, which, in turn, demonstrate that TTK-A02-9-462 (SEQ ID NO: 227), TTK-A02-9-719 (SEQ ID NO: 233), TTK-A02-9-547 (SEQ ID NO: .228) and TTK-A02-10-462 (SEQ ID NO: 254), show potent IFN-gamma production. "d" depicts the CTL-inducing ability of TTK A02-9-547 (SEQ ID NO: 228). TTK-A02-9-547 (SEQ ID NO: 228) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CTL line and clones were established from the positive well #2 shown in boxed wells. The established CTL line showed specific CTL activity against COS7 transfected both full length of TTK gene and HLA-A02 molecule. Also, COS7 transfected full length of TTK but not HLA-A02, COS7s transfected LA-A02 but not full length of TTK and COS7s transfected HLA-A02 and pulsed with TTK- 10-462 were prepared for the negative contrl. [fig.8-3]Figure 8 depicts the results of the screening of epitope peptides, which, in turn, demonstrate that TTK-A02-9-462 (SEQ ID NO: 227), TTK-A02-9-719 (SEQ ID NO: 233), TTK-A02-9-547 (SEQ ID NO: 228) and TTK-A02-10-462 (SEQ ID NO: 254), show potent IFN-gamma production. "e" depicts the CL-inducing ability of TTK A02-10-462 (SEQ ID NO: 254). TTK-A02-10-462 (SEQ ID NO: 254) demonstrated 18 WO 20081102557 PCT/JP2008/000290 potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CTL line and three clones were established from the positive well #8 shown in boxed wells. The established CTL clone showed specific CTL activity against COS7 transfected both full length of TrK gene and HLA-A02 molecule. Also, COS7 transfected full length of TTK but not HLA-A02, COS7s transfected HLA-A02 but not fulilength of TTK and COS7s transfected HLA-A02 and pulsed with TTK-9-547 peptide were prepared for the negative control. [fig.9-1]Figure 9 depicts the results of the screening of epitope peptides, which, in turn, demonstrate that URLC1O-A02-9-206 (SEQ I) NO: 271), URLCJO-A02-9-212 (SEQ ID NO: 272) and URLCIO-A02-1O-211 (SEQ ID NO: 288) show potent iPN-gamma production. "a" depicts the exhmple-of negative peptides Which could not be detected CTL-inducing ability despite possible binding activity with HLA. "b" depicts the CTL inducing ability of URLC10 -A02-9-206 (SEQ ID NO: 271). URLC 10-A02-9-206 (SEQ ID NO: 271) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and CTL line, that was established from the positive well #7 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide. "c" depicts the CTL-inducing ability of LIRLC1O-A02-9-212 (SEQ ID NO: 272). URLC10-A02-9-212 (SEQ ID NO: 272) demonstrated potent IFN-gamma production as compared to the control by IFN gamma ELISPOT assay, and CIL line, that was established from the positive well #3 shown in boxed wells, demonstrated the specific response against the target cells pulsed with the epitope peptide. "d" depicts the CTL-inducing ability of URLC1O-A02-10-211 (SEQ ID NO: 288). URLCIO-A02,10-211 (SEQ ID NO: 288) demonstrated potent JFN-gamma production as compared to the control by IFN gamma ELISPOT assay, and CIL line and clones, that were established from the positive well #5 shown in boxed wells.: [fIg.9-2]Figure 9 depicts the results of the screening of epitope peptides, which, in turn, demonstrate that URLCW0-A02-9-206 (SEQ ID N& 271), URLCIO-A02,9-212 (SEQ ID NO: 272) and URLC1O-A02-10-211 (SEQ ID NO: 288) show potent lEN-gamma production. " Continuation of d" The established CTL clone showed high specific CTL activity against COS7, Helk293 and 293T which were transfected both ful length of URLC10 gene and HLA-A02 molecule. Also, COS7, Hek293 or293T which were transfected full length of URLC10 but not HLA-A02 and COS7s, Hek293s or 293Ts, which were transfected HLA-A02 and pulsed with URLC10-10-64, were prepared for the negative control. In this drawings, "+" means the peptide pulsed target, "-" means the no peptide pulsed target, "R" means Responder, "S" means Stimulator, "E" means Effector, and "T" means Target. [0016] Detijed Description of the Invention -19 WO 2008/102557 PCT/JP200S/000290 The words "a", "an", and "the" as used herein mean "at least one" unless otherwise spe cificaly indicated. Unless otherwise defined, all technical and scientific terms used herein have the same meaning as commonly understood by one of ordinary skill in the art to which this invention belongs. [00171 The present invention is based in part on the discovery of applicable targets of im munotherapy. Identification of new TAAs, particularly those that induce potent and specific anti-tumor kimune responses, warrants further development of the clinical -ap plication of the peptide vaccination strategy in various types of cancer (Boon T et aL, (1996) J Exp Med 183: 725-9.; van der Bruggen P et al., (1991) Science 254: 1643-7.; Brichard V et al., (1993) J Exp Med 178: 489-95.;.Kawakami Y et aL, (1994) J Exp Med 180: 347-52,; Shichijo S et al., (1998) J Exp Med 187:277-88.; Chen YT et al., (1997) Proc.Natl.Acd. ScLiUSA, 94: 1914-8.; Harris CC, (1996) J Natl Cancer Inst 88:1442-55.; Butteifield LH et al, (1999) Cancer Res 59:3134-42.; Vissers IL et al., (1999) Cancer Res 59; 5554-9.; van der Burg SH et al., (1996) J. hnmunol 156:3308-14.; Tanaka F et al., (1997) Cancer Res 57:4465-8.; Fujie T et aL, (1999) Int J Cancer 80:169-72.; Kikuchi M et al., (1999) Int J Cancer 81: 459-66.; Oiso M et al., (1999) Int I Cancer 81:387-94.). Because TAAs have often no immunogenicity, discovery of fitting targets is extremely important issue. [00181 As noted above, CDH3 (GenBank Accession No. NM-0I 793; SEQ ID Nos. 1, 2), EPHA4 (GenBank Accession No. L36645; SEQ ID Nos.3, 4), ECT2 (GenBank Accession No. AY376439; SEQ ID Nos.5, 6), 11102 (GenBank Accession No. NMV013332; SEQ ID Nos.7, 8) INHBB (GenBank Accession No. NM 002193; SEQ ID Nos.9, 10), KIF2OA (GenBank Accession No. NMV005733; SEQ ID Nos. 11, 12), CKNTC2 (GenBank Accession No. AF017790; SEQ ID Nos. 13, 14), TTK (GenBank Accession No. NM_003318; SEQ ID Nos.15, 16) and URLCl0 (GenBank Accession No. NM_017527; SEQ ID Nos.17, 18) were previously identified as over-expressed in various cancers using cDNA microarray technologies. [0019) In the present invention, peptides derived from CDH3, EPHA4, ECT2, HIG2, INHBB, KEF20A, KNTC2, TTK or URLC10 are shown to be TAA epitopes restricted by HLA-A24 and HLA-A2, an HLA allele commonly found in the Japanese and Caucasian populations. Specifically, using their binding affinities to ILA-A24 or HLA-A2, candidates of HLA-A24 or HLA-A2 binding peptides derived from CDH3, EPHA4, ECT2, H102, 11HB, KIF20A, KNTC2, TTK or URLC10 were identified. After the in vitro stimulation of T-cells by dendritic cells (DCs) loaded with these 20 WO 2001/102557 PCTJP2008/000290 peptides, CTLs were successfully established using the following peptides. CDH3-A24-9-513 (SEQ ID NO: 19), CDH3-A24-9-406 (SEQ ID NO: 22), CDH3-A24-10-807 (SEQ ID NO: 30), CDH3-A24-10-332 (SEQ ID NO: 34), CDH3-A24-10-655 (SEQ ID NO: 344), CDH3-A24-10-470 (SEQ ID NO: 358), EpbA4-A24-9-453 (SEQ ID NO: 41), EphA4-A24-9-5 (SEQ ID NO: 44), EphA4-A24-9-869 (SEQ ID NO: 46), EphA4-A24-9-420 -(SEQ ID NO; 48),. EphA4-A24-l0-24 (SEQ ID NO: 78), EphA4-A02-9-501 (SEQ ID NO; 376), EphA4-AD2-9-165 (SEQ ID NO; 379), ECT2-A24-9-515 (SEQ ID NO: 80), ECT2-A24-10-40 (SEQ ID NO: 100), ECT2-A24-10-101 (SEQ tD NO: 101), HIIG2-A24-9-19 (SEQ ID NO: 110), HIG2-A24-9-22 (SEQ ID NO: 111), HIG2-A24-9-8 (SEQ ID NO: 387), H1G2-A24-10-7 (SEQ ID NO: 112), HIG2-A24-10-18 (SEQ ]D NO: 394), HIG2-A02-9-8 (SEQ ID NO: 114), HIG2-A02-9-15 (SEQ ID NO: 116), HIG2-A02-9-4 (SEQ ID NO: 117), HIG2-A02-10-8 (SEQ ID NO: 121), INHBB-A24-9-180 (SEQ ID NO: 395), INHBB-A24-1Or-18 (SEQ ID NO: 133), INHBB-A24-10-305 (SEQ ID NO: 135), INHBB-A24-10-7 (SEQ ID NQ: 137), INHBB-A24-10-212 (SEQ ID NO: 426), KIF20A-A24-9-305 (SEQ ID NO: 174), IF2OA-A24-9-383 (SEQ ID NO: 173), KIF20A-A24-10-304 (SEQ ID NO: 186), KIF20A-A24-10-66 (SEQ ID NO; 194), KNTC2-A24-9-309 (SEQ ID NO: 196), KNTC2-A24-9-124 (SEQ ID NO: 202), KNTC2-A24-9-154 (SEQ ID NO; 210), CNIU'ljfl1WCCiAEA55.~LiDD~c/DI 1 -21 KNTC2-A24-9-150 (SEQ ID NO: 213), KNTC2-A24-10-452 (SEQ ID NO: 214), KNTC2-A24-10-227 (SEQ ID NO: 217), KNTC2-A24-10-273 (SEQ ID NO: 223), TTK-A02-9-462 (SEQ ID NO: 227), TTK-A02-9-547 (SEQ ID NO: 228), TTK-A02-9-719 (SEQ ID NO: 233), TTK-A02-10-462 (SEQ ID NO: 254), URLC-A02-9-206 (SEQ ID NO: 271), URLC-A02-9-212 (SEQ ID NO: 272) and URLC-A02-10-211 (SEQ ID NO: 288) [0020]These peptides are epitope peptides of each TAA restricted by HLA-A24 or HLA A2. Since these antigens are over-expressed in most cancers and are associated with tumor cell proliferation, they find utility as inimunotherapeutic targets against cancers. Exemplary cancers include, but are not limited to, bladder cancer, breast cancer, cervical cancer, cholangincellular carcinoma, CML, colorectal cancer, endometriosis, esophageal cancer, gastric cancer, diffused type gastric cancer, liver CANCER, NSCLC, lymphoma, osteosarcoma, ovarian cancer, pancreatic cancer, prostate cancer, renal carcinoma, SCLC, soft tissue tumor and testicular tumor. [002 1]Accordingly, the present invention further provides methods of treating or preventing a disease associated with the over-expression of CDH3, EPHA4, ECT2, HIG2, INHBB, KIF20A, KNTC2, TTK and/or URLC10, e.g. cancers in a subject, such methods including the steps of administering to the subject an immunogenic peptide of less than about 40 amino acids, often less than about 20 amino acids, usually less than about 15 amino acids and having the amino acid sequence of SEQ ID NOs: 19, 22, 30, 34, 344, 358, 41, 44, 46,48, 78, 376,379, 80, 100,101, 110, 111, 387, 112,394, 114, 116,117, 121, 395, 133, 135, 137, 426,174, 178, 186, 194, 196,202,210, 213,214, 217, 223,227, 228, 233, 254, 271, 272 or 288. [0022jAltematively, the immunogenic peptide may have an amino acid sequence as set forth in SEQ ID NOs: 19, 22, 30, 34, 344, 358, 41, 44, 46, 48, 78, 376, 379, 80, 100, 101, 110, 111, 387, 112, 394, 114, 116, 117, 121, 395, 133, 135,137, 426, 174, 178, 186, 194, 196, 202, 210, 213, 214, 217, 223, 227,228, 233, 254, 271, 272 or 288 in which 1, 2, or several (e.g., up to 5) amino acids are substituted, deleted or added, provided the resulting variant peptide retains the immunogenic activity (i.e., the ability to induce CTLs specific to cells expressing CDH3, EPHA4, ECT2, HIG2, INHBB, KIF20A, KNTC2, TTK and/or URLC 10, e.g. cancers). [0023]The number of residues to be substituted, deleted, or added is generally 5 amino acids or less, preferably 4 amino acids or less, more preferably 3 amino acids or less, cCAMMylKDWE55_..I.DDC.WD.... -22 even more preferably one or two amino acids. The cancers contemplated include, but are not limited to, bladder cancer, breast cancer, cervical cancer, cholangincellular carcinoma, CML, colorectal cancer, endometriosis, esophageal cancer, gastric cancer, diffused type gastric cancer, liver cancer, NSCLC, lymphoma, osteosarcoma, ovarian cancer, pancreatic cancer, prostate cancer, renal carcinoma, SCLC, soft tissue tumor and testicular tumor. Furthermore the present invention provides methods for preventing post-surgery recurrence of these diseases mentioned above. [0024] Variant peptides (i.e., peptides having an amino acid sequence modified by substituting, deleting, or adding one, two or several amino acid residues to an original amino acid sequence) are known to retain the original biological activity (Mark DF et al., (1984) Proc Natl Acad Sci USA 81: 5662--6; Zoller MJ and Smith M, (1982) Nucleic Acids Res 10:6487-500.; Dalbadie-McFarland G et al., (1982) Proc Nail Acad Sci USA 79: 6409 13.). In the context of the present invention, it is preferable that the amino acid modification results in conservation of the properties of the original amino acid side-chain (a process known as conservative amino acid substitution). Examples of properties of amino acid side chains include hydrophobic amino acids (A, I, L, M, F, P, W, Y, V), hydrophilic amino acids (R, D, N, C, E, Q, G, H, K, S, T), and side chains having the following functional groups or characteristics in common: an aliphatic side-chain (G, A, V, L, I, P); a hydroxyl group containing side-chain (S, T, Y); a sulfur atom containing side chain (C, M); a carboxylic acid and aide containing side-chain (D, N, E, Q); a base containing side-chain (R, K, H); and an aromatic containing side-chain (H, F, Y, W). Note, the parenthetic letters indicate the one-letter codes of amino acids. [0025] In preferred embodiments, the immunogenic peptide is a nonapeptide (9-mer) or a decapeptide (10-mer). The present invention further provides a method of inducing anti-tumor immunity for a disease associated with the over-expression of CDH3, EPHA4, ECT2, HIG2, 1NHBB, KIF20A, KNTC2, TTK and/or URL C10, e.g. cancers, in a subject, such a method including the steps of administering to the subject an imrunogenic peptide of the present invention, namely one having the amino acid sequence of SEQ ID NOs: 19, 22, 30, 34, 344,358, 41,44, 46,48,78,376,379,80,100, 101, 110, 111,387, 112, 394,114, 116, 117,121, 395, 133, 135, 137, 426, 174, 178, 186, 194, 196, 202,210,213,214,217, 223, 227,228, 233, 254, 271, 272 or 288, or a variant thereof (i.e., including 1, 2, or several (e.g., up to 5) amino acid substitutions, deletions, or additions) to the subject in need thereof. The cancers contemplated include, but are not limited to, bladder cancer, breast cancer, cervical cancer, cholangincellular carcinoma, CML, colorectal cancer, endometriosis, esophageal cancer, gastric cancer, diffused type gastric cancer, liver cancer, NSCLC, lymphoma, osteosarcoma, ovarian cancer, CRfPgribflCRAAMEM4I~I.DC1MilII - 23 pancreatic cancer, pancreatic cancer, prostate cancer, renal carcinoma, SCLC, soft tissue tumor and testicular tumor. [0026] In the context of the present invention, the subject is preferably a mammal. Exemplary mammals include, but are not limited to, e.g., a human, non-human primate, mouse, rat, dog, cat, horse, or cow. In the present invention, the peptide can be administered to a subject via an in vivo or ex vivo protocol. Furthermore, the present invention also provides use of nonapeptide or decapeptide selected from peptides having the amino acid sequence of SEQ ID NOs: 19, 22, 30, 34, 344, 358, 41, 44, 46, 48, 78, 376, 379, 80, 100, 101, 110, 111, 387, 112, 394, 114,116,117,121,395, 133, 135,137,426,174,178,186,194, 196,202,210,213, 214, 217, 223, 227, 228, 233, 254, 271, 272 or 288 (and variants thereat) for manufacturing an immunogenic composition for treating or preventing a disease associated with the over expression of CDH3, EPHA4, ECT2, HIG2, INHBB, KWF20A, KNTC2, TTK and/or URLC 10, e.g. cancers. The cancers contemplated include, but are not limited to, bladder cancer, breast cancer, cervical cancer, cholangincellular carcinoma, CML, colorectal cancer, endometriosis, esophageal cancer, gastric cancer, diffused type gastric cancer, liver cancer, NSCLC, lymphoma, osteosarcoma, ovarian cancer, pancreatic cancer, pancreatic cancer, prostate cancer, renal carcinoma, SCLC, soft tissue tumor and testicular tumor. [0027] Homology analyses of the following peptides demonstrate that they do not have significant homology with the peptides derived from any known human gene products. CDH3-A24-9-513 (SEQ ID NO: 19), CDH3-A24-9-406 (SEQ ID NO: 22), CDH3-A24-10-807 (SEQ ID NO: 30), CDH3-A24-10-332(SEQ ID NO: 34), CDH3-A24-10-655 (SEQ ID NO: 344), CDH3-A24-10-470 (SEQ ID NO: 358), EphA4-A24-9-453 (SEQ ID NO: 41), EphA4-A24-9-5 (SEQ ID NO: 44), EphA4-A24-9-869 (SEQ ID NO: 46), EphA4-A24-9-420 (SEQ ID NO: 48), EphA4-A24-10-24 (SEQ ID NO: 78), EphA4-A02-9-501 (SEQ ID NO: 376), EphA4-A02-9-165 (SEQ ID NO: 379), ECT2-A24-9-515 (SEQ ID NO: 80), ECT2-A24-10-40 (SEQ ID NO: 100), ECT2-A24-10-101 (SEQ ID NO: 101), HIG2-A24-9-19 (SEQ ID NO: 110), 24 WO 2008/102557 PCTJP2008/000290 IG2-A24-9-22 (SEQ ID NO: I 11), HIG2-A24-9-8 (SEQ ID NO: 387), HIG2-A24-10-7 (SEQ ID NO: 112), IG2-A24-10-18 (SEQ ID NO: 394), HIG2-A02-9-8 (SEQ ID NO: 114), HIG2-A02-9-15 (SEQ ID NO: 116), HIG2-A02-9-4 (SEQ ID NO: 117), HIG2-A02-10-8 (SEQ ID NO: 121), INMBB-A24-9-180 (SEQ ID NO: 395), INHBB-A24-10-180 (SEQ ID NO: 133), INHBB-A24-10-305 (SEQ ID NO: 135), INHBB-A24-10-7 (SEQ ID NO: 137), INHBB-A24-10-212 (SEQ ID NO: 426), KIF20A-A24-9-305-(SEQ ID NO: 174), KIF20A-A24-9-383 (SEQ ID NO: 178), KIF20A-A24-10-304 (SEQ ID NO: 186), KIF20A-A24-10-66 (SEQ JD NO: 194), KNTC2-A24-9-309 (SEQ ID NO: 196), KNTC2-A24-9-124 (SEQ ID NO: 202), KNTC2-A24-9-154 (SEQ ID NO: 210), KNTC2-A24-9-150 (SEQ ID NO: 213), KNTC2-A24-10-452 (SEQ ID NO: 214), KNTC2-A24-10-227 (SEQ D NO: 21.7), KNTC2-A24-10-273 (SEQ ID NO: 223), TTK-A02-9-462 (SEQ ID NO: 227), TTK-A02-9-547 (SEQ ID NO: 228), TTK-A02-9-719 (SEQ ID NO: 233), TTK-AO2-10-462 (SEQ ID NO: 254), URLC-A02-9-206 (SEQ ID NO: 271), URLC-A02-9-212 (SEQ ID NO: 272) and URLC-A02-10-211 (SEQ ID NO: 288) [0028] Accordingly, the possibility of unknown or undesirable immune responses with im munotherapy against these molecules is significantly reduced. [0029] Regarding HLA antigens, the data presented here demonstrate that the uses of A-24 type or A-2 type antigens (which are said to be highLy expressed among the Japanese) are favorable for obtaining effective results. The uses of subtypes such as A-2402 and A-0201 are even more preferable. Typically, in the clinic, the type of HLA antigen of the patient requiring treatment is investigated in advance, which, in turn, enables the 25 WO 2008/102557 PCT/JP2008/000290 selection of appropriate peptides having high levels of binding affinity to the patient antigen, or having cytotoxic T cell (CTL) inducibility by antigen presentation. Fur thermore, in order to obtain peptides having high binding affinity and CTL indu cibility, substitution, deletion, or addition of 1,2, or several (e.g., up to 5) amino acids may be performed based on the amino acid sequence of the naturally occurring CDH3, EPHA4, BCT, HIG2, INHBB, KIF20A, KNTC2, TTK and URLC10 partial peptide. Herein, the term "several" means refers to 5 or less, more preferably 3 or less. Fur thermoje, in addition to peptides that are naturally displayed, since the regularity of the sequences of peptides displayed by binding to HLA antigens is already known (Kubo RT, et al., (1994) 1 ImmunoL, 152, 3913-24.; Rammensee HG, et al., (1995) Immuno genetics. 41:178-228.; Kondo A, et al., (1995) . Immunol. 155:43:07-12.), modi fications based on such regularity can be performed on the immunogenic peptides of the invention. For example, peptides possessing high HLA-24 binding affinity in which the second amino acid from the N terminus substituted with phenylalanine, tyrosine, methionine, or tryptophan may be favorably used. Likewise, peptides whose C-terminal amino acid is substituted with phenylalanine, leucine, isoleucine, tryptophan, or methionine may also be used favorably. On the other hand, peptides possessing high HLA-A2 binding affinity in which the second amino acid from the N terminus substituted with leucine or methionine, and peptides whose C-teminal amino acid is substituted with valine or leucine may be used favorably. The substitution is performed not only at the terminus amino acids but also at the position of potential TCR recognition of peptides. Several studies have demonstrated that amino acid sub stitutions in a peptide can be equal to or better than the original, for example CAP1, p 53 (x4.272), Her-2/neu c.m or gplOQ m00 27) (Zaremba et al. Cancer Res. 57, 4570-4577, 1997, T. K. Hoffmann et al. Jimmuanol. (2002) Feb 1;168(3):1338-47., S. 0. Dionne et al. Cancer Imumunol immunother. (2003) 52: 199-206 and S. 0. Dionne et al. Cancer Inununology, immunotherapy (2004) 53, 307-314). Furthermore, I to 2 amino acids may be added to the N terminus and/or C terminus of the peptide. [0030] However, when the peptide sequence is identical to a portion of the amino acid sequence of an endogenous or exogenous protein having a different function, side effects such as autoimmune disorders or allergic symptoms against specific substances may be induced. Therefore, it is preferable to avoid the situation wherein the im munogenic sequence matches the amino acid sequence of a known protein. This situation may be avoided by performing a homology search using available databases. If homology searches confirm that peptides in which 1, 2 or several different amino acids do not exist in nature, then the danger that modifications of the above-mentioned anino acid sequence that, for example, increase the binding affinity with HLA antigens, and/or increase the CTL inducibility can be avoided, 26 WO 200/102557 PCT/JP20s/oOv029 [0031] Although peptides having high binding affinity to the HLA antigens as described above are expected to be highly effective as cancer vaccines, the candidate peptides, which are selected according to the presence of high binding affinity as an indicator, must be examined for the actual presence of CTL inducibility. CTL inducibility may be routinely confirmed by inducing antigen-presenting cells canying human MHC antigens (for example, B-lymphocytes, macrophages, and dendritic cells), or more spe cifically dendritic cells derived from human peripheral blood.mcxonuclear leukocytes, and, after stimulation with the peptide of interest, mixing with CD8-positive cells and measuring the cytotoxic activity against the target cells..As the reaction system, transgenic animals produced to express a human HLA antigen (for example, those described in BenMohamed L, et al., (2000) Hum. Immunol.; 61(8):764-79 Related Articles, Books, Linkont.) may be used. For example, the target cells can be radio labeled with nCr and such, and cytotoxic activity can be calculated from radioactivity released from the target cells. Alternatively, it can be examined by measuring IFN gamma produced and released by CTL in the presence of antigen-presenting cells that carry immobilized peptides, and visualizing the inhibition zone on the media using anti-IFN-gamma monoclonal antibodies. [0032] As a result of examining the CTL inducibility of peptides as described above, it was discovered that those peptides having high binding affinity to an HLA antigen did not necessarily have high inducibility. However, nonapeptides or decapeptides selected from the group of peptides having the amino acid sequences indicated by the following peptides showed particularly high CTL inducibility. CDH3-A24-9-513 (SEQ ID NO: 19), CDH3-A24-9-406 (SEQ ID NO: 22), CDH3-A24-10-807 (SEQ ID NO: 30), CDH3-A24-10-332 (SEQ ID NO: 34), CDE3-A24-10-655 (SEQ ID NO: 344), CDH3-A24-10-470 (SEQ ID NO: 358), EphA4-A24-9-453 (SEQ ID NO: 41), EphA4-A24-9-5 (SEQ ID NO: 44), EphA4-A24-9-869 (SEQ ID NO: 46), EphA4-A24-9-420 (SEQ ID NO: 48), EphA4-A24-10-24 (SEQ ID NO: 78), EphA4-A02-9-501 (SEQ ID NO: 376), EphM-A02-9-165 (SEQID NO: 379), ECT2-A24-9-515 (SEQ ID NO: 80), ECT2-A24-10-40 (SEQ ID NO: 100), ECT2-A24-10--101 (SEQ ID NO: 101), 27 WO 2008/102557 PCT/JP2008/00290 HIG2-A24-9-19 (SEQ ID NO: 110), HG2-A24-9-22 (SEQ ID NO: 111), HIG2-A24-9-8 (SEQ ID NO: 387), HIG2-A24-10-7 (SEQ ID NO: 112), IG2-A24-10-18 (SEQ ID NO: 394), HIG2-A02-9-8 (SEQ ID NO: 114), mG2-A02-9-15 (SEQ ID NO: 116), HIG2-A02-9-4 (SEQ ID NO: 117), HIG2-A02-10-8 (SEQ ID NO: 121), INIBB-A24-9-180 (SEQ ID NO 395), INHBB-A24-10-180 (SEQ ID NO: 133), IBB-A24-10-305 (SEQ ID NO: 135), INHBB-A24-10-7 (SEQ ID NO: 137), INBB-A24-10-212 (SEQ ID NO: 426), KIF20A-A24-9-305 (SEQ ID NO: 174), KIF20A-A24-9-383 (SEQ ID NO: 178), KIF20A-A24-10-304 (SEQ ]ID NO: 186), KIF20A-A24-10-66 (SEQ ID NO: 194), KNTC2-A24-9-309 (SEQ ID NO: 196), KNTC2-A24-9-124 (SEQ ID NO: 202), KNTC2-A24-9-154 (SEQ ID NO: 210), KN'IC2-A24-9-150 (SEQ ID NO: 213), KNTC2-A24-10-452 (SEQ ID NO: 214), KNTC2-A24-10-227 (SEQ ID NO: 217), KNTC2-A24-10-273 (SEQ ID NO: 223), TTK-A02-9-462 (SEQ ID NO: 227), TTK-A02-9-547 (SEQ ID NO: 228), TTK-A02-9-719 (SEQ ID NO: 233), TTK-A02-10-462 (SEQ ID NO: 254), URLC-A02-9-206 (SEQ ID NO: 271), URLC-A02-9-212 (SEQ ID NO- 272) and URLC-A02-10-211 (SEQ ID NO: 288) [00331 As noted above, the present invention provides pepiides having cytotoxic T cell indu cibility, namely those having the amino acid sequence of SEQ ID NOs: 19,22, 30, 34, 344,358,41,44,46, 48,78, 376,379,80, 100,101, 110,111, 387,112, 394,114, 116, 117, 121, 395, 133, 135, 137,426, 174, 178, 186, 194, 196, 202, 210, 213, 214, 217, 223, 227, 228, 233, 254, 271, 272 or 288 or a variant thereof (i.e., those in which 1, 2, or several amino acids are substituted, deleted, or added).

28 WO 2008/102557 PCT/JP200&/00U290 [00341 It is prferable that the amino acid sequences composed of 9 or 10 amino acids indicated in SEQ ID NOs: 19, 22, 30, 34, 344,358,41, 44,46, 48, 78, 376, 379, 80, 100, 101, 110, 111, 387, 112, 394, 114,116, 117, 121,395,133, 135, 137, 426, 174, 178, 186, 194, 196, 202, 210, 213, 214, 217, 223, 227, 228, 233, 254, 271, 272 or 288 or a variant thereof do not match an amino acid sequence associated with another en dogenous protein. [0035] In particular, amino acid substitution to leucine or methionine at the second amino acid from the N terminus, amino acid substitution to valine or leuciDe at the C-terminal amino acid, and amino acid addition of 1 to 2 amino acids at theN terminus and/or C terminus are examples of prefeed variants. [0036] One of skill in the art will r&ognize that in addition to amino acid substitutions and additions, immunologically active fragments of the peptides may also be used in the methods of the invention. Methods for determining active fragments are well known in the art. CTL clones obtained by stimulation by these modified peptides can recognize the original peptides and cause damage for cells expressing the original peptides. [0037] Peptides of the present invention can be prepared using well known techniques. For example, the peptides can be prepared synthetically, using either recombinant DNA technology or chemical synthesis. Peptides of the present invention may be synthesized individually or as longer polypeptides composed of two or more peptides. The peptides of the present invention are preferably isolated, i.e., substantially free of other naturally occurring host cell proteins and fragments thereof. [00381 The peptides of the present invention may contain modifications, such as glyc osylation, side chain oxidation, or phosphorylation; so long as the modifications do not destroy the biological activity of the peptides as described herein, namely the ability to binding to an HLA antigen and induce CTL Other modifications include incorporation of D-amino acids or other amino acid mimetics that can be used, for example, to increase the serum half life of the peptides. [00391 Moreover, this invention may contain a method of screening for a peptide which 1, 2, or several amino acids are substituted, wherein said peptide comprises an amino acid sequence selected from the group consisting of SEQ ID NO: SEQ ID NO: 19, 22, 30, 34, 344, 358, 41, 44, 46, 48, 78, 80, 100, 101, 110, 111, 387, 112, 394, 395, 133, 135, 137, 426, 174, 178, 186, 194, 196, 202, 210,213, 214,217 or 223, said method comprising the steps of: (a) comforting no significant sequence homology to the entire sequence of 1, 2 or several amino acids substitute; (b) measuring the CTL inducibility of the candidate substitute peptide; and (c) selecting the peptide which CTL inducibility is same to or higher than the original peptide.

-29 [0040] For example, in preferred embodiments, the present invention provides a method of identifying for a peptide having an ability to induce CTL against cells expressing at least one tumor-associated antigen, wherein the tumor-associated antigen is antigen selected from the group consisting of CDH3, EPHA4, ECT2, HIG2, INHBB, KIF20A, KNTC2, TTK and URLCJ0, said method comprising the steps of (i) providing or generating at least one candidate sequence which consists of an amino acid sequence modified by substituting, deleting, or adding one, two or several amino acid residues to an original amino acid sequence, wherein the original amino acid sequence is selected from the group consisting of SEQ ID NO: SEQ ID NO: 19, 22, 30, 34, 344, 358, 41, 44, 46, 48, 78, 80, 100, 101, 110, 111, 387, 112,394, 395, 133, 135, 137, 426, 174, 178, 186, 194, 196, 202, 210, 213, 214, 217 or 223; (ii) selecting the candidate sequence that does not have substantial significant homology with the peptides derived from any known human gene products other than said tumor-associated antigens; (iii) contacting a peptide consisting of the candidate sequence selected in step (ii) with antigen presenting cells; (iv) contacting the antigen presenting cells of step (iii) with T-cells to evaluate the ability of the peptide to stimulate the T-cells; and (v) identifying the peptide of which CTL inducibility is same to or higher than a peptide consisting of the original amino acid sequence. [0041] Preferably, the amino acid is substituted for a different amino acid in which the properties of the amino acid side-chain are conserved (a process known as conservative amino acid substitution). Examples of properties of amino acid side chains are hydrophobic amino acids (A, I, L, M, F, P, W, Y, V), hydrophilic amino acids (R, D, N, C, E, Q, G, H, K, S, T), and side chains having the following functional groups or characteristics in common: an aliphatic side-chain (G, A, V, L, I, P); a hydroxyl group containing side-chain (S, T, Y); a sulfur atom containing side-chain (C, M); a carboxylic acid and amide containing side-chain (D, N, E, Q); a base containing side-chain (R, , H); and an aromatic containing side-chain (H, F, Y, W). Note, the parenthetic letters indicate the one-letter codes of amino acids. In the present invention, substantial significant homology is, for example, more than 90%, preferably 95%, more preferably 99%/0 or 100% identity with a known human gene product to be compared. [0042] The peptides of this invention can be prepared as a combination, which includes two or more of peptides of the invention, for use as a vaccine for a disease associated with the over-expression of CDH3, EPHA4, ECT2, HIG2, INHBB, KIF20A, KNTC2, TTK and/or URLC 10, e.g. cancers, such a vaccine inducing CTL in vivo. The cancers contemplated include, but are not limited to, bladder cancer, breast cancer, cervical cancer, -30 cholangincellular carcinoma, CML, colorectal cancer, endometriosis, esophageal cancer, gastric cancer, diffused type gastric cancer, liver cancer, NSCLC, lymphoma, osteosarcoma, ovarian cancer, pancreatic cancer, prostate cancer, renal carcinoma, SCLC, soft tissue tumor and testicular tumor. The peptides may be in a cocktail or may be conjugated to each other using standard techniques. For example, the peptides can be expressed as a single polypeptide sequence. The peptides in the combination may be the same or different. [0043] By administering the peptides of this invention, the peptides are presented at a high density on the HLA antigens of antigen-presenting cells, which, in turn, induces CTLs that specifically react toward the complex formed between the displayed peptide and the HLA antigen. Alternatively, antigen-presenting cells having immobilized the peptides of this invention on their cell surface, obtained by removing dendritic cells from the subjects, may be stimulated by the peptides of this invention. Re-administration of these cells to the respective subjects induces CTL, and, as a result, aggressiveness towards the target cells can be increased. [0044] More specifically, the present invention provides drugs for treating and/or preventing proliferation, metastasis, and such of a disease associated with the over expression of CDH3, EPHA4, ECT2, 1IG2, INH1BB, KIF20A, KNTC2, TTK and/or URLC10, e.g. cancers, which include one or more of peptides of the present invention, or a polynucleotide encoding the peptides. The peptides or polynucleotides of the present invention find particular utility in the treatment of a disease associating CDH3, EPHA4, ECT2, HIG2, INHBB, KIF20A, KNTC2, TTK and/or URLC1O, e.g. cancers. The cancers contemplated include, but are not limited to, bladder cancer, breast cancer, cervical cancer, cholangincellular carcinoma, CML, colorectal cancer, endometriosis, esophageal cancer, gastric cancer, diffused type gastric cancer, liver cancer, NSCLC, lymphoma, osteosarcoma, ovarian cancer, pancreatic cancer, prostate cancer, renal carcinoma, SCLC, soft tissue tumor and testicular tumor. [0045] The peptides of this invention can be administered to a subject directly, as a pharmaceutical composition that has been formulated by conventional formulation methods. In such cases, in addition to the peptides of this invention, carriers, excipients, and such that are ordinarily used for drugs can be included as appropriate, without particular limitations. The immunogenic compositions of this invention may be used for treatment and prevention of a disease associated with the over-expression of CDH3, EPHA4, ECT2, HIG2, INHBB, KIF20A, KNTC2, TTK and/or URLC10, e.g. cancers, The cancers contemplated include, but are not limited to, bladder cancer, breast cancer, cervical cancer, cholangincellular carcinoma, CML, colorectal cancer, endometriosis, esophageal cancer, gastric cancer, diffused type gastric cancer, liver cancer, NSCLC, lymphoma, osteosarcoma, ovarian cancer, pancreatic cancer, prostate cancer, -31 renal carcinoma, SCLC, soft tissue tumor and testicular tumor. [0046] The immunogenic compositions for treatment and/or prevention of a disease associated with the over-expression of CDH3, EPHA4, ECT2, HIG2, INHBB, KIF20A, KNTC2, TTK and/or URLC1O, e.g. cancers, which include as the active ingredient one or more peptides of the present invention, can further include an adjuvant so that cellular immunity will be established effectively. Alternatively, they may be administered with other active ingredients, such as anti-cancer agents. [0047] The cancers contemplated include, but are not limited to, bladder cancer, breast cancer, cervical cancer, cholangincellular carcinoma, CML, colorectal cancer, endometriosis, esophageal cancer, gastric cancer, diffused type gastric cancer, liver cancer, NSCLC, lymphoma, osteosarcoma, ovarian cancer, pancreatic cancer, prostate cancer, renal carcinoma, SCLC, soft tissue tumor and testicular tumor. Suitable formulations include granules. Suitable adjuvants are described in the literature (Johnson AG. (1994) Clin. Microbiol. Rev., 7:277-89.). [0048] Exemplary adjuvants include, but are not limited to, aluminum phosphate, aluminum hydroxide, and alum. Furthermore, liposome fonnulations, granular formulations in which the drug is bound to few-mo m diameter beads, and formulations in which a lipid is bound to the peptide may be conveniently used. The method of administration may be oral, intradermal, subcutaneous, intravenous injection, or such, and may include systemic administration or local administration to the vicinity of the targeted tumor. [0049] The dose of the peptide(s) of this invention can be adjusted appropriately according to the disease to be treated, age of the patient, weight, method of administration, and such. Though the dosage is ordinarily 0.00 1 mg to 1000 mg, preferably 0.01 rag to 100 Mg, more preferably 0.1 mg to 10 mg, preferably administered once in a few days to few months, one skilled in the art can readily select the appropriate dose and method of administration, as, the selection and optimization of these parameters is well within routine skill. [0050] The present invention further provides intracellular vesicles called exosomes, which present complexes formed between the peptides of this invention and HLA antigens on their surface. Exosomes can be prepared, for example, by using the methods described in detail in Published Japanese Translation of International Publication Nos. Hei 11-510507 and 2000-512161, and are preferably prepared using antigen-presenting cells obtained from subjects who are targets of treatment and/or prevention. The exosomes of this invention can be inoculated as cancer vaccines, similarly to the peptides of this invention. [0051] The type of HLA antigens used must match that of the subject requiring treatment and/or prevention. For example, in the Japanese population, HLA-A24 or HLA-A2, 32 WO 2008/102557 PCT/JP2008/000290 particularly HLA-A2402 or HLA-A0201, is often appropriate. [0052] In some embodiments, the vaccine compositions of the present invention include a component which primes cytotoxic T lymphocytes. Lipids have been identified as agents capable of piming CTL in vivo against viral antigens. For example, palmitic acid residues can be attached to the epsilon-and alpha-amino groups of a lysine residue and then linked to an immunogenic peptide of the invention. The lipidated peptide can then be administered either directly, in a micelle or particle, incorporated into a liposome, or emulsified in an adjuvant. As another example of a lipid priming of CTL responses, E. coli lipoproteins, such as tripalmitoyl-S-glycerylcysteinlyseryl- seripe (P3CSS), can be used to fie CTL when covalently attached to an appropziate peptide (see, e.g., eres K, et al., (1989) Nature 342:561-4.). [00531 The immunogenic compositions of the present invention may also include nucleic acids encoding one or more of the immunogenic peptides disclosed hem. See, e.g., Wolff JA et al., (1990) Science 247:1465-8; U.S. Patent Nos. 5,580,859; 5,589,466; 5,804,566; 5,739,118; 5,736,524; 5,679,647; and WO 98/04720. Examples of DNA based delivery technologies include "naked DNA", facilitated (bupivicaine, polymers, peptide-mediated) delivery, cationic lipid complexes, and particle-mediated ("gene gun") or pressure-mediated delivery (see, e.g., U.S. Patent No. 5,922,687). [0054] The immunogenic peptides of the invention can also be expressed by viral or bacterial vectors. Examples of suitable expression vectors include attenuated viral hosts, such as vaccinia or fowlpox. This approach involves the use of vaccinia virus, e.g., as a vector to express nucleotide sequences that encode the peptide. Upon in troduction into a host, the recombinant vaccinia virus expresses the immunogenic peptide, and thereby elicits an immune response. Vaccinia vectors and methods useful in immunization protocols are described in, e.g., .U.S. Patent No. 4,722,848. Another suitable vector is BCG (Bacille Calmette Guerin). BCG vectors are described in Stover CK, et al., (1991) Nature 351:456-60. A wide variety of other vectors useful fbr therapeutic administration or immunization e.g., adeno and adeno-associated virus vectors, retroviral vectors, Salmonella typhi vectors, detoxified anthrax toxin vectors, and the like, are known in the art. See, e.g., Sbata MT, et aL, (2000) Mol. Med. Today 6:66-71; Shedlock DI and Weiner DR., et al., (2000) 1. Leukoc. Biol. 68:793-806; and Hipp JD, et al., (2000) In Vivo 14:571-85. [0055] The present invention also provides methods of inducing antigen-presenting cells using one or more peptides of this invention. The antigen-presenting cells can be induced by inducing dendritic cells from the peripheral blood monocytes and then contacting (stimulating) them with one or more peptides of this invention in vitro, ex vivo or in vivo. When peptides of the present invention are administered to the subjects, antigen-presenting cells that have the peptides of this invention iranobilized -33 to them are induced in the body of the subject Alternatively, after immobilizing the peptides of this invention to the antigen-presenting cells, the cells can be administered to the subject as a vaccine, For example, the ex vivo administration may include the steps of: a: collecting antigen-presenting cells from a subject, and b: contacting the antigen-presenting cells of step a with a peptide of the present invention. [0056] Alternatively, according to the present invention, use of the peptides of this invention for manufacturing a pharmaceutical composition inducing antigen-presenting cells is provided. Further, the present invention also provides the peptide of the present invention for inducing antigen-presenting cells. The antigen-presenting cells obtained by step b can be administered to the subject as a vaccine, [0057] This invention also provides a method for inducing antigen-presenting cells having a high level of cytotoxic T cell inducibility, in which the method includes the step of transferring genes composed of polynucleotide(s) encoding one or more peptides of this invention to antigen-presenting cells in vitro. The introduced genes may be in the forn of DNAs or RNAs. For the method of introduction, without particular limitations, various methods conventionally performed in this field, such as lipofection, electroporation, and calcium phosphate method may be suitably used. More specifically, transfection may be perfonned as described in Reeves ME, at al., (1996) Cancer Res., 56:5672-7.; Butterfield LH, et at, (1998) J. Irrnunol., 161:5607-13.; Boczkowski D, et al., (1996) J. Exp. Med., 184:465-72.; Published Japanese Translation of International Publication No. 2000 509281. By transferring the gene into antigen-presenting cells, the gene undergoes transcription, translation, and such in the cell, and then the obtained protein is processed by MHC Class I or Class II, and proceeds through a presentation pathway to present partial peptides. [0058] The present invention further provides methods for inducing CTL using one or more peptides of this invention. When the peptides of this invention are administered to a subject, CTL are induced in the body of the subject, and the strength of the immune system targeting the cells expressing CDH3, EPHA4, ECT2, IG2, NHBB, KIF20A, KNTC2, TTK and/or URLC1 0, e.g. cancer cells in the tumor tissues is thereby enhanced. [0059] The cancers contemplated include, but are not limited to bladder cancer, breast cancer, cervical cancer, cholangincellular carcinoma, CML, colorectal cancer, endometriosis, esophageal cancer, gastric cancer, diffused type gastric cancer, liver cancer, NSCLC, lymphoma, osteosarcoma, ovarian cancer, pancreatic cancer, prostate cancer, renal carcinoma, SCLC, soft tissue tumor and testicular tumor. Alternatively, the peptides of the present invention may be used in the context of an.ex vivo therapeutic 34 WO 2008/102557 PCT/JP2008/000290 method, in which subject-derived antigen-presenting cells and CD8-positive cells or peripheral blood mononuclear leukocytes am contacted (stimulated) with one or more peptides of this invention-in vitro, and, after inducing CTL, the celIs are returned to the subject. For example, the method may include the steps of:. a: collecting antigen-presenting cells from a, subject, b: contacting the antigen-presenting cells of step a with a peptide of the present invention, c: inxing the antigen-presenting cells of step b with CD'+ T cells and co-culturing so as to induce cytotoxic T-cells:, and d: collecting CDII T cells from the co-culture of step c. [0060] Alternatively, according to the present invention, use of the peptides of tlis invention for manufacturing a pharmaceutical composition inducing CTLs is provided. Father, the present invention also provides the peptide of the present invention for inducing CTLs. The CD" T cells having cytotoxic activity obtained by step d can be ad ministered to the subject as a vaccine. [0061] The present invention further provides isolated cytotoxic T cels induced using the peptides of this invention. The cytotoxic T cells, induced by stimulation with an antigen-presenting cell presenting one or more peptides of this invention, are preferably derived from subjects who are the target of treatment and/or prevention, and can be administered alone or in combination with other drugs, including one or more peptides of this invention or exosomes having anti-tunor activity. The obtained cytotoxic T cells act specifically against target cells presenting the peptides of this invention, or preferably the same peptide(s) used for induction. The target cells may be cells that express CDH3, EPHA4, ECT2, HIG2, JIBB, KIF2OA, KNTC2, TTK and/ or URLC1O endogenously, or cells that are transfected with CDH3, EPHA4, ECT2, HIG2, INBB,XW20A, KNTC2, TTK and/or URLC1O genes. Cells that present the peptides of this invention on the cell surface, due to stimulation with these peptides, can also become targets of attack. [0062] The present invention also provides antigen-presenting cells presenting complexes formed between HLA antigens and one or more peptides of this invention. The antigen-presenting cells, obtained through contact with the peptides of this invention or the nucleotides encoding such peptides, are preferably derived from subjects who are the target of treatment and/or prevention, and can be administered as vaccines, alone or in combination with other drugs, including the peptides, exosomes, or cytotoxic T cells of the present invention. [0063] The present invention also provides a composition composed of nucleic acids encoding polypeptides that are capable of forming a subunit of a T cell receptor (TCR), and methods of using the same. The TCR subunits have the ability to forn TCRs that 35 WO 2008102557 PCT/JP2008/000290 confer specificity to T cells for tumor cells presenting CDH3, EPHA4, ECT2, HIGZ INRBB, KIF20A, KNTC2, TTK or URLC10. By using the known method in the art, the nucleic acids of alpha- and betachain as the TCR subunits of the CTL induced with one or mom peptides of this invention may be identified (WO20071032255 and Morgan et al., J nmunol, 171, 3288 (2003)). The derivative TCRs preferably bind target cells displaying the CDH3, EPHA4, ECT2, HIG2, BB, KIF2OA, KNTCZ TTK or JRLC10 peptide with high avidity, and optionally mediate efficient killing of target cells presenting the CDH3, EPHA4, ECT2, HIG2, INHBB, KIF20A, KNTC2, TTK or URLC10 peptide in vivo and in vitro. [00641 The nucleic acids encoding the TCR subunits can be incorporated into suitable vectors e.g. rtroviral vectors. These vectors are well known in the art. The nucleic acids or the vectors containing them usefully can be transferred into a T cell, which T cell is preferably from a patient. Advantageously, the invention provides an off the-shelf composition-allowing rapid modification of a patient's own T cells (or those of another mammal).to rapidly and easily produce modified T cels having excellent cancer cell killing properties. [0065 Also, the present invention provides CTLs which are prepared by transduction with the nucleic acids encoding the TCR subunits polypeptides binding with CDH3, EPHA4, ECT2, HIGZ INHBB, KIP20A, KNTC2, TTK or URLC10 peptide e.g. SEQ ID NOs: 19, 22, 30, 34, 344, 358, 41, 44, 46,48,78,376, 379, 80, 100, 101, 110, 111, 387, 112, 394, 114, 116, 117, 121, 395, 133, 135, 137, 426, 174, 178, 186, 194, 196, 202,210,213,214, 217, 223, 227, 228, 233, 254, 271, 272 or 288 in the context of HLA-A24 or HLA-A2. The transduced CTLs aue capable of homing to cancer cells in vivo, and expanded by well known culturing method in vitro (e.g., Kawakami et al., J Immunol., 142, 3452-3461 (1989)). The T cells of the invention can be used to form an immunogenic composition useful in treating or preventing cancer in a patient in need of therapy orprotection (WO2006/031221). [00661 In the context of the prsent invention, the term "vaccine" (also referred to as an im munogenic composition) refers to a substance that induces anti-tumor immunity or suppresses cancers upon inoculation into animals. According to the present invention, polypeptides having the amino acid sequence of SEQ ID NO: 19, 22, 30, 34, 344, 358, 41, 44,46,48,78,80, 100, 101, 110, 111, 387, 112,394,395, 133, 135,137,426, 174, 178, 186, 194, 196,202, 210,213, 214, 217 or 223 were suggested to be HLA-A24 re stricted epitope peptides and those of SEQ ID NO: 376, 379, 114, 116, 117, 121, 227, 228, 233, 254, 271, 272 or 288 were suggested to be ELA-A2 restdcted epitope peptides that may induce potent and specific immune response against cells expressing CDH3, EPHA4, ECT2, HIG2, INHBB, KIF20A, KNTC2, TTK and/or URLC 10, e.g. cancer cells expressing CDH3, EPHA4, ECT2, HIG2, INHBB, KIF20A, KNTC2, TTK -36 and/or URLCI 0. The cancers contemplated include, but are not limited to bladder cancer, breast cancer, cervical cancer, cholangincellular carcinoma, CML, colorectal cancer, endometriosis, esophageal cancer, gastric cancer, diffused type gastric cancer, liver cancer, NSCLC, lymphoma, osteosarcoma, ovarian cancer, pancreatic cancer, prostate cancer, renal carcinoma, SCLC, soft tissue tumor and testicular tumor. [0067] Thus, the present invention also encompasses a method of inducing anti-tumor immunity using polypeptides having the amino acid sequence of SEQ ID NO: 19,22,30, 34, 344, 358, 41, 44, 46, 48, 78, 376, 379, 80, 100, 101, 110, 111, 387, 112, 394, 114,116, 117, 121,395, 133, 135, 137, 426, 174, 178, 186, 194, 196,202, 210, 213, 214,217, 223, 227, 228,233, 254, 271,272 or 288 or a variant thereof (i.e., including 1, 2, or several (e.g., up to 5) amino acid substitutions, deletions, or additions). In general, anti-tumor immunity includes immune responses such as follows: -an induction of cytotoxic lymphocytes against tumors containing cells expressing CDH3, EPHA4, ECT2, HIG2, INHBB, KIF20A, KNTC2, TTK and/or URLC10, - an induction of antibodies that recognize tumors containing cells expressing CDH3, EPHA4, ECT2, HIG2, IMIBB, KIF20A, KNTC2, TTK and/or URLCI0, and - an induction of anti-tumor cytokine production. [0068] Therefore, when a certain peptide induces any one of these immune responses upon inoculation into an animal, the peptide is decided to have anti-tumor immunity inducing effect. The induction of the anti-tumor immunity by a peptide can be detected by observing in vivo or in vitro the response of the immune system in the host against the peptide. [0069] For example, a method for detecting the induction of cytotoxic T lymphocytes is well known. A foreign substance that enters the living body is presented to T cells and B cells by the action of antigen-presenting cells (APCs). T cells that respond to the antigen presented by APC in antigen specific manner differentiate into cytotoxic T cells (also referred to as cytotoxic T lymphocytes or CTLs) due to stimulation by the antigen, and then proliferate; this process is referred to herein as "activation" of T cells. Therefore, CTL induction by a certain peptide can be evaluated by presenting the peptide to a T cell by APC, and detecting the induction of CTL. Furthermore, APCs have the effect of activating CD4+ T cells, CD8+ T cells, macrophages, eosinophils and NK cells. Since CD4+ T cells are also important in anti-tumor immunity, the anti-tumor immunity inducing action of the peptide can be evaluated using the activation effect of these cells as indicators. [0070] A method for evaluating the inducing action of CTL using dendritic cells (DCs) as APC is well known in the art. DC is a representative APC having the strongest CTL inducing action among APCs. In this method, the test polypeptide is initially contacted with DC and then this DC is contacted with T cells. Detection of T cells having - 37 cytotoxic effects against the cells of interest after the contact with DC shows that the test polypeptide has an activity of inducing the cytotoxic T cells. Activity of CTL against tumors can be detected, for example, using the lysis of 5t Cr-labeled tumor cells as the indicator. Alternatively, it is well known to evaluate the degree of tumor cell damage using 311-thymidine uptake activity or LDH (lactose dehydrogenase)-release as the indicator. Furthermore, it can be also examined by measuring IFN-gamma produced and released by CTL in the presence of antigen-prosenting cells that carry immobilized peptides by visualizing using anti-IFN-gamma antibodies, such as an BLISPOT assay. [0071] Apart from DC, peripheral blood mononuclear cells (PBMCs) may also be used as the APC. The induction of CTL is reported to be enhanced by culturing PBMC in the presence of GM-CSF and IL-4. Similarly, CTL has been shown to be induced by culturing PBMC in the presence of keyhole limpet hemocyanin (KLH) and IL-7. [0072] The test polypeptides confirmed to possess CTL inducing activity by these methods are polypeptides having DC activation effect and subsequent CTL inducing activity. Therefore, polypeptides that induce CTL against cells expressed CDH3, EPHA4, ECT2, HIG2, INHBB, KIF20A, KNTC2, TIK and/or URLCI1O are useful as vaccines against diseases associating CDH3, EPHA4, ECT2, [1G2, INHBB, KIF20A, KNTC2, TTK and/or URLCJ0, e.g. cancers. Furthermore, APC that have acquired the ability to induce CTL against a disease associated with the over-expression of CDH3, EPHA4, ECT2, HIG2, INHBB, KIF20A, KNTC2, TTK and/or URLCIO, e.g. cancers, by contacting with the polypeptides are useful as vaccines against the disease. Furthermore, CTL that have acquired cytotoxicity due to presentation of the polypeptide antigens by APC can be also used as vaccines against a disease associating CDH3, EPHA4, ECT2, HIG2, INHBB, KfF20A, KNTC2, TTK and/or URLC10, e.g. cancers. Such therapeutic methods for a disease associating CDH3, EPHA4, ECT2, HIG2, JNHBB, KIF20A, KNTC2, TTK and/or URLC1 0, e.g. cancers, using anti-tumor immunity due to APC and CTL, are referred to as cellular immunothempy. The cancers contemplated include, but ae not limited to, bladder cancer, breast cancer, cervical cancer, cholangincellular carcinoma, CML, colorectal cancer, endometriosis, esophageal cancer, gastric cancer, diffused type gastric cancer, liver cancer, NSCLC, lymphoma, osteosarcoma, ovarian cancer, pancreatic cancer, prostate cancer, renal carcinoma, SCLC, soft tissue tumor and testicular tumor. {0073] Generally, when using a polypeptide for cellular iununotherapy, efficiency of the CU-induction can be increased by combining a plurality of polypeptides having different structures and contacting them with DC. Therefore, when stimulating DC with protein fragments, it is advantageous to use a mixture of multiple types of fragments.

38 WO 20081102557 PCT/JP2008/00029 0 [0074] The induction of and-tumor immunity by a polypeptide can be further confirmed by observing the induction of antibody production against tumors. For example, when an tibodies against a polypeptide am induced in a laboratory animal immunized Wit the polypeptide, and when growth, proliferation and/or metastasis of tumor cells is suppressed by those antibodies, the polypeptide is determined to induce anti-tumor immunity. [0075] Anti-tumor immunity can be induced by administering a vaccine of this invention, and the induction of anti-tumor immunity enables treatment and prevention of a disease associated with the over-expression of CDH3, EPHA4, ECT2, HIG2, NBB, KEIF20A, KNTC2, TK and/or URLC10, e.g. cancers. Therapy against or prevention of the onset of a disease associated with the over-sxpmssion of CDH3, EPHA4, ECT2; HIG2, INHBB, KIF20A, KNTC2, TTK and/or URLCIO, e.g. cancers, may include in hibition of the growth of cells expressing CDH3, EPHA4, ET2, EIG2, INHBB, KIF20A, KNTC2, TTK and/or URLC10, eg. cancer cells, involution of these cells and suppression of occurrence of these cells, eg. cancer cells. Decrease in mortality of in dividuals having a disease associating CDH3, EPHA4, ECT2, 1102, INHBB, KIF2OA, KNTC2, TTK and/or URLC1O, e.g. cancers, decrease of the disease markers in the blood, alleviation of detectable symptoms accompanying the disease and such are also included in the therapy or prevention of the disease, e.g. cancers. Such therapeutic and preventive effects are preferably statistically significant, for example, observed at a significance level of 5% or less, wherein the therapeutic or preventive effect of a vaccine against a disease associating CDH3, EPHA4, ECT2, IG2, INHBB, KJF20A, KNTC2, TTK and/or URLC1O, e.g. cancers, is compared to a control without vaccine administration. For example, Student's t-test, the Mann-Wbitney U-test or ANOVA may be used for determining statistical significance. [0076] '.In that the present invention provides a method for treating, or preventing a disease associated with the over-expression of CDE3, EPHA4, ECT2, HIG2, INBB, K20A, KNTC2, TTK and/or URLC10, e.g. cancers, the therapeutic compounds or compositions may be administered prophylactically or therapenticaly to subjects suffering from or at risk of (or susceptible to) developing the disease. Such subjects may be identified using standard clinical methods. In the context of the present invention, prophylactic administration occurs prior to the manifestation of overt clinical symptoms of disease, such that a disease or disorder is prevented or al ternatively delayed in its progression. In the context of the field of medicine, the term "prevent" encompasses any activity which reduces the burden of mortality or morbidity from disease. Prevention can occur at primary, secondary and tertiary prevention levels. While primary prevention avoids the development of a disease, secondary and tertimy levels of prevention encompass activities aimed at preventing the progression 39 WO 20W162557 PCT/JP2008/OOO290 of a disease and the emergence of symptoms as well as reducing the negative impact of an already established disease by restoring function and reducing disease-related corn pliations. 10077] In the context of cancer treatment, the tem "effccious" refers to a treatment that leads to a decrease in size, prevalence or metastatic potential of cancer in a subject When a treatment is applied prophylactically, "efficacious" means that the treatment retards or prevents occurence of non cancer or alleviates a clinical symptom of cancer. The assessment of cancer can be made'using standard clinical protocols. Furthermore, the efficaciousness of a treatment may be determined in association with any known method for diagnosing or treating cancer. For example,eancercaii be diagnosed histo pathologically or by identifying symptomatic anomalies. [0078] The above-mentioned peptide, having immunological activity, or a polynucleotide or vector encoding such a peptide, may be combined with an adjuvant. An adjuvant refers to a compound that enhances the immune response against the peptide when ad ministered together (or successively) with the peptide having immunological activity. Examples of suitable adjuvants include cholera toxin, salmonella toxin, alum and such, but are not limited thereto. Furthermore, a vaccine of this invention may be combined appropriately with a pharmaceutically acceptable carrier. Examples of such carriers are sterilized water, physiological saline, phosphate buffer, culture fluid and such. Fur thermor, the vaccine may contain as necessary, stabilizers, suspensions, preservatives, surfactants and such. The vaccine is administered systemically or locally. Vaccine ad ministration may be performed by single administration or boosted by multiple admin istrations. [00791 When using APC or CTL as the vaccine of this invention, a disease associated with the over-expression of CDH3, EPHA4, 9CT2, HIG2, INHBB, KIF20A, KNTC2, TTK and/or UJRI10, e.g. cancers, can be treated or prevented, for example, by the ex vivo method. More specifically, PBMCs of the subject receiving treatment or prevention are collected, contacted ex vivo with a peptide of the present invention. Following the induction of APC or CTL, the cells may be administered to the subject APC can be also induced by introducing a vector encoding the peptide into PBMCs ex vivo. APC or CTL induced in vitro can be cloned prior to administration. By cloning and growing cells having high activity of damaging target cells, cellular immunotherapy can be performed more effectively. Furthermore, APC and CIL isolated in this manner may be used for cellular immunotherapy not only against individuals from whom the cells are derived, but also against similar types of diseases in other individuals. [0080] Aspects of the present invention are described in the following examples, which are presented only to illustrate the present invention and to assist one of ordinary skill in making and using the same. The examples ar not intended in any way to otherwise 40 WO 2008/102557 PCT/JP2008/006290 limit the scope of the invention. [0081] Although methods and materials similar or equivalent to those described herein can be used in the practice or testing of the present invention, suitable methods and materials are described below. [0082] . E&AMPLES Hereinafter, the present invention is exemplified, but not restricted, by the following Examples. However, materials, methods and such described herein only illustrate aspects of the invention and in no way am intended to limit the scope of the present invention. As such, materials, methods and such similar or equivalent to those described therein may be used in the practice or testing of the present invention. [0083] MATERIALS AND METHODS Cell 1ines A24-LCL cells (HLA-A24), human B-Iymphoblastoid cell line, was established by transforming with Epstain-bar virus. T2 cell, COS7, A498, Caki-2 and HEK 293 were purchased from ATCC. Caki-1 and MLAPaca-2 were purchased from JCRB. PK-45P, PK-59, TE-5 and TE-6 were purchased from TKG. 293 T was purchased from GenHunter. [0084] Candidate selecIon of peptide derived from CDH3. EPHA4 EC72. HTO2. TNHB. KIF20A. KNTC2. TTK and URLC10 9-mer and 10-mer peptides derived from CDH3, EPHA4, ECT2, H[G2, INHBB, KIF20A, KNC2, TTK or URLC 10 that bind to HLA-A*2402 or HLA-A*0201 molecule were predicted using the binding prediction software "BIMAS' (bttp:lbimas.dcrtnih.gov/cgi-bin/molbio/ken-parker._comboform) (Parker KC, et al., (1994) J Inmunol.;152(1):163-75.; Kuzushima K, et al, (2001) B-lood.;98(6):1872-81.). These peptides were synthesized by Sigma (Sapporo, Japan) according to the standard solid phase synthesis method and purified by reversed phase EPLC. The purity (>90%) and the identity of the peptides were determined by analytical IPLC and mass spectrometry analysis, respectively. Peptides were dissolved in dimethylsvlfoxide (DMSO) at 20 mg/nil and stored at -80 degrees C. [0085] In vitro CTL Induction Monocyte-derived dendritic cells (DCs) wete used as antigen-presenting cells (APCs) to induce CTL responses against peptides presented on HLA. DCs were generated in vitro as described elsewhere (Nukaya I et al., (1999) Int. J. Cancer 80, 92-7., Tsai V et al., (1997) J. Imunol 158:1796-802.). Briefly, peripheral blood mononuclear cells (PBMCs) isolated from a normal volunteer (RLA-A*2402 and/or HLA-A*0201) by Ficoll-Paque (Pharmacia) solution were separated by adherence to a plastic tissue culture flask (Becton Dickinson) so as to enrich them for the monocyte fraction. The monocyte-enriched population was cultured in the presence of 1000 U/ml 41 WO 2008/102557 PCTJP208/000290 of GM-CSF (Genzyme) and 1000 U/mI of IL-4 (Genzyme)in AIM V(Invitrogen)containing 2% heat-inactivated anlologous serum (AS). After 7 days in the culture, the cytoldne-generated DCs were pulsed with 20 micro g/ml of the syn thesized peptides in thepresence of 3 micro g/ml of beta 2-microglobulin for 4 hrs at 20 degrees C in AIM-V. These peptide-pulsed DCs were then inactivated by MMC (30micro g/ml for 30 mins) and mixed at a 1:20 ratio with autologous CD8+ T cells, obtained by positive selection with Dynabeads M-450 CD8 (Dynal) and DETACHA BEAD'" (Dynal). These cultures were set up in 48-well plates (Coming); each well contained 1.5x104 peptide-pulsed DCs, 3x1O5 CD8+ T cells and 10 ng/nl of IL-7 (Genzyme) in 0.5 ml of AIM-V/2% AS. Three days later, these cultures were sup plermented with I-2 (CHIRON) to a final concentration of 20 IU/mI On day 7 and 14, the T cells were further restimulated with the autologous peptide-pulsed DCs. The DCs were prepared each time by the same way described above. CTL was tested against peptide-pulsed A24-LCL cells or T2 cells after the 3rd round of peptide stimulation on day 21. [0086] CTL Expansion Procedur CTLs were expanded in culture using the method similar to that described by Riddell SR, et al., (Walter EA et al., (1995) N Engl J Med 333:1038-44.; Riddel SR, et al., (1996) Nature Med. 2:216-23.). A total 5x 104 of CTLs were resuspended in 25 ml of AJIM-V/5% AS with 2 kinds of human B-lympboblastoid cell lines, inactivated by MMC, in the presence of 40 ng/m1 of anti-CD3 monoclonal antibody (Phanningen). One day after initiating the cultures, 120 I/mI of ILr2 were added to the cultures. The cultums were fed with fresh AIM-V/5% AS containing 30 IU/ml of IL-2 on days 5, 8 and 11. [0087] Establishment of CTL clones The dilutions were made to have 0.3, 1, and 3 CTLs/wel in 96 round-bottomed micro titer plate (Nalge Nunc International). CTLs were cultured with 7x10 4 cells/well of 2 kinds of human B-lymphoblastoid cell lines, 30ng/ml of anti-CD3 antibody, and 125 U/mI of IL-2 in total of 150micro 1/well of AIM-V containing 5%AS. 50 micro / well of IL.-2 was added to the medium 10 days later so that IL-2 became 125 U/ml in the final concentration. CTL activity of CTLs was tested on the 14th day, and CTL clones were expanded using the same method above. [0088] Specific CT activity To examine the specific CTL activity, WN-gamma ELISPOT assay and lFN-gamma ELISA assay were performed. Briefly, peptide-pulsed A24-LCL or T2 cell (1x10 4 /well) was prepared as stimulator cells. Cultured Cells in 48 wells or CTL clones after limiting dilution were used as responder cells. IFN-gamma ELISPOT assay and ELISA assay were performed under CflwaenbICA AUH Sf 5,..D oC.WlI t I -42 manufacture procedure. [00891 Establishment of the cells forcibly expressing either or both of the target gene and HLA-A02 or HLA-A24 The cDNA encoding an open reading frame of target genes or HLA-A02 or HLA-A24 was amplified by PCR. The PCR-anplified product was cloned into pcDNA3.1 myc-His vector (Invitrogen). The plasmids were transfected into the target cells, HLA-A02 and HLA-A24 null nomal human cell line COS7 or 293T using lipofectamine (Invitrogen) according to the manufacturer's recommended procedures. Alternatively, the plasmid contained the target genes were transfected into A24-LCL by electroporation using GenePulserli (Biorad). Briefly, 2.5x10 6 A24-LCL cells were pulsed with 10 mg prasrnid at 140V and 1000 micro F. After 2 days from transfection, the transfected cells were treated with Cell dissociation solution and used as the target cells for CTL activity assay. [0090] Cytotoxicity Assay Cytotoxic activity was evaluated by a four-hour 5t Cr release assay. The target cells were pulsed with a 20 micro g/mL concentration of peptide ovemight. The target cells were labeled with 100 micro Ci of Na2'CrO 4 at 37 degrees C for one hour, and then washed three times with RPM1640. The target cells (1x 104/100 micro L) and 100 micro L of effector cells at various numbers with a total volume of 200 micro L were placed into a round-bottomed 96-well microtiter plate (Coining), and cultured at 37 degrees C in a C02 incubator for four hours. After culturing, 100 micro L of the supernatant was collected from each well, and measured the radioactivity using a gamma counter. Spontaneous release was the radioactivity from the target cells with medium in the absence of effector cells, and maximum releasewas the radioactivity from the target cells with 1 M HCL. The Percentage of specific cytotoxicity was determined by calculating as following formula: % Specific lysis = [(experimental release - spontaneous release) / (maximum release spontaneous release)} x100. [00911 RESULTS Enhanced CDH3, EPHA4, ECT2, H102. INHBB, K]F20A, KNTC2, TTK and URLC10 expression in cancers The global gene expression profile data obtained front various cancers using cDNA microarray revealed that the expression of the following genes was elevated. CDH3 (GenBank Accession No. NM_001793; SEQ ID Nos. 1, 2), EPHA4 (GenBank Accession No. L36645; SEQ ID Nos.3, 4), ECT2 (GenBank Accession No. AY376439; SEQ ID Nos.5, 6), HIG2 (GenBank Accession No. NM_01 3332; SEQ ID Nos.7, 8), 43 WO 2008/102557 PCT/JP2008/000290 INHBB (GenBank Accession No. NM_002193; SEQ ID Nos,9, -10), KIF20A (GenBank Accession No. NM_005733; SEQ ID Nos. l, 12), KNTC2 (GenBank Accession No. AF017790; SEQ ID Nos 13, 14), TTK (GenBank Accession No. NM_003318; SEQ IfNos.15, 16) and URLCO (GenBank Accession No. NMv017527; SEQ ID Nos. 17, 18) CDH3 expression was validly elevated in the following cancers in comparison with corresponding normal tissue. 26 out of 34 bladder cancer, 17 out of 19 cervical cancer, 19 out of 19 cholangincellular caminoma, 30 out of 34 colorectal cancer, 20 out of 21 endometriosis, 13 out of 20 gastric cancer, 7 out of 8 diffuse-type gastric cancer, 36 out of 37 NSCLC, 16 out of 16 pancreatic cancer, 21 out of 21 soft tissue tumor and 10 out of 10 testicular tumor [0092] EPHA4 expression was validly elevated in the following cancers in comparison with corresponding normal tissue. 14 out of 34 bladder cancer, 8 out of 14 cervical cancer, 10 out of 25 cholangincellular carcinoma, 5 out of 15 endometriosis, 5 out of 8 diffuse-type gastric cancer, 5 out of 5 ovarian cancer, 14 out of 14 pancreatic cancer, 20 out of 51 prostate cancer and 14 out of 23 soft tissue tumor [0093] ECT2 expression was validly elevated in the following cancers in comparing with corresponding normal tissue. 17 out of 19 bladder cancer, 5 out of 12 breast cancer, 14 out of 14 cervical cancer, 13 out of 13 cholangiocellular carcinoma, 5 out of 5 CML, 7 out of 8 colorectal cancer, 12 out of 16 esophageal cancer, 44 WO 2008/102557 PCT/JP20081000290 6 out of 16 NSCLC, 8 out of 10 lymphoma, I out of 1 pancreatic cancer, 10 out of 13 prostate cancer, 3 out of 6 renal carcinoma and 12 out of 13 SCLC cancer HIG2 expression was validly elevated in 19 out of 20 renal cancer and 7 out of 9 soft tissue tumor in comparing with corresponding normal tissue. INEHB expression was validly elevated in the following cancers in comparing with corresponding nonal tissue. 10 out of 21 cholangiocellular carcinoma, 12 out of 12 esophageal cancer, 10 out of 13 NSCLC, 22 out of 24 renal carcinoma, 8 out of 14 SCLC cancer and 45 out of 49 soft tissue tumor [0094J KIF20A expression was validly elevated in the followingcancers in comparing with corresponding normal tissue. 31 out of 31 bladder cancer, 38 out of 61 breast cancer, 10 out of 11 cholangiocellular carcinoma, 7 out of 19 esophageal cancer, 21 out of 22 NSCLC, 6 out of 6 ovarian cancer, 17 out of 36 prostate cancer, 6 out of 11 renal caminoma and 15 out of 15 SCLC (00951 KNTC2 expression was validly elevated in the following cancers in comparing with corresponding normal tissue. 30 out of 32 bladder cancer, 47 out of 56 brast cancer, 10 out of 10 cervical cancer, 16 out of 22 cholangioncellular carcinoma, 17 out of 37 CML, 3 out of 10 colorectal cancer, II out of 46 esophagus cancer, 15 out of 19 NSCLC, 7 out of 8 lymphoma, 45 WO 2008/102557 pCrJP2008/000290 20 out of 24 osteosawcoma, 3 out of 5 ovarian cancer, 2 out of 2 pancreatic cancer, 15 out of 37 prostate cancer, 14 out of 19 renal carcinoma, 15 out of 15 SCLC and 40 out of 59 soft tissue tumor [0096] TTK expression was validly elevated in the following cancers in compartg with cor - spon4ing normal tissue 27 out of 27 bladder cancer, 25 out of 30 breast cancer, 15 out of 16 cervical cancer, 10 out of 10 cholangiocelIular carcinoma, 5 out of 7 CML, 6 out of 10 colorectal cancer, 24 out of 44 esophageal cancer, 8 out of 15 liver cancer, 12 out of 12 NSCLC, 6 out of 6 lymphoma, 13 out of 16 osteoblastoma, 12 out of 17 prostate cancer, 15 out of 15 SCLC and 16 out of 33 soft tissue tumor [0097] URLC1O expression was validly elevated in the following cancers in comparing with corresponding nonnal tissue 29 out of 29 bladder cancer, 15 out of 16 cervical cancer, 7 out of 7 cholangiocellular carcinoma, 7 out of 19 esophageal cancer, 3 out of 3 gastric cancer, 24 out of 27 NSCLC, 15 out of 19 osteosarcoma, 4 out of 5 pancreatic cancer, 33 out of 43 soft tissue tumor. [00981 46 WO 2008/102557 PCTJP20O8/000290 [Table 1) Ratio of cases observed up-regulation of CDI, EPA4, ECT2, I0G2, INREB, KF204 KNC2, TK oURCO in cancerous tissue as compared to nomal Corresponding tissue - CDH3 EPHA4 ECT2 1IG2 iNURB Bladder cancer 26/34 14/34 17/1 - Breast cancer - - 5/12 - Cervical Cancer 17/19 8/14 14/14 - Cholangloeellularcarcinom 19/19 10/25 13/13 - 10/21 CML - - 5/5 -1 Culectal cancer 30/34 - 7/8 - Eudometriouis 20/21 5/15 - - Esophaeal cancer - '- 12/16 - 12/12 Gastc career 13120 - - - Diffuse-type Gastric cancer 7/8 5/8 Liver cancer - - - - non-small cell lung cancer 36/37 - 6/16 - 10/13 Lymphoma, - 8/10 - Osteosarcoma - - - Ovarian cancer - 5/5 - - Paucreatic cancer 16/16 14/14 1/1 - IProstate cancer - 20/51 10/131 - Renal cardcinoma - - 3/6 19/20 22/24 Small cel Ing cancer - - 12/13 - 8/14 Soft tissue tumor 21/21 14/23 - 7/9 45/49 Testicular tumor 10/10 - - KF2OA KNTC2 TTK URLC1O Bladder cancer 31/31 30/32 27/27 29/29 Breast cancer 38/61 47/56 25)30 Cervical cancer - 10/10 15/16 15/16 Cholanglocellularcarcinom 10/11 16/22 10/10 7/7 ClML - 17/37 5/7 Colecial cancer - 3/10 6/10 Endometriasis - - - Esophageal Cancer 7/19 11(46 24/44 7/19 Gastrie cameer - - - 3/3 Diffuse-te Gastric cancer - - - Liver cancer - - 8/15 non-small cl lung cancer 21/22 15/19 12/12 24/27 Lymphma8 66 Osteosarcoma - 20/24 13/16 15/19 Ovarian cancr- 3/5 - Pancreatic cancer 6/6 2/2 - 4/5 Prostate cancer 17/36 15/37 12/17 Renal carcinoma 6/11 14/19 - Small cell lung cancer 15/15 15/15 15/15 Soft tissue tumor - 40/59 16/33 33/43 Testicular tumor - - - - 47 WO 2008/102557 PCTIJP2008/000290 [0099] Pfdiction of HLA-A24 or HLA-A2 binding- peptides derived from CDH3, EPH . ECT2. HIG2. INBB. KJF2OA, KNTC2, TTK or URLCI0 Table 2 sets forth the HLA-A*2402 binding peptides for CDH3 in order of binding affinity, Table 2A sets forth 9-mer peptides derived from CDH3 and Table 2B sets forth-10-mer peptides derived from CDH3. Table 3 sets forth the HLA-A*2402 and HLA-A*0201 binding peptides for EPHA4 in order of binding affinity. Table 3A sets forth the HLA-A*2402 binding 9-mer peptides derived from EPHA4, Table 33 shows the HLA-A*2402 binding 10-mer peptides derived from EPHA4 and Table 3C sets forth the HLA-A*0201 binding 9-mer peptides derived from EPHA4. Table 4 sets forth the iLA-A*2402 binding peptides for ECT2 in order of binding affinity. Table 4A sets forth 9-mer peptides derived from ECT2 and Table 4B shows 10-mer peptides derived from ECT2. Table 5 sets forth the ELA-A*2402 and HLA-A*0201 binding peptides for HIG2, Table 5A sets forth the HLA-A*2402 binding 9-mer peptides derived from HIG2, Table 5B sets forth the HLA-A*2402 binding 10-mer peptides derived from IG2, Table 5C sets forth the HLA-A*0201 binding 9-mer peptides derived from HIG2, and Table 5D sets forth HLA-A*0201 binding 10-mer peptides derived from HIG2. Table 6 sets forth the HLA-A*2402 and HLA-A*0201 binding peptides for INIBB, Table 6A shows the HLA-A*2402 binding 9-mer peptides derived fromINHRB, Table 6B sets forth the HLA-A*2402 binding 10-mer peptides derived from INHBB, Table 6C sets forth the HLA-A*0201 binding 9-mer peptides derived from INHBB, and Table 6D sets forth HLA-A*0201 binding 10-mer peptides derived from INHBB. Table 7 sets forth the HLA-A*2402 binding peptides for KIF20A in order of binding affinity. Table 7A sets forth 9-mer peptides derived from KIF2OA and Table 73 sets forth 10-mer peptides derived from KIF20A. Table 8 sets forth the HLA-A*2402 binding peptides for KNTC2 in order of binding affinity. Table 8A sets forth 9-mer peptides derived from KNTC2 and Table 8B sets forth 10-mer peptides derived from KNTC2. Table 9 sets forth the IILA-A*0201 binding peptides for TTK in order of binding affmity. Table 9A sets forth 9-mer peptides derived from TTK and Table 9B sets forth 10-mer peptides derived from TK. Table 10 sets forth the HLA-A*0201 binding peptides for URLC10 in order of binding affinity. Table 10A sets forth 9-mer peptides derived from URLC 10 and Table 10B sets forth 10-mer peptides derived from URLC 10. [0100] Explanation and definition about the terms jp tables Start position indicates the number of amino acid from N-terninal. Binding score is derived from "BIMAS" described in Materials and Methods.

4.B WO 2008/102557 PCT/JrZ 00/9007 Positive donor number indicates the number of doner whoes CD8+-T-cells can be induced to the specific CTL by the ex vivo stimulation with antigen-presenting cells. This is shown as (positive donor number /hole donor nember). Positive well number indicates the number of wells where specific IFN-gamma production can be detected by IFN-gana ELISPOT assay. 4 to 8 wells can be prepared from one donor. This is shown as (positive wells number / the number of hole wels tested by IFN-gamna ELISPOT assay). Positve CTL line indicates the number of CIL line established from positive wells. The generation of CTL line is determined by ELISA. This is shown as (established CTL line number /the number of positive wells tested by WN-gamma ELISPOT assay). No positive donor is not defined by no detectable positive wells, but by no established CTL line. The peptides showed by bold character in tables possesses the stimulation activity of the T cells. No data at positive donor number, positive wil number and positive CTL line in dicating "- means that the peptides can't be synthesized for any reason. [0101] 49 WO 2008/102557 PCT/JP20O000290 [Table 2A-1] HL.A-A*2402 bind 9-mer p des deivedifrom CDH3 Sat Amino adid Dinding Polddve Posiive Poslitve SEQ D position sequence Score nubr numer CTL line NO. 513 VYEVLAM 37.5 /319 667 LFLLLVLLL 36 - 20 30 VFRBAEVTL 24 0/3 1/22 0/1 21 406 1LYVEVTNEA 16.632 113 22 332 KYEAHVPEN 16.5 1/22 0/1 23 180 KYBLFGHAV 15 0/3. 1/22 0/1 24 85 RSLKERNPL 14.4 0/3 1/22 0/1 25 5 RGPLASLL 12 0/3 2/22 0/2 26 652 KGGEILPVL 11.2 0/3 0/22 - 27 248 TYNGVVAYS 10.5 0/3 2/22 0/2 28 65 LFSTDNDDF 10 0/3 0/22 - 29 94 KIFPSKlIL 9.6 1Oi 0/8 - 306 221. RGSVLEOVL 9.6 0/1 0/8 - 307 668 FLLLVLLLL .4 - - - 308 754 IGNFUENL 8.4 - - - 309 311 TAVAVVEIL 8.4 0/1 0/8 - 310 557 NQSPVRQVL 8.064 0/1 0/8 - 311 611 KQDTYDVHL 8 o] 0/8 - 312 781 DYEGSGSDA 7.5 a/1 0/8 - 313 165 G-WLLLNKPL 7.2 0/1 0/8 - 314 6D WO 2008/102557 PCT/JZOOB/O00290 [Table 2A-2] 656 ILPVLGAVL 7.2 ] O/ 0/8 - 315 770 TAPPYDTLL 7.2 0/1 0/8 - 316 602 VYLSLKKFL 7.2 0/I 0/8 - 317 665 ALLFLLLVL 7.2 - - - 318 410 VTNBAPFVL 7.2 O/1 0/8 - 319 662 AVLALLFLL 7.2 - - - 320 613 DTYDVHILSL 6,72 0/1 0/8 - 321 6 GPLASLLLL 6 0/1 0/8 - 322 564 VLNITDKDL 6 0/1 0/8 323 159 AVBKBTGWL 6 0/ -0/8 - - 324 511 NNIYEYMVL 6 0/1 ./8 .- 325 11 LLLLQVCWL -6--- 326 57 - GCPOQBPAL 6 0/1 018 - 327 293 BYTLTIQAT 6 0/1 0/8 - 328 79 ETVQERRSL 6 0/1 0/8 - 329 475 SY1ULRDPA 6 0/1 0/8 - 330 493 GQVTAVTL 1 6 0/1 0/8 - 331 661 GAVLALLFL 6 0/1 0/8 332 388 GILTTRKGL 6 0/1 ' /8 - 333 382 HFESNQGIL 6 0/1 0/8 - 334 663 VLALLFLLL 5.76 - - - 335 598. BGDTVVLSL 5.6 0/1 0/8 - 336 278 TISVISSGL 5.6 0/1 218 0/2 337 659 VLGAVLALL 5.6 0/1 0/8 - 338 811 EWGSRFKKL 5.28 0/1 0/8 - 339 445 KVVEVQBGI 5.04 0/1 0/8 - 340 614 TYDVELSLS 5 0/1 0/8 - 341 142 FYSWIPGA 5 0/1 0/8 - 342 246 IYTYNVA 5 0/1 0/8 343 [0102] 51 WO 200810J2557 PCTJP2008/000290 [Table 2B-1] HLA-A*2402 bindig 10-m p desderivedftomCDIB . strat Binding positive positive posiive EQID sequpee, donor Weu poiillEQI position eScore nu r n ber _______ ____________ _____ uber ____ 807 DYLNeWGSRF 150 1/3 30 248 TYNGvVAYSI 105 0/3 4/22 0/4 31 667 ILFLLVLLLL 42 - -- 32 397 DFEAkNQHTL 30 2/22 0/2 33 332 KYEMbVPXNA 21 1/3 34 180 KYELFGHAVS 15 0/3 2/22 0/2 35 510 RNNIYEVMVL 12 0/3 4/22 .0/4 36 5 RCPLASLLLL 12 0/3 1/22 0/1 37 477 RILRDPAGWL 12 0/3 1/22 0/1 38 556 CNQSPVRQVL 10.08 0/3 2/22 0/2 39 655 F"L vLGAVL 8.64 113 344 662 AVLAIFLLL 8.64 - - 345 52 WO 2008/102557 PCT/JF200800290 [Table 2B-21 277 GTISvISSGL 8.4 0/ - 020 - 346 781 DYBGSGSDAA 7.5 0/3 0/20 - 347 601 TVVLUXKFL 7.2 03 3/20 0 348 158 FAVBkETGWL 7.2 0/3 0/20 - 349 665 ALLEILLVLL 7.2 - - - 350 259 SQEPkDPHDL 7.2 D/ 1 0/20 - 351 664 LALIMLLVL 7.2 - .- - 352 42 GABQePGQAL 7.2 03 1/20 0/1 353 661 GAVLaLLFLL 7.2 - .- 354 595 VNEEgDTVVL 7.2 0/2 0/12 - 355 340 NAVGihBVQRL 7.2 0/2 0/12. - 356 411 -TNEApFVLKL 6.6 0/2 0/12 - 357 470 ENQKiSYR1L 6 1/2 358 10 SLLL1QVCWL 6 0/2 1/12 0/1 359 721 GLEArPEVVL 6 0/2 2/12 0/2 360 345 EVQRlTVTDL 6 0/2 4112 0/4 361 2 GLPRgPLASL 6 0/2 3112 0/3 362 657 LPVLgAVLAL 6 - - 363 563 QVLNiTDKDL 6 0/2 1/12 0/1 364 159 AVBKCTGWLL 6 0/2 2/12 0/2 365 492 SGQVtAVGTL 6 0/2 - - 366 387 QGILTRKCOL 6 0/2 - - 367 525 SPP1GTGTL 6 0/2 2/12 0/2 368 358 NSPAwRATYL 6 0/2 2/12 0/2 369 122 IFPqRLNQL 5.76 0/2 3/12 0/3 370 753 EIGNffMBNL 5.6 0/2 1/12 0/1 371 310 TTAVa&VVEIL 5.6 - - - 372 246 IYTYnWVAY 5 0/2 2/12 0/2 373 805 DYDY1NEWS 5 0/2 0/12 ..- 374 [0103] 53 WO 2008/102557 PCT/Jr2008/IO1290 [Table 3A] HLA-A*2402 binding 94nw pieces derived fromEPH4 Pte ctive pusidve posidve SEQ U) psitin Soe CTL He NO mequene Number 97 VYBIlTL 504 0/2 1/16 Oil 40 453 RYSVALAWL 400 | 13 41 25 VYPANBYTL 300 0S 0/22- 42 384 HYTPQQNGL 288 013 1/22 0/1 43 5 FFALFSCL 288 M3 44 519 GYGDFSE L 240 0/3 3/22 0/3 45 869 -KFGQIVNML 67.2 11- 46 777 AYTTRGGI 55 08 1/22 0/1 47 420 KYNPNPDQS 18 1a 48 749 RNILVNSNL 16.8 03 1/22 0/1 49 734 KYLSDMSYV 15 03 0/22 - 50 879 KLlRNPNSL 14.4 0/3 0/22 - 51 926 RYKDNFTAA 14.4 013 0/22 - 52 834 KAIBEGYRL 14.4 013 0/22 - 53 574 KYSIkAXQBA 13.2. 0/3 0/22 - 54 184 AFQDVGACI 12.6 08 1/22 0/1 55 252 WLVPIGNCL 12.096 013 0/22 - 56 326 RPPSAPLNL 12 0/3 0/22 - 57 203 KCPLTVRNL 12 0/3 0/22 - 58 360 SYNVVCKKC 11.55 03 0/22 - 59 [01041 54 WO 2008/102557 PCT/JPZOOS/00a290 [Table 3E] HLA-A*2402 bind 10-er pptides derived from EPHA4 strat sequel Mtive p SEQ ID position Scorenuber uHmbre NO 25 VYPANEVTLL 300 0/3 0/22 - 60 244 MYCGADGEWL 200 013 1/22 0/1 61 657 GYTDKQRRDF 120 0/3 1/22 6/1 62 5 FYAMFCLF 100 --- 63 102 KFTLRDCNSL 48 0/3'- 122 0/1 64 818 SYGERPYWDM 30 0/3 2/22 0/2 65 4 IFWYALFSCL 28.8 - - - 66 808 SYGIVMWEVM 25 - - - 67 630 EFGEVCSGRL 24 0/3 0/22 - 68 420 KYNPNPDQSV 21.6 0/3 0/22 - 69 930 NFTAAGYTTL 20 0/2 0/16 - 70 675 QFDBPNHL 20 0/3 0/22 - 71 708 AFLRKNDGRF 15 0/3 0/22 72 579 KQEADEEKHL 12 013 1/22 0/1 73 727 RGIGSGMKYL 12 0/3 0/22 - 74 96 RVYIEIFTL 11.2 0/2 1/16 0/1 75 507 SYVPHVRART 10.5 0/3 [/22 0/1 76 251 EWLVfIGNCL 10.08 0/3 0/22 - 77 24 RVYPANEVTL 9.6 1/3 78 699 EYMENGSLDA 9 0/3 0/22 - 79 [01051 [Table 3C] HLA-A*0201 bindg 9-mr peptides derived from EPHA4 strat Binding poe p positive SEQ ID position sequence Score nmr. imer CTL 4ige NO - number iue 8 -ALFSCLFQI '514.942 - 375 501 GLNPLTSYV 382.536 1/1 376 12 CLFGICDAV 126.098 0/1 1/5 0/1 377 977 QMIHGRMVPV 115.534 0/1 115 0/1 378 165 KLNTERDV 111.979 1/1 379 252 WLVPIGNCL 98.267 0/1 1/5 0/1 380 879 KLRNPNSL 74,768 . 0/1 1/5 0/1 381 559 VVRJAAFV 56.902 - - - 382 812 VMWEVMSYG 39.386 0/1 0/5 - 383 728 GIGSGMKYL 37.157 0/1 015 - 384 750 NILVNSNLV 35.385 0/1 1/5 0/1 385 937 TTLEAVVHV 33.705 0/1 1/5 01 386 [0106] 55 WO 2008/102557 PCT/JP2008/000290 [Table 4A] HLA-A*2402 bindg 9nr ppides derived f-om ECT2 start Binding positive psitive positive SEQ ED position sequence Score donor well CL ine NO number number 515 TYPPFVNFF 216 1/1 80 140 LYCTSMMNL 200 0/1 0/8 - 81 298 LYVVKQEWF 150 0/1 0/8 - 82 435 NYVN.UATI 105 0/1 0/8 - 83 773 IYTADPESF 100 0/1 0/8 - .84 110 LYKADCRVI 50 0/1 0/8 - 85 739 SFQMTSDEL 33 0/1 0/8 - 86 504 IFLKYSrDL 30 0/1 0/8 - 87 867 FFERRSHTL 30 0/1 0/8 - 88 178 DFNSKVTHL 30 0/1 0/8 - 89 61 KQBBLIKAL 17.28 0/1 0/8 - 90 657 RGEQVTLFL 16.8 0/1 2/8 0/2 91 568 RLPSVALLL 16.8 0/1 0/8 - 92 550 KPECGRQSL 14.4 0/1 0/8 - 93 470 IFuSIPD)F 14 0/1 0/8 - 94 116 RVIGPPVVL 12 0/1 0/8 - 95 507 KYSKDLVKT 11 0/1 0/8 - 96 223 DFYAAVDDF 10 0/1 0/8 - 97 [01071 [Table 4B] HLA-A*2402 binding 10-mer pe tides delved from ECT2 PSIC positiveI strat Binding o well positive SEQ ID position Score CTL line NO 322 LYEKaNTPEL 330 0/1 0/8 - 98 435 NYVNLATII 90 0/1 0/8 - 99 40 SYVEeEMPQI 90 1/1 100 101 DFQDPVFNDL 72.576 1/1 101 866 SFFBrRSHTL 24 0/1 0/8 - 102 811 SFSKtPKRAL 20 01l 1/8 0/1 103 260 KYLPIGDERC 18 i 0/8 - 104 84 EFEGIDSPEF 16,5 / 118 0/1 105 236 KVPPfQDCIL 14.4 0/1 0/8 - 106 72B IPPTeQANVL 14.4 0/1 0/8 - 107 507 KYSKdLVKTY 12 0/1 0/8 - 108 281 VVEEnIVKDL 10.08 W/1 0/8 - 109 [01081 56 WO 2008/102557 PC/JP2008/000290 [Table 5A] HLA-A*24d2 b 9-mer pepis derivedfromrG2 trat s BindingPositive positive SEQ ID position Score donor Well CTL line NO number number 19 IFVRVMESL 42 1/3 110 22 RVMESLEGL 14.4 1/3 111 8 YLEGVVLTL 8.4 1/3' 387 7 LYLLGVVLT 7.5 0/2 3115 0/3 388 23 VMESLBGLL 7.2 0/2 0/16 - 389 9 LLGVVLTLL 5.6 - - - 390 [0109] [Table5B] Table 5B .HLA-A*242hinding o-merp tides dived frovm G2 sat sBinding positive Positive positive SEQ ID strutD~ sequence Bicdin donor wenl CIL line NO position Score number number 7 LYLLGVVLTL 420 13 112 22 $.VMESLELL 17.28 Q/3 4/24 0/4 113 8 YLLGVVLTLL 8.4 - - - 391 5 LNLYLLGVVL 72 0/2 0/12 - 392 46 LANTEPTKGL 6 0/2 0/14 - 393 18 SIFVRVMESL 5.6 1/2 394 [0110] [Table 5C] HLA-A*0201 binding 9-mr Pepti derived from 1G2 strat Binding Positive positive positive SEQ ID position sequence Score donor well CTL line NO ouster number 8 YLLGVVLTL 836.253 I/ 114 13 VLTLLSIPV .650.311 0/1 0/12 - 115 15 TLLSIFVRV 488.951 1/1 116 4 VLNLYLLGV 271.948 1/1 117 9 LLGVVLTLL 83.527 0/1 0/12 - 118 22 RVMESLEGL 31.957 0/1 0/12 - 119 6 NLYLLGVVL 28.027 0/1 0/12 - 120 [0111] 57 WO 2008/102557 PCT/JP2008/000290 [Table 5D] ULA-A*0201 bindin 10-mcr peptides derived fromMIG2 strat eunc positive positive SE position sequence donor well CTL line NO number number 8 YLLGvVLTLL 836.253 111 121 12 VVLTILSIFV 210.538 - - - 122 29 GLLEsPSPGT 113.047 0/1 0/12 - 123 6 NLYLGVVLT 54.847 - - - 124 4 VLNLyLLGVV 14.495 0/1 0/12 - 125 15 TLLSWFVRVM 13.174 0/1 0/12 - 126 18 SIFVrVMBSL 12.248 0/1 0/12 - 127 14 LTLLsIFVRV 1L545 - - - 128 {0112] [Table 6A] ILA-A*2402bin 9-mer peptides drived from INfRBB strat Binding positive positive positive SEQ ID position Store number number CTL line NO 383 LYDDBYNI 60 0/3 0/20 - 129 238 LFERERRL .30 0/3 1/19 W/ 30 7 RALGAACLL 12 0/3 0/21 - 131 388 EYNLVKRDV 10.5 0/3 0/18 - 132 180 LYIMLPYV 9 M2 395 163 ISNEGNQNL 8.64 0/1 0/8 - 396 223 RSOWRTFPL 8 0/1 0/6 - 397 176 ASLWLYLKL 7.92 0/1 0/7 - 398 338 AYLAGVPGS 7.5 . 0/1 1/7 Oi 399 213 NMVEKRVDL 7,2 0/1 0/8 - 400 102 -AMVTALRKL - 6.6 0/1 W/8 - 401 250 VQCDSCQEL 6.336 0/1 0/8 - 402 369 NSCCIPTKL 6.16 0/1 0/8 - 403 330 NYCEGSCPA 6 0/1 /7 .- 404 172 FVVQASLWL 6 0/1 0/8 - 405 355 VNQYRMRGL 6 0/1 0/8 - 406 307 QFFIDFRLI 6 0/1 OtT - 407 14 LLLLAAGWL 6 - - - 408 306 QQFFIDFRL 5.6 0/1 0/6 409 170 NLFVVQASL 5.6 Oi 0/7 - 410 327 YY&NYCEGS 5 0/1 1/8 W/ 411 [0113] 58 WO 20081102557 PCT/JP2008/00290 [Table 6B] , HLA-A*2402 binding 10-mer petides derived ftom MIBB . strat Bequeno awtve posie ke SEQ ED posiion cor ninnberI number N I8O LYLKLLPYVL 360-- a 1/ 133 171 -LFVVQASLWL 3D' -- 134 305 RQQFFIFRL_ 16.8 113 135 73 DFLEAVXRHI .12.6 0/3 4/20 014 136 7 RALGAACLLXL 12 13 - 137 273 RPFVVVQARL 11.2. 0/3 1/20 0/1 138 338 AYLAGVPGSA 10 W3 2/20 0/2 139 169 QNLPvVQASL . 8.4 0/1 1/6 0/1 412 249 DVQCdSCQBL 7.92 01 416 0/4 413 173 VVQAsLWLYL 7.2 Wi 0/6 414 383 LYFDdEYNIV 7,2 0/1 0/6 - 415 229 FPLTeAIQAL 7.2 0/1 1/6 0/1 416 299 RTNLOCRQQF 7.2- 6/1 516 0/5 417 101 AAM tALRKL 6.6 0/1 2/6 0/2 418 368 VNSCcIPTL 6.16 0/1 2/6 02 419 13 CLLLIAAOWL 6 - - - 420 354 VVNQyRMRGL 6 0/1 0/6 - 421 150 DGLASSRVRL 6 0/1 2/6 0/2 422 293 GLECdGRTNL 6 0/1 0/6 423 330 NYCBgSCPAY 6 0/1 1/6 0/1 424 176 ASLWZYLKLL 6 0/1 1/6 0/1 425 212 WNMVeKRVDL 6 11 426 74' PLAvKRHIL 6 0/1 2/6 0/2 427 331 YCBGsCPAYL 6 0/1 1/6 0/1 428 77 AVKRIiLSRL 5.6 0/1 1/6 0/1 429 175 QASLWLYLKL 5.28 0/1 2/6 0/2 430 326 GYYGnYCEGS 5 0/1 16 0/1 431 159 LYFISNEGN 5 0/1 4/6 0/4 43,2 327 YYGNyCEGSC i 5 0/1 1/6 0/1 433 [01141 59 WO 20081102557 PCT/JM200O000290 [Table 6C] HLA-A*0201 binding 9-mer peptides derived from )NIBBB strt ining positive positive positive SEQ ID position dOre onor wer CTL line NO ________ ________ number 'number ___ ____ 177 SLWLYLKLL 407.08 0/1 018 140 14 LLLLAAGWL 96.074 - - - 141 170 NLFVVQASL 79.041 011 0/8 142 213 NMVEKRVDL 63.256 0/1 0/8 143 172 FVVQASLWL 47.291 0/1 0/8 144 306 QQFFIDFRL 4648 0/1 0/8 145 281 RLQDSRHRI 42.774 0/1 U/S 146 174 VQASLWLYL 34.427 0/1 0/8 147 257 ELAVVPVFV 28.69 0/1 1/8 0/1 148 313 RLIGWNDWI 28.116 0/1 1/8 0/1 149 139 RVSBITSFA 22.546 0/1 3/8 0/3 150 151 eLASSRVRL 21.362 0/1 0/8 151 8 ALGAACLLL 21362 0/1 118 0/1 152 250 VQCDSCQEL 15.096 0/I 1/8 0/1 153 [0115] [Table 6D] HLA-A*0201 binding 10-mr ye >tides derived fmaMBHBB strat Binding positive Positive positive SEQ ID Position sequence Score door we CTLlie NO number numberI 179 WLYLKLLPYV 12951.1 0/1 1/8 0/1 154 301 NLCCRQQFFl 332.806 0/1 0/8 155 237 ALFERGERRL 64.814 0/1 0/8 156 382 MLYFDDEYNI 56.754 0/1 0/8 157 13 CLLLLAAGWL 56.514 - - - 158 8 ALGAACLLLL 49.134 - - - 159 313 RLIGWNDWII 32,081 0/1 0/8 160 173 VVQASLWLYL 29.711 0/1 2/8 0/2 161 256 QBLAVPVFV 27.521 0/1 0/8 162 162 FISNEGNQNL 13.512 0/1 1/8 0/1 163 30 RQQFFIDFRL 12.562 0/1 0/8 164 362 GLNPGTVNSC 11.426 0/1 0/7 165 85 RLQMRGRPNI 10.433 0/1 1/8 01 166 69 RVDGDFLEAV 10.425 0/1 0/8 167 [0116] 6D WO 2008/102557 PCT/JF2008/000290 [Table 7A] ELA-A*2402 W 9-mer pptides derived ftoan 2F204 ratBindig positive positive positive SEQ ID position Sequence Score nnmer Dumber CTL line NO 308 IYNELLYDL 432 0/2 0/14 - 168 621 MYENIL 432 0/2 0/14 - 169 67 VYLRVRPLL 420 0/2 0/14 - 170 499 KFSAIASQL 56 0/2 0/14 - 171 304 SFFEIYNEL 44.352 0M 0/14 - 172 187 IFNSLQQL 36 0/2 0/14 - 173 305 FFOMYNLL 1 30 1/2 174 23 MFBSTAADL 30 0/2 0/14 - 175 256. SFDSGIAGL 20 0/2 0/14 - 176 298 RFS1WJSFF 20 - - - 177 383 1 FSIRILHL 20 1/a 178 647 KIEELALL 17.28 0/2 0/14 - 179 625 KLNILKESL 14.4 0/2 0/14 - 180 695 KLQQCKAEL 13.2 0/2 0/14 - 181 726 FTDVDKKL 11.088 0/2 0/14 - 182 688 QLQEVKAKL 11.088 D/2 0/14 - 183 [0117] [Table 7B$ HLA-A*2402 binding 10-mer peptides derived fromKIF20A strat Binding p~dtive positive positive SEQ ID position sequence Score. number number CT lime NO 308 IYNEILYDLL 432 0/2 0/14 - 184 182 RSLAILFNSL 24.192 0/2 1/14 W/I 185 304 SFFENELL 24 12 186 742 RLLRtBLQKL 15.84 D/2 0/14 . 187 739 KNIRLRTEL 15.84 0/2 0/14 - 188 218 RQEEmKKLSL 14.4 02 2/14 0/2 189 70 RVRPILPSEL 12.672 0/2 0/14 - 190 871 RILRsRRSPL 12 0/2 0/14 - 191 89 RIENyBTLVL 12 0/2 1/14 0/1 192 364 KNQSfASTHL 12 0/2 0/14 - 193 66 KVYLrVRPLL 11.2 1/2 194 60 DSMEkVKVYL 10.08 o 0/14 - 195 [01181 61 WO 2008/102557 PCTJPOGS/000290 [Table 8A] HLA-A*2402 biding 9-iner petides derived fim 1N7C2 strat s nBinding positv positive SEQ D Ustin qene D~e donor Well CTL fine NO position Score number number 309 KYQAYMSNL 600 113 196 457 VYVPLKELL 432 D3 0/18 - 197 414 EYHKLARKL 264 0/3 0/18 - 198 139 SYELPDTKF 165 03 0/18 - 199 629 KYEKKATLI 150 0/3 0/18 - 200 400 KYARGKBAI 100 0/3 1/28 0/1 201 124 DFIUTffL 50.4 1 202 134 GFLOPSYEL 33 0/3 0/18 203 257 LFNVDAFKL 33 073 048. - 204 242 SFDBMNAEL 26.4 0/3 0/18 - 205 128 XFTFLYGFL 24 D3 0/18 - 206 146 ICFBEEVPRI 18 /3 1/18 0/1 207 368 RINHERNEL 15.84 0/3 .1118. 0/1 208 235 SFMSGADSF 15 03 0/18 - 209 154 WKDLGVPF 14.4 1/3 210 563 EYQLVVQTT 12.6 0/3 0/1 - 211 474 KALNIKKMGL 12 /3 1/18 01 212 150 EVPRIWKDL 10.08 1----T 213 [0119] [Table SB] HLA.-A*2402 binding 10.-mer tides derived from ENC2 strat Binding positive positive p S position sequence Score CTL line NO I number number 452 KYRAQVYVEL 560 2M 214 610 EYEECMSEDL 360 0/3 1/18 0/1 215 360 KYSVADERI 100 0/3 0/18 - 216 227 DYTIKCYESF 100 13 217 146 KFEEEVPRIF 50.4 0/3 0/18 - 218 90 APIQQCIRQL 30 0/3 0/18 - 219 20 RSQDVNKQGL 17.28 0/3 1/18 0/1 220 501 RTLKEEVQKL 15.84 0/3 0118 - 221 403 RGKEAIETQL 13.44 0/3 1/18 0/1 222 273 RALNEQLARL 12 1/3 223 563 EYQLVVQITT 10.5 0/3 3/22 0/3 224 467 ETBBEINKAL 10.08 0/3 1/22 0/1 225 541 LLESTVNQGL , 10.08 0/3 1/22 0/1 226 [01201 62 WO 2008/102557 PCT/JoR/000O [Table 9A) HA-*0201 idng9-mer pueptides.drived from ITK strat Bding Positive posited positive SEQ ID posdeon seq"en** score doorm CTL lIne NO 462, YMscRTry k78.-55 1 227 547 KQ)YAIXYV 312,218 -11 228 630 NMLBAVHEU 262,897 0/1 1/8 0/1 229 278 ILNSaDCDV 1.1.23S 0/1 1/8 0/1 230 498 ILATPJQNL 83.527 0/ 0/8 .231 811 YVLGQLVGL 73172 01 08 - i232 719 SLGCILYM- 62.845 1 233 670 , QMQPDTSV 50.232 6/1 0/8 - 234 804 OTTEEMKYV 50.162 0/1 0/8 - 235 654 L1VOMLKL 47.088 0/1 1/8 W/ 236 363 SLLAKLBBT 31.074 0/1 0/8 - 237 790 YVQIQTHPV 27.995 0/1 0/8 238 785 LLAHPYVQI 26.604 0/1 0/8 - 239 86 KLIGRYSQA 26.082 0/1 0/8 - 240 186 NLNLQKKQL 21.362 0/1 0/8 - 241 671 MQPDTTSVV 20.152 0/1 0/8 - 242 577 KLQQHSDI 17.892 0/1 0/8 - 243 142 FAFVHISFA 14.856 0/1 0/8 - 244 322 CELRNLKSV 11,509 0/1 0) - 245 824 SIKAAKTL 10.868. 0/1 0/S - 246 [0121] 63 WO 2008/102557 PCT/JP28/000290 [Table 9B rULA-A*0201 binding 10-mer peptides derived from ITK strat .e Bnding posidve positive positive SEQ ID poton sequence Sn donor we o CTLive NO number number 68 LLLKLEKNSV 437.482 0/1 0/8 - 247 277 NLLNSPDCDV 257.342 0/1 0/8 - 248 653 FLVDGMLKCL 226.0i4 0/1 0/s - 249 423 T'PEQPVFSV 195.487 0/1 . /8 - 250 542 VLNEKKQIYA 19O.448 0/1 08 251 658 GMLCLIDFOI 161.697 0/1 0/8 - 252 194 LLSBBBKKNL 148.896 0/1 O/8 - 253 462 . YMSCFRTPVV 94.738 i/ 254 57 MMANNPEDWL 70.685 0/1 0/8 - 255 600 MVMECGNIDL 48.205 0/1 /S - 256 689 YMIPPBAIKDM 37.961 0/1 0/8 - 257 86 KLIGRYSQAI 36.515 0/1 0/8 - 258 669 NQMQPDTTSV 26.092 0/ 1/8 0/1 259 497 Q]iATPLQNL 24,997 0/1 0/8 - 260 654- LIVDGMLKLI 22.997 0/1 0/8 - 261 186 NLNLQKKQLL 21.362 0/1 1/8 0/1 262 670 QMQPDMSVV 20.595 0/1 0/8 - 263 803 KGTTEEMKYV 20.102 0/1 0/8 - 264 11 LTJDSIMNKV 15.486 0/1 0/8 - 265 577 KLQQHSDKJ 14.971 0/1 0/8 - 266 [0122] 64 WO 2008/102557 PCT/JP200/000290 [Table 10A] HLA-A*0201 binding 9-mer p des dedved from URLCIO strait Bpositive posidve py tv SEQ ED poston sequence Rhding donor well C'lline NO position Score number number 131 KIFPRFFMV 1364.78 0/1 0/8 - 267 204 GLWLAILLL 407.808 0/1 0/8 - 268 65 LLVVALPRV 271.948 0/1 0/8 - 269 60 ALLALLLVV 242.674 - - . 270 2M6 WLAILLLA 52.61 1/1 271 212 LLASIAAGL 36.316 / 272 210 LLLLASIAA 31249 0/1 0/8 - 273 137 FMVAKQCSA - 16.505 0/1 2/8 0/2 274 58 TMALLALLL 15.428 0/1 2/8 0/2 275 59 MALLALILV 13.975 0/1 2/8 0/2 276 209 ILLLLASIA 12.812 0/1 0/8 - 434 208 AILLLLASI 12,208 - - - 277 69 ALPRVWTDA 8.446 0/1 0/8 -- 278 197 SMGESCGGL 8.223 0/1 0/8 - 279 61 LLALLLVVA 7.964 - - - 280 67 VVALPRVWT 6.097 0/1 0/8 - 281 72 RVWTDANLT 5.412 0/1 0/8 - 282 160 FLLBEMPPF 5.2 a/1 1/8 0/1 283 62 LALLLVVAL 4.292 0/1 0/8 - 284 57 GTMALLALL 2.525- 0/1 1/8 0/1 285 [0123] 65 WO 20081102557 PCT/fP2008/000290 [Table 10B] BILA-A*0201 binding 10-mer tides deved from URLCI0 strat Biuding positive positive SEQ D position seuenc Score uoner nu er CL aHe NO 64 LLLVVALPRV 1006.21 01 0/8 - 286 204 GLWLAILLLL 407.808. 0/L 118 O/l 287 21l LLLASIAAGL 134369 1/1 288 258 TMALLALLLV 115.534 - - . 289 61 LLALLLVVAL 83.527 - - - 290 160 FLLBPMPFP 65.782 011 0/8 - 291 209 ILLLLASIAA 31.249 Oil 018 - 292 131 KJFPRFFMVA 26.186 oi 0/8 .- 293 60 ALLALLLVVA 17.334 - - 294 66 LVVALPRVWT 6.097 0/l 0/8 - 295 59 MALLALLLVV 5.73 - - - 296 2 RLQRPRQAPA 4,968 0/1 1/8 0/1 297 112 CQNPRRCKWT 4.156 0/1 0/8 - 298 72 RVWTDANLTA 3.608 0/1 0/8 - 299 53 WAPLGTMALL 3.139 0/1 0/8 - 300 121 TEPYCVIAAV 3.111 0/1 0/8 - 301 162 LEEPMPFFYL 2.739 Ol 1/8 i 302 181 LEPPUNSSV 2.299 0/1 2/8 0/2 303 170 YLKCCKIRYC 2.024 0/1 0/8 - 304 130 VKFPRFFMV 1.81 0/I 0/8 - 305 [0124] Stimulation of the T cells using the predicted peptides frQm CDH3 restricted with HLA-A*2402 and establishment for CTL lines stimulated with CDH3 derived peptides CTLs for those peptides dedved from CDH3 were generated according to the protocols set forth in "Materials and Methods" section above. Resulting that CTLs having detectable specific CTL activity, as determined by IFN-gamma ELISPOT assay, are shown in Figure 1. In particular, CDH3-A24-9-513 (SEQ ID NO: 19), CDH3-A24-9-406 (SEQ ID NO: 22), CDH3-A24-10-807 (SEQ ID NO: 30), CDH3-A24-10-332 (SEQ ID NO: 34), CDH3-A24-10-655 (SEQ-ID NO: 344) and CDH3-A24-10-470 (SEQ ID NO: 358) demonstrated potent IFN-gamma production as compared to the control by IFN-gamma ELISPOT assay, and the cells in the positive well number #5 stimultaed with SEQ MD NO: 19, #2 with SEQ ID NO: 22, #5 with SEQ ID NO: 30, #4 with SEQ ID NO: 34, #1 with SEQ ID NO: 344 and #4 with SEQ ID NO: 358 were expanded and CTL lines were established. Those CTL lines having higher specific CTL activities against the peptide-pulsed target as compared to the activities against target without peptide pulse were determined by ELISA. Results are shown in Figure 1. While, other peptides shown in table 2 could not establish the CTL 66 WO 2008/102557 PCT/JP2008/000290 lines despite possible binding activity with HLA-A*2402. For example, the tipical negative peptide (CDH3-A24-10-248) were shown in Figure Ia. In this invention, th e peptiedes which could establish CTL line were selected as potent CTL stimulation peputide. [0125] Establishment for CTL clones stitulated with CDH3 derived pepjides Furthermore, the limiting dilution from these CTL lines was performed according to the protocols set forth in the "Materials.and Methods" section above. The estab lishment of CTL clones from CDH3-A24-10-807 (SEQ ID NO: 30) #5 and CDH3-A24-10-655 (SEQ ID NO: 344) #1 CTL line are shown in Figurelf and g. CTL clones had potent and specific CTL activities against the peptide-pulsed target as compared to the activities against target without peptide pulse. .[01261 SpeQific CTL activity against the target cells exressing CDH3 and HILA-A*2402 The established CTL line raised against these peptides were examined for their ability to recognize the target cells expressing CD=U and HLA-A*2402. Specific CTL activity against C087 transfected with both full length CW gene and the HLA A*2402 molecule, which serves as a specific model for the target cells endogenously expess CDH3 and HLA-A*2402, was tested using as effector cells the CTL lines raised by CDI3-A24-10-807 (SEQ ID NO: 30) and CDH3-A24-10-655 (SEQ ID NO: 344). COS7 transfected with full length £D33l but not fHLA-A*2402 and COS7 transfected with HLA-A*2402 but not full length CDH3 were prepared as controls. The CTL clones demonstrating the highest specific CTL activity against COS7 was that transfected with both CDH3 and HLA-A2402 (Figure If and g). These results clearly demonstrate that CDR3-A24-10-807 (SEQ ID NO: 30) and CDH3-A24-10-655 (SEQ ID NO: 344) are naturally expressed on the target cell surface with HLA-A2402 molecule and recognize CTL. Furthermore, these peptides are epitope peptides, which may serve as cancer vaccines targeting CDH3 expressed tumors. [0127] Stiulation of the T cella using the predicted peptides fronEPHA4 restricted with HLA-A*2402 or HLA-A*0201. and establishment for CTLines stimulated with EPHA4 derived petides CTLs for those peptides derived from EphA4 were generated by FN-gawma ELISPOT assay. Resulting that CTLs having detectable specific CTL activity , as de termined by IFN-gamma ELISPOT assay, are shown in Figure 2. In particular, EphA4-A24-9-453 (SEQ I) NO: 41), EphA4-A24-9-5 (SEQ ID NO: 44), EphA4-A24-9-869 (SEQ ID NO: 46), EphA4-A24-9-420 (SEQ ID NO: 48), EphA4-A24-10-24 (SEQ ID NO: 78), EphA4-A02-9-501 (SEQ ID NO- 376) and EphA4-A02-9-165 (SEQ ID NO: 379) demonstrated potent IFN-gannma production by IFN-gamma ELISPOT assay, and the cells in the positive well number #3 stimultaed - 67 with EphA4-A24-9-453 (SEQ ID NO: 41), #2 with EphA4-A24-9-5 (SEQ ID NO: 44), #5 with EphA4-A24-9-869 (SEQ ID NO: 46), #6 with EphA4-A24-9-420 ($Q JD NO: 48), #4 with EphA4-A24-10-24 (SEQ ID NO: 78), #8 with EphA4-A02-9-501 (SEQ ID NO: 376) and #3 with EphA4-A02-9-165 (SEQ ID NO: 379) were expanded and CTL lines were established. Those CTL lines having higher specific CTL activities against the peptide-pulsed target as compared to the activities against target without peptide pulse were determined by ELISA. Especially, CTL lines stimulated with EphA4--A02-9-501 (SEQ ID NO: 376) and EphA4-A02-9-165 (SEQ ID NO: 379) were tested by 51Cr-release assay according to the protocols set forth in the "Materials and Methods" section above, Results are shown in Figure 2a-h. While, other peptides shown in table 3 could not establish the CTL lines despite possible binding activity with HLA-A*2402 or HLA A*0201. For example, the typical negative peptide (EphA4-A24-9-384) were shown in Figure 2a. In this invention, the peptides which could establish CTL line were selected as potent CTL stimulation peptides. [0128] Stimulation of the T cells usina the predicted peptides from ECT2 restricted with HLA-A*2402, and establishment for CTL lines stimulated with ECT2 derived peptides CTLs for those peptides derived from ECT2 were generated according to the protocols set forth in the "Materials and Methods" section above. Resulting CTLs having detectable specific CTL activity as determined by an IFN-gamua ELISPOT assay are shown in Figure 3. In particular, ECT2-A24-9-515 (SEQ ID NO: 80), ECT2-A24-10-40 (SEQ ID NO: 100) and ECT2-A24-10-101 (SEQ ID NO: 101) showed potent IFN-gamma production, and the cells in the positive well number #7 stimulated with EC'2-A24-9-515 (SEQ ID NO: 80), #2 with ECT2-A24-10-40 (SEQ ID NO: 100) and #1 with ECT2-A24 10-101 (SEQ ID NO: 101) were expanded and CTL lines were established. Those CTL lines having higher specific CTL activities against the peptido-pulsed target as compared to the activities against target without peptide pulse were determined by ELISA. Results are shown in Figure 3a-d. While, other peptides shown in table 4 could not establish the CTL lines despite possible binding activity with HLA-A*2402. For example, the typical negative peptide (ECT2-A24-10-322, ECT2-A24-9-657 and ECT2-A24-10-81 1) were shown in Figure 3a. In this invention, the peptides which could establish CTL line were selected as potent CTL stimulation peptide. [0129] Establishment for CTL clones stimulated with ECT2 derived peptides Furthermore, the limiting dilution from these CTL lines was performed according to the protocols set forth in the "Materials and Methods" section above. The establishment of CTL clones from ECT2-A24-10-40 (SEQ ID NO: 100)#2 CTL line are shown in Figure 3c. CTL clones had potent and specific CTL activities against the peptide-pulsed target as compared to the activities against target without peptide pulse.

BB WO 200/102557 PCTJP2008/000290 [0130] Secifc CTL ivi against the tamet cells expressing ECT2 and HLA-A*24_2 The established CTL line raised against these peptides were examined for their ability to recognize the target cells expressing ECT2 and HLA-A*2402. Specific CTL activity against COS7 transfected with both full length ECT2 gene and the HLA A*2402 molecule, which serves as a specific model for the target cells endogenously express ECT2 and HLA-A*2402, was tested using as effector cells the CTL clone raised by ECT2-A24--10-40 (SEQ ID NO: 100) and the CTL line raised by ECT2-A24-10-101 (SEQ ID,NO: 101). COS7 transfected with full length ECT2 but not HLA-A*2402 and COS7 transfected with HLA-A*2402 but not full length ECT2 (replaced other gene e.g. URLC10 or MHBB) were prepared as controls. The CTL line demonstrating the highest specific CTL activity against COS7 was that transfected with both ECT and HLA-A2402 (Figure 3c and d). These results clearly demonstrate that ECr2-A24-10-40 (SEQ ID NO: 100) and ECT2-A24-10-101 (SEQ ID NO; 101) are naturally expressed on the target cell surface with HLA-A2402 molecule and recognize CTL. Furthermore, these peptides are epitope peptides, which may serve as cancer vaccines targeting ECT2 expressed tumors. [0131] Cytotoxc activity against cancer cell line endogenously expressing HLA-A*24O2 and ECT Furthermore, Cytotoxic activity was performed by cytotoxicity assay according to the protocols set forth in the "Materials and Methods" section above. As a result, as shown in Fig. 3b, CTL clone stimulated with ECT2-A24-9-515 (SEQ ID NO: 80) showed remadkably high cytotoxic effect towards HLA-A24-positive and ECT-positive cancer cell lines TE6, compared to that towards HLA-A24-negative and ECT-positive cancer cell lines TE5. [0132] Stimulationf the T cells using the predicted peptides from HG2 restricted with HLA-A*240_or HLA-A*020L and establishment for CT lines stimulated with HIG2 CTLs for those peptides derived fromH G2 were generated according to the protocols set forth in the "Materials and Methods" section above. Resulting CTLs having detectable specific CTL activity as determined by an IN-gamma ELISPOT assay are shown in Figure 4. In particular, HIG2-A24-9-19 (SEQ ID NO: 110), HIG2-A24-9-22 (SEQ ID NO: 111), HIG2-A24-9-8 (SEQ ID NO: 387), FHG2-A24-10-7 (SEQ ID NO: 112), HIG2-A24-10-18 (SEQ ID NO: 394), HI02-A02-9-8 (SEQ ID NO: 114), IG2-A02-9-15 (SEQ ID NO: 116), HIG2-A02-9-4 (SEQ ID NO: 117) and HIG2-A02-10-8 (SEQ ID NO: 121) demonstrated potent IFN-gamma production by IFN-gamma ELISPOT assay, and the cells in the positive well number #6 stimultaed with H[G2-A24-9-19 (SEQ ID NO: 69 WO 2008/102557 PCT/JP20B/000290 110), #7 wit HIG2-A24-9-22 (SEQ ID NO: 111), #5 with MG2-A24-9-8 (SEQ ID NO; 387), #1 with EfG2-A24-10-7 (SEQ ID NO: 112), #7 with 1G2-A24-10-18 (SEQ ID NO; 394), #10 with HIG2-AO2-9-8 (SEQ ID NO: 114), #10 with HIG2-A02-9-15 (SEQ ID NO: 116), #10 with HIG2-A02-9-4 (SEQ ID NO: 117) and #9 with HIG2-A02-10-8 (SEQ ID NO: 121) were expanded and CIL lines were es tablished. Those CTh lines having higher specific CTL activities against the peptide pulsed target as compared to the activities against target without peptide pulse were de tennined by ELISA. Results are shown in Figure 4a-j. While, other peptides shown in table 5 could not establish the CTL lines despite possible binding activity with LA A*2402. For example, the tipical negative peptide (HIG2-A24-9-7) were shown in Figure 4a. In this invention, the peptiedes which could establish CTL line were selected as potent CTL stimulation peputide. [0133] Establishment for CTL clones stimulated with HIG2 derived peptides Furthermore, the limiting dilution from these CTL lines was perfonned according to the protocols set forth in the "Materials and Methods" section above. The estab lishment of CTL clones from H1G2-A24-9-22 (SEQ ID NO: 111) #7 CTL line, HIG2-A24-9-8 (SEQ ID NO: 387) #5 CTL line, 1HG2-A24-10-7 (SEQ ID NO: 112) #1 CTL line, HIG2-A24-10-18 (SEQ ID NO: 394) #7 CTL line and HIG2-A02-9-4 (SEQ ID NO: 117) #10 CT line are shown in Figure 4c, e, f, g and i. CTL clones had potent and specific CTL activities against the peptide-pulsed target as compared to the activities against target without peptide pulse. [0134] Specific CT activity against the target cells expressing HIG2 and HLA-A*02QI. - The established CTL line raised against these peptides were examined for their ability to recognize the target cells expressing HG2 and HLA-A*0201. Specific CTL activity against 293T or COS7 transfected with both full length HIG2 gene and the HLA-A*0201 molecule, which serves as a specific model for the target cells endo genously express IG2 and HLA-A*0201, was tested using as effector cells the CTL lines raised by HG2-Ao2-9-8 (SEQ ID NO: 114), IG2-A02-9-15 (SEQ ID NO: 116) and the CTL clone raised by mG2-A02-9-4 (SEQ ID NO: 117). 293T or COS7 transfected with full length ECT2 but not HLA-A*0201 and 293T or COS7 transfected wit HLA-A*0201 but not full length ECT2 (or replaced other gene ag. FoxP3 or TTK) were prepared as controls. The CTL line demonstrating the highest specific CTL activity against 293T or COS7 was that transfected with both ECT2 and HLA-A*0201 (Figure 4e, h and i). [0135] These results clearly demonstrate that HIG2-A02-9-8 (SEQ ID NO: 114), HIG2-A02-9-15 (SEQ ID NO: 116) and HIG2-AQ2-9-4 (SEQ ID NO: 117) are naturally expressed on the target cell smface with HLA-A2402 or HLA-A0201 molecule and recognize CTL Furthermore, these peptides are epitope peptides, which - 70 may serve as cancer vaccines targeting IRG2 expressed tumors. [0136] Cytotoxic activity against cancer cell line endogenously expessing HLA-A*0201 and Furthermore, Cytotoxic activity was perfonned by cytotoxi city assay according to the protocols set forth in the "Materials and Methods" section above. As a result, as shown in Fig. 4i, CTL clone stimulated with H02-A02-9-4 (SEQ ID NO: 117) showed remarkably high cytotoxic effect towards HLA-A02-positive and 1G2-positive cancer cell lines CAki- 1, compared to that towards HLA-A02-negative and HIG2-positive cancer cell lines A498. [0137] Stimulation of the T ells using the predicted peptides from INHBB resisted with HLA-A*2402 orHLA-A*020L, and establishment for CTL lines stimuLate with INHBB derived peptides CTLs for those peptides derived from NHB were generated according to the protocols set forth in the "Materials and Methods" section above. Resulting CTLs having detectable specific CTL activity as determined by an lFN-gamma ELISPOT assay are shown in Figure 5. In particular, INHBB-A24-9-180 (SEQ ID NO: 395), INHBB-A24-10-180 (SEQ ID NO: 133), INHBB-A24-10-305 (SEQ ID NO: 135), INHBB-A24-10-7 (SEQ ID NO: 137) and INHBB-A24-10-212 (SEQ ID NO: 426) demonstrated potent IFN-gamma production by IFN-gamma ELISPOT assay, and the cells in the positive well number #7 stimulated with INiBB-A24-9-180 (SEQ ID NO: 395), #3 with INHBB-A24- 0-180 (SEQ ID NO; 133), #2 with INHBB-A24-10-305 (SEQ ID NO: 135), #8 and #2 with NhBB-A24-10-7 (SEQ ID NO: 137) and #1 with INHBB-A24-10-212 (SEQ ID NO: 426) were expanded and CTL lines were established. Those CTL lines having higher specific CTL activities against the peptide-pulsed target as compared to the activities against target without peptide pulse were determined by ELISA. Results are shown in Figure 5b-e. While, other peptides shown in table 6 could not establish the CTL lines despite possible binding activity with HLA-A*2402 and HLA*020 1. For example, the typical negative peptide (INHBB-A24-9-238) were shown in Figure 5a. In this invention, the peptides which could establish CTL line were selected as potent CTL stimulation peptide. [0138] Establishment for CTL clones stimulated with INHBB derived peptides Furthermore, the limiting dilution from these CTL lines was performed according to the protocols set forth in the "Materials and Methods" section above. The establishment of CTL clones from INHBB-A24-9-180 (SEQ ID NO: 395) #7 CTL line, and INHBB-A24 10-305 (SEQ ID NO: 135) #2 CIL line are shown in Figure 5b and d . CTL clones had potent and specific CTL activities against the peptide-pulsed target as compared to the activities against target without peptide pulse. [0139] Specific CTL activity against the target cells expressing INHBB and HLA-A*2402 71 WO 2008/102557 PCT/JP2008/000290 The established CTL line raised against these peptides were examined for their ability to recognize the target cells expressing INHBB and HLA-A*2402. Specific CMT activity against 293T transfected with both full length INBB gene and the HLA A*2402 molecule, which serves as a specific model for the target cells endogenously express INHEB and BLA-A*2402, was tested using as effector cells the CTL lines raised by INHBB-A24-10-180 (SEQ ID NO: 133) and INHBB-A24-10-7 (SEQ ID NO: 137) and the CTL clone raised by INHBB-A24-10-305 (SEQ ID NO: 135),. 293T transfected with full length INFBB but not HLA-A*2402 and 293T transfected with HLA-A*2402 but not full length INHBB were prepared as controls. The CTL line demonstrating the highest specific CIL activity against 293T was that transfected with both INHBB and HLA-A*2402 (Figure 5c, d and e). [0140] These results clearly demonstrate that INHBB-A24-10-305 (SEQ ID NO: 135), INHBB-A24-10- 180 (SEQ ID NO: 133) and INHBB-A24-10-7 (SEQ ID NO: 137) are naturally expressed on the target cell surface with HLA-A2402 molecule and recognize CTL. Furthermore, these peptides are epitope peptides, which may serve as cancer vaccines targeting INB B expressed tumors. [0141] Cytotoxic activity against cancer cell line endogenously expressing HLA-A*2402 andIHB Furthermore, Cytotoxic activity was performed by cytotoxicity assay according to the protocols set forth in the "Materials and Methods" section above. As a result, as shown in Fig. 5b, CTL clone stimulated with IBB-A24-9-180 (SEQ ID NO: 395) showed remarkably high cytotoxic effect towards HLA-A24-positive and INHBB positive cancer cell lines MLAPaca2, compared to that towards HLA-A24-negative and INHBB -positive cancer cell lines CAki-2. [0142) Stimulation of the T cells using the predicted peptides from KIF2OA restricted with HLA-A*2402. and esfablishment for CfL lines stimulated with KF20A derive CTLs for those peptides derived from KIF20A were generated according to the protocols set forth in the "Materials and Methods" section above. Resulting CTLs having detectable specific CTL activity as determined by an IPN-gamma EUSPOT assay are shown in Figure 6. In particular, KIF2OA-A24-9-305 (SEQ ID NO: 174), KIF20A-A24-9-383 (SEQ ID NO: 178), KJF20A-A24-10-304 (SEQ ID NO: 186) and KIF20A-A24-10-66 (SEQ ID NO: 194) demonstrated potent IFN-gamma production by IFN-gamma ELISPOT assay, and the cells in the positive well number #2 stimultaed with KIF20A-A24-9-305 (SEQ ID NO: 174), #3 with KIF20A-A24-9-383 (SEQ ID NO: 178), #5 with KIF20A-A24-10-304 (SEQ ID NO: 186) and #6 with KIF20A-A24-10-66 (SEQ ID NO: 194) were expanded and CT lines were es tablished. Those CTL lines having higher specific CTL activities against the peptide- 72 WO 2008/102557 PCT/JP2008/000290 pulsed target as compared to the activities against target without peptide pulse were de termined by ELISA. Results are shown in Figure 6a-e. While, other peptides shown in table 7 could not establish the CTL lines despite possible binding activity with HLA A*2402. For example, the tipical negative peptide (KIP20A -A24-9-647 and KIF20A A24-10-182) were shown in Figure 6a. In this invention, the peptides which could establish CTL line were selected as potent CTL stimulation peputide. [01431 Establishment for CTL clones stimulated with KIF20A derived peptides Furthermore, the limiting dilution from these CTL lines was performed according to the protocols set forth in the 'Materials and Methods" settion above. The estab lishmet of CTL clones from KIF2OA-A24-9-305 (SEQ ID NO: 174) #2 CTL line, KIF20A-A24-10-304 (SEQ ID NO: 186) #5 CTM line and flP20A-A2440-66 (SEQ ID NO: 194) #6 CTL line are shown in Figue 6b, d and e. CTL plnes had potent and specific CTL activities against the peptide-pulsed target as compared to the activities against target without peptide pulse. [D144] Specific CTL activity against the target cells expressing KIF20A and HLA-A*2402 The established CTL line raised against these peptides were examined for their ability to recognize the target cells expressing KIF20A and HLA-A*2402. Specific CTL activity against COS7 transfected with both full length KIF20A gene and the HLA-A*2402 molecule and A24-LCL transfected by electropolation with full length KIF20A gene, which serve as a specific model for the target cells endogenously express KIF20A and HLA-A*2402, was tested using as effector cells the CTL lines raised by KIF20A-A24-9-383 (SEQ ID NO: 178) and KIF20A-A24-10-304 (SEQ ID NO: 186) and the CTL clone raised by KIF20A-A24-10-66 (SEQ ID NO: 194). COS7 transfected with full length KIF20A but not HLA-A*2402 and COS7 transfected with HLA-A*2402 but not full length KIF20A (or replaced full length URLC10 gene), COS7 traasfected with HLA-A*2402 and pulesd with KIF20A- 10-308, and A24-LCL transfected with mock vector were prepared as controls. The CTL line demonstrating the highest specific CTL activity against COS7 was that transfected with both KIF20A and HLA-A*2402 (Figure 6b, c and d). Alternatively, the CTIL line stuimurated with KIF20A-A24-10-304 (SEQ B) NO: 186) demonstrated against A24-LCL transfected with KIF20A. [01451 These results clearly demonstrate that KIF20A-A24-9-383 (SEQ ID NO: 178), KIF20A-A24-10-304 (SEQ ID NO: 186) and KIF20A-A24-10-66 (SEQ ID NO: 194) is naturally expressed on the target cell surface with HLA-A2402 molecule and recognize CTL. Furthermore, these peptides are epitope peptides, which may serve as cancer vaccines targeting KIF20A expressed tumors. [0146] Cytotoxic activity against cancer cell line endogenously expressing HLA-A*2402 and KIF2OA .73 WO 2008/102557 PCT/JP2008/000290 Furthermore, Cytotoxic activity was performed by cytotoxicity assay according to the protocols set forth in the "Materials and Methods" section above. As a result as shown in Fig. 6b and e, CTL clone stimulated with KIF20A-A24-9-305 (SEQ ID NO: 174) or KIP20A-A24-10-304 (SEQ ED NO: 186) showed remarkably high cytotoxic effect towards HLA-A24-positive and KIF20A-positive cancer cell lines PK45P or MIAPaca2 respectively, compared to that towards HLA-A24-negative and KIF20A-positive cancer cell lines PK59. [0147] Stimulation of th& T cells using the predicted peptides fm KNTC2 restricted with HLA-A*2402. and establishment for CIL lines stimulatd with KNTC2 derived oeptides CTLs for those peptides derived from KNTC2 were generated according to the protocols set forth in the "Materials and Methods" section above. Resulting CTLs having detectable specific CTL activity as determined by an IFN-gamma ELISPOT assay are shown in Figure 7. In particular, KNTC2-A24-9-309 (SEQ ID NO: 196), KNTC2-A24-9-124 (SEQ ID NO: 202), KNTC2-A24-9-154 (SEQ ID) NO: 210), KNTC2-A24-9-150 (SEQ ID NO: 213), KNTC2-A24-10-452 (SEQ ID NO: 214), KNTC2-A24-10-227 (SEQ ID NO: 217) and KNTC2-A24-10-273 (SEQ ID NO: 223) demonstrated potent IFN-gamma. production by IFN-gamma ELISPOT assay, and the cells in the positive well number #8 stimultaed with KNTC2-A24-9-309 (SEQ ID NO: 196), #5 with KNTC2-A24-9-124 (SEQ ID NO: 202), #5 with KNTC2-A24-9-154 (SEQ ID NO: 210), #7 with KNTC2-A24-9-150 (SEQ ID NO; 213), #4 and #5 with KNTC2-A24-10-452 (SEQ ID NO: 214), #1 with KNTC2-A24-10-227 (SEQ ID NO: 217) and#8 with KNTC2-A24-10-273 (SEQ ID NO: 223) were expanded and CTL lines were established. Those CTL lines having higher specific CTL activities against the peptide-pulsed target as compared to the activities against target without peptide pulse. were determined by ELISA. Results are shown in Figure 7a-h. While,,other peptides shown in table 8 could not establish the CTL lines despite possible binding activity with HLA-A*2402. For example, the tipical negative peptide (KNTC2-A24-10-610) were shown in Figure7a. In this invention, the peptides which could establish CIL line were selected as potent CTL stimulation peputide. [0148] Establishment for CTL clones stimulated with KNTC2 derived peptides Furthermore, the limiting dilution from these CTL lines was performed according to the protocols set forth in the "Materials and Methods" section above. The estab lishment of CTL clones from KNTC2-A24-9-154 (SEQ ID NO: 210) #5 CTL line and KNTC2-A24-10-452 (SEQ ID NO: 214) #5 CTL line are shown in Figure 7d and f. CTL clones had potent and specific CTL activities against the pep tide-pulsed target as compared to the activities against target without peptide pulse. [0149] Specific CTL activity against the target cells expressing KNTC2 and HLA-A*2402 74 WO 2008/102557 PCT/3P2008/00029 0 . The established CTL line raised against these peptides were examined for their ability to recognize the target cells expressing KNTC2 and HLA-A*2402. Specific CTL activity against HBK293 transfected with both full length KNTC2 gene and the HLA A*2402 molecule which serves as a specific model for the target cells endogenously express KNTC2 and HLA-A*2402, was tested using as effector cells the CTL clones raised by KNTC2-A24-10-452 (SEQ ID NO: 214). HEK293 transfected with full length KNTC2 but not HLA-A*2402, HEK293 transfected with HLA-A*2402 but not full length KNTC2 and HEK293 transfected with HLA-A*2402 and pulesd with KNTC2-9-309 were prepared as controls. The CTL line demonstrating the highest specific CTL activity against HEK293 was that transfected with both KNTC2 and HLA-A*2402 (Figure 7f). [01501 These results clearly demonstrate that KNTC2-A24-10-452 (SEQ ID NO: 214) is naturally expressed on the target cell surface with HLA-A2402 molecule and recognize CTL Furthermore, thesepeptides are epitope peptides, which may serve as cancer vaccines targeting KNTC2 expressed tumors. [0151] Stimulation of the T cells using the predicted peptides from TK restricted with HLA-A*020l. and establishment for CIL lines stimulated with TTK derived peptides CTLs for those peptides derived from TTK were generated according to the protocols set forth in the "Materials and Methods" section above. Resulting CTLs having de tectable specific CIL activity as determined by an IFN-garnma ELISPOT assay are shown in Figure 8. As depicted in Figure 8b-d, TTK-A2-9-462 (SEQ ID NO: 227), TTK-A2-9-547 (SEQ ID NO: 228), TTK-A2-9-719 (SEQ ID NO: 233) and TTK A2-10-462 (SEQ ID NO: 254) demonstrated potent IFN-ganmna production by IFN gamma ELISPOT assay, and the cells in the positive well number #4 stimultaed with TTK-A2-9-462 (SEQ ID NO: 227), #2 with TTK-A2-9-547 (SEQ ID NO: 228), #1 with ITK-A2-9-719 (SEQ ID NO: 233) and #8 with TlK-A2-10-462 (SEQ ID NO: 254) were expanded. Those CTL lines having higher specific CTL activities against the peptide-pulsed target as compared to the activities against target without peptide pulse were determined by ELISA. While, other peptides shown in table 9 could not establish the CTL lines despite possible binding activity with HLA-A*0201. For example, the tipical negative peptide (TTK-A2-9-278) were shown in Figure 8a. In this invention, the peptiedes which could establish CTL line were selected as potent CTL stimulation peputide. [0152] Establishment for CTL clones smulated with TTK derived peptides Parthermore, the limiting dilution from these CT lines was performed according to the protocols set forth in the "Materials and Methods" section above. The estab lishment of CTL clones from TTK-A2-9-462 (SEQ ID NO: 227) #4 CTL line, TTK A2-9-547 (SEQ ID NO: 228) #2 CTL line, TTK-A2-9-719 (SEQ ID NO: 233) #1 CTL 75 WO 2008/102557 PCT/JP2008/000290 line and TTK-A2-10-462 (SEQ ID NO: 254) #8 CTL line were shown in Figure 8d, c, d and e. CTL clones bad potent and specific CTL activities against the peptide-palsed target as compared to the activities against target without peptide pulse. [01531 Secifc CTL activity against the target cells expressing TTK and HLA-A*0201 The established CTL clone raised against these peptides were examined for their ability to recognize the target cells endogenously expressing TTK and HLA-A*020L. Specific CTL activity against COS7 transfected with both the full length TTK gene and the HLA-A*0201 molecule, which is a specific model for the target cells endo genously express TTK and HLA-A*0201, was tested using as effector cells the CTL clones raised by TTK-A2-9-462 (SEQ BD NO- 227), TTK-A02-9-547 (SEQ ID NO: 228), TTK-A2-9-719 (SEQ IDNO: 233) and TTK-A2-10-462 (SEQ ID NO: 254). COS7 transfected with fulaI length TTK but HLA-A*0201, C07 transfected HLA A*0201 but not full length of TTK (or replaced full length HIG2 gene) and COS7 transfected with HLA-A*0201 and pulsed with different target epitope peputide, were prepared as controls. The CTL Clone having the highest specific CTL activity against COS7 was that transfected with both TTK and HLA-A*0201 (Figure 8b, c, d and e), [0154] These results clearly demonstrate that TTK-A2-9-462 (SEQ ID NO: 227), TTK A02-9-547 (SEQ ID NO: 228), TTK-A2-9-719 (SEQ ID NO: 233) and TTK A02-10-462 (SEQ ID NO: 254) are naturally expressed on the target cell surface with HLA-A2 molecule and recognize CTL. Furthermore, these peptides are epitope peptides, which may serve as cancer vaccines targeting TTK expressed tumors. [0155] Stimulation of the T cells using the predicted peptides from URLCl0 restricted wit HLA-A*020L. and establishment for CTL lines stimulated with URLCI0 derived CTLs for those peptides derived from URLCO were generated according to the protocols set forth in the "Materials and Methods" section above. Resulting CTLs having detectable specific CTL activity as detenined by IFN-gamma ELISPOT assay are shown in Figure 9. As shown in Figure 9b-d, URLC-A2-9-206 (SEQ ID NO: 271), URLC-A2-9-212 (SEQ BD NO: 272) and URLC-A2-10-211 (SEQ ID NO: 288) demonstrated potent IFN-ganna production by IFN-gamma ELISPOT assay, and the cells in the positive well number#7 stimultaed with URLC-A2-9-206 (SEQ ID NO: 271), #3 with URLC-A2-9-212 (SEQ ID) NO: 272) and #5 with URLC-A2-10-211 (SEQ ID NO: 288) were expanded. Those CTL lines having higher specific CIL activities against the peptide-pulsed target as compared to the activities against target without peptide pulse were determined by ELISA. While, other peptides shown in table 10 could not establish the CTL lines despite possible binding activity with HLA A*0201. For example, the tipical negative peptide (URLC-A2-9-58) were shown in Figure 9a. In this invention, the peptiede which could establish CTL line were selected 76 WO 2008/102557 PCT/JP2008/000290 as potent CTL stimulation peputide. [01561 Specific CTL activity against the trget cells epressing URLCI 0 and HLA-A*0201 The established CT line raised against these peptides were examined for their ability to recognize the target cells endogenously expressing URLC10 and HLA A*0201. Specific CTL activity against COS7, Hek293 and 293T transfected with both full length URLCJO gene and the HLA-A*0201 molecule, which serves as a specific model for the target cells endogenously express URLC1O and ELA-A*0201, was tested using as effector cells the CT lineraised by URLCIO-A02-10-211. C057, Hek293 or 293T transfected with full length URLC1O but not.HLA-A*0201 (replaced HLA-A*2402), COS7, Hek293 or 293T transfected with HLA-A*0201 but not full length URLC10 and COS7 transfected-with HLA-A*0201 and pulsed-with different target epitope peputide (URLC1O-A02-10-64) were prepared as controls. The CTL line demonstrating the highest specific CTL activity against COS7, Hek293 or 293T was that ftnsfected with both URLC1O and HLA-A*0201 (Figure 9-2). [0157] These results clearly demonstrate that URCI10-A02-10-21 1 is naturally expressed on the target cell surface with HLA-A*0201 molecule and recognizes CU. Fur thermore, this peptide was epitope peptides, which may utilize cancer vaccine targeting URLC 10 expressed tumors. [0158] Homologv analvsis of the antiken tides The CTL clones established against the following peptides showed potent specific CTL activity. CDH3-A24-9-513 (SEQ ID NO: 19), CDH3-A24-9-406 (SEQ ID NO: 22), CDH3-A24-10-807 (SEQ ID NO: 30), CDH3-A24-10-332 (SEQ ID NO: 34), CDH3-A24-10-655 (SEQ ID NO: 344), CDH3-A24-10-470 (SEQ ID NO: 358), EphA4-A24-9-453 (SEQ ID NO: 41), EphA4-A24-9-5 (SEQ ID NO: 44), EphA4-A24-9-869 (SEQ ID NO: 46), EphA4-A24-9-420 (SEQ ID NO: 48), EphA4-A24-10-24 (SEQ ID NO: 78), EphA4-A02-9-501 (SEQ ID NO: 376), EphA4-A02-9-165 (SEQ ID NO: 379), ECT2-A24-9-515 (SEQ ID NO: 80), ECT2-A24-10-40 (SEQ ID NO: 100), ECT2-A24-1O-l01 (SEQ ID NO: 101), HIG2-A24-9-19 (SEQ ID NO: 110), 77 WO 2008/102557 PCT/JP2008/000290 1G2-A24-9-22 (SEQ ID NO: 111), HIG2-A24-9-8 (SEQ ID NO: 387), HIG2-A24-10-7 (SEQ 1D NO: 112), MG2-A24-10-18 (SEQ ID.NO: 394), HG2-A02-9-8 (SEQ ID NO: 114), H102-A02-9-15 (SEQ ID NO: 116), H1G2-A02-9-4 (SEQ ID NO: 117), HIG2-A02-10-8 (SEQ ID NO: 121), INHBB-A24-9-180 (SEQ ID NO: 395), INHBB-A24-10-180 (SEQ ID NO: 133), NhTBB-A24-10-305 (SEQ ID NO: 135), ]NHB-A24-10-7 (SEQ ID NO: 137), INHBB-A24--10-212 (SEQ ID NO: 426), KF20A-A24-9-305 (SEQ ID NO: 174), KIF20A-A24-9-383 (SEQ ID NO: 178), KIF20A-A24-10-304 (SEQ ID NO; 186), KIF20A-A24-10-66 (SEQ ID NO: 194), KNTC2-A24-9-309 (SEQ ID NO: 196), KNTC2-A24-9-124 (SEQ ID NO: 202), KNTC2-A24--9-154 (SEQ ID NO: 210), KNTC2-A24-9-150 (SEQ ID NO: 213), KNTC2-A24-10-452 (SEQ ID NO: 214), KNTC2-A24-10-227 (SEQ ID NO: 217), KNTC2-A24-10-273 (SEQ ID NO: 223), TTK-A02-9-462 (SEQ ID NO: 227), TTK-A02-9-547 (SEQ ID NO: 228), TTK-A02-9-719 (SEQ ID NO: 233), TTK-A02-10-462 (SEQ ID NO: 254), URLC-A02-9-206 (SEQ ID NO: 271), URLC-A02-9-212 (SEQ ID NO: 272) and URLC-A02-10-211 (SEQ ID NO: 288) [0159] This suggests that the sequences of SEQ ID NO: 19, 22, 30, 34, 344, 358, 41, 44, 46, 48, 78, 376, 379,80,100,101,110,111,387, 112, 394, 114,116,117,121,395, 133, 135, 137,426, 174, 178, 186, 194, 196, 202, 210,213, 214, 217, 223, 227, 228, 233, 254,271,272 or 288 are homologous to the peptides derived from other molecules, which are known to sensitize human immune system. [0160] To exclude this possibility, homology analysis was performed with the peptide sequences as queries using BLAST algorithm 78 WO Z008/102557 PCTJP2008/000290 (http:f/www.ncbi.nlm.nih.gov/blast/blast.cgi). No significant sequence homology was revealed. These results suggest that the sequences of SEQ ID NO: 19, 22,30,34,344,358,41, 44,46,48, 78, 376, 379, 80, 100, 101, 110, 111, 387, 112, 394, 114, 116, 117, 121, 395, 133, 135, 137, 426, 174, 178, 186, 194, 196, 202, 210, 213, 214, 217, 223, 227, 228, 233, 254,271, 272 or 288 are unique and thus possess a low risk of raising un intended immunologic response to any unrelated molecule. [0161] DISCUSSION Identification of new TAAs, particularly those that induce potent and specific anti tumor immune responses, warrants further development of the clinical application of peptide vaccination strategies in various types of cancer (Boon T. et al., (1996) JExp' Med 183: 725-9.; van der Bruggen P et al., (1991) Science 254:1643-7.; Brichard V et aL, (1993) J Exp Med 178:489-95.; Kawakami Y et al, (1994) J Exp Med 180: 347-52.; Shichijo S et al., (1998) J Exp Med 187:277-88.; Chen YT et al., (1997) Proc.Natl.Acd. Sc. USA, 94: 1914-8.; Harls CC., (1996) JNatI Cancer Inst 88:1442-5.; Butterfield LH et al., (1999) Cancer Res 59:3134-42.; Vissers JL et al, (1999) Cancer Res 59:5554-9.; van der Burg SH et at, (1996) J. Immunol 156:3308-14.; Tanaka F et al, (1997) Cancer Res 57:4465-8.; Fujie T et al, (1999) Int J Cancer 80:169-72.; Kikuchi M et al., (1999) lot ICancer 81: 459-66.; Oiso M et al, (1999) Int J Cancer 8 1:387-94.). [01621 cDNA microarray technologies can disclose comprehensive profiles of gene ex pression of malignant cells (Lin YM, et al., Oncogene. 2002 Jun 13;21:4120-8.; Kitahara 0, et al, Cancer Res. 2001 May 1;61:3544-9.; Suzuki C, et al, Cancer Res. 2003 Nov 1;63:7038-41.; Ashida S, Cancer Res. 2004 Sep 1;64:5963-72.; Ochi K, et al, Int J Oncol. 2004 Mar;24(3):647-55.; Kaneta Y, et al., Int J Oncol. 2003 Sep;23:681-9 1.; Obana K, Hepatology. 2005 Jun;41:1339-48.; Kan T, et al., Cancer Res. 2005 Jul 1;65:5638-46.; Kitahara 0, et al., Neoplasia. 2002 Jul-Aug;4:295-303.; Saito-Hisaminato A et al, DNA Res 2002, 9: 35-45.) and, find utility in the identi fication of potential TAM. Among the transcripts that are up-regulated in various cancers, novel human genes, termed CDH3, EPHA4, ECT2, 1HG2, 1BB, KIF20A, KNTC2, TTK and URLC10, were identified using these technologies. [0163] As demonstrated above, CDH3, EPHA4, ECT2, HIG2, INHBB, KIF20A, KNTC2, TTK and LJRLC 10, are over-exprssed in various cancers but show minimal ex pression in normal tissues. In addition, these genes have been shown to have a sig nificant function related to cell proliferation. Thus, peptides derived from CDH3, EPHA4, ECT2, 11102, INUBB, KIF20A, KNTC2, TK and URLC1O can serve as TAA epitopes, which, in turn, can be used to induce significant and specific immune responses against cancer cells.

79 WO 20081102557 PCT/JP200/0029I Thus, as CDH3, EPHA4, ECT2, BIG2, INDB, KW2OA, KNTC2, TIKand URLCIO are novel TAAs, vaccines using these epitope pepddes find utility as immuno therapeutics against vaIous carcinomas or other disease expressing these molecules. Industrial Applicability [0164] The present invention identifies new TAAs, particularly those which induce potent and specific anti-tur immune responses. Such TAAs wants further development as peptide vaccines against diseases associated with the over-expression of CDH3, EPHA4, ECT2, HIG2, IN B, KIF20A, N'IC2, TTK and/or VRLC10 e.g. cancers; All patents, patent applications, and publications cited herein are incorporated by - xetbwnce. [0165] . While the inventionhas been described in detail and with reference to specific embodiments thereof, it is to be understood that the fregoing description is exemplary and explanatory in nature andis intended to illustrate the invention and its preferred embodiments. Through routine experimentation, one skilled in the art will readily recognize that various changes and modifications can be made therein without departing from the spirit and scope of the invention. Thus, the invention is intended to be defined not by the above description, but bythe following claims and their equivalents. Throughout this specification, unless the context requires otherwise, the word "comprise" or variations such as "comprises" or "comprising", will be understood to imply the inclusion of a stated element or integer or method step or group of elements or integers or method steps but not the exclusion of any element or integer or method step or group of elements or integers or method steps. Reference to any prior art in this specification is not, and should not be taken as, an acknowledgment or any form of suggestion that this prior art fbms part of the common general knowledge in any country.

Claims

1. An isolated peptide of less than about 15 amino acids, wherein said peptide is selected from the group consisting of: (a) a peptide comprising an amino acid sequence of SEQ ID NO: 30, 19, 22, 34, 344, 358, 41, 44, 46, 48, 78, 80, 100, 101, 196, 202, 210, 213, 214, 217 or 223; and (b) a peptide having cytotoxic T cell inducibility, wherein said peptide comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 30, 19, 22, 34, 344, 358, 41, 44, 46, 48, 78, 80, 100, 101, 196, 202, 210, 213, 214, 217 and 223, in which 1, 2, or several amino acids are substituted, deleted, or added.

2. The peptide of Claim 1, wherein said peptide is selected from the group consisting of: (a) a peptide consisting of an amino acid sequence of SEQ ID NO: 30, 19,22,34,344,358,41,44,46,48,78,80,100,101,196,202,210,213,214, 217 or 223; and (b) a peptide having cytotoxic T cell inducibility, wherein said peptide consists of an amino acid sequence selected from the group consisting of SEQ ID NO: 30, 19, 22, 34, 344, 358, 41, 44, 46, 48, 78, 80, 100, 101, 196, 202, 210, 213, 214, 217 and 223, in which 1, 2, or several amino acids are substituted, deleted, or added.

3. The peptide of Claim 1 or 2, wherein the peptide has one or both of the following characteristics: (a) the second amino acid from the N-terminus is phenylalanine, tyrosine, methionine, or tryptophan; and (b) the C-terminal amino acid is phenylalanine, leucine, isoleucine, tryptophan, or methionine. C: \DOCUME- I \MELFAC- I LOCALS-I\Temp\20I30307111154490ArnoDocSent I 5597890.doc-7 03 2013 - 81

4. An isolated peptide of less than about 15 amino acids, wherein said peptide is selected from the group consisting of: (a) a peptide comprising an amino acid sequence of SEQ ID NO: 376, or 379; and (b) a peptide having cytotoxic T cell inducibility, wherein said peptide comprises an amino acid sequence selected from the group consisting of SEQ ID NO: 376, and 379, in which 1, 2, or several amino acids are substituted, deleted, or added.

5. The peptide Claim 4, wherein said peptide is selected from the group consisting of: (a) a peptide consisting of an amino acid sequence of SEQ ID NO: 376, or 379; and (b) a peptide having cytotoxic T cell inducibility, wherein said peptide consists of an amino acid sequence selected from the group consisting of SEQ ID NO: 376, and 379, in which 1, 2, or several amino acids are substituted, deleted, or added.

6. The peptide of Claim 4 or 5, wherein the peptide has one or both of the following characteristics: (a) the second amino acid from the N-terminus is leucine or methionine; and (b) the C-terminal amino acid is valine or leucine.

7. A pharmaceutical composition for treating or preventing a disease associated with over-expression of the genes of SEQ ID NO: 1, 3, 5, and/or 13, wherein said composition comprises at least one peptide of any one of Claims 1 to 6 or a polynucleotide encoding the peptide.

8. An exosome that presents on its surface a complex comprising a peptide of any one of Claims 1 to 3 and an HLA antigen. C: \DOCUME- I \MELFAC- I LOCALS-I\Temp\20I30307111154490ArnoDocSent I 5597890.doc-7 03 2013 - 82

9. The exosome of Claim 8, wherein the HLA antigen is HLA-A24.

10. The exosome of Claim 9, wherein the HLA antigen is HLA-A2402.

11. An exosome that presents on its surface a complex comprising a peptide of any one of Claims 4 to 6 and an HLA antigen.

12. The exosome of Claim 11, wherein the HLA antigen is HLA-A2.

13. The exosome of Claim 12, wherein the HLA antigen is HLA-A0201.

14. A method of inducing an antigen-presenting cell having high cytotoxic T cell inducibility, comprising the step of: (a) contacting an antigen-presenting cell with a peptide of any one of Claims 1 to 6, or (b) transferring a gene comprising a polynucleotide encoding a peptide of any one of claims 1 to 6 to an antigen-presenting cell.

15. A method of inducing cytotoxic T cells by contacting a T cell with a peptide of any one of Claims 1 to 6, or which comprises the steps of: (i) contacting an antigen-presenting cell with a peptide of any one of Claims 1 to 6, and (ii) mixing the antigen-presenting cell of step (i) with a T cell and co culturing them.

16. An isolated cytotoxic T cell, which is induced by the method of Claim 15 or which is transduced with nucleic acids encoding TCR subunit polypeptides binding with a peptide of any one of Claims 1 to 6 in the context of HLA-A24 or HLA-A2. C: \DOCUME- I \MELFAC- I LOCALS-I\Temp\20I30307111154490ArnoDocSent I 5597890.doc-7 03 2013 - 83

17. An antigen-presenting cell, which comprises a complex formed between an HLA antigen and a peptide of any one of Claims 1 to 6 or which is induced by the method of Claim 14.

18. A vaccine for inhibiting proliferation of a cell expressing the genes of SEQ ID NO: 1, 3, 5, and/or 13, wherein the vaccine comprises a peptide of any one of Claims 1 to 6 as the active ingredient.

19. The vaccine of Claim 18, wherein the cell expressing genes of SEQ ID NO: 1, 3, 5, and/or 13 is a cancer cell.

20. A method of treating or preventing a disease associated with over expression of the genes of SEQ ID NO: 1, 3, 5, and/or 13 in a subject, comprising administering to said subject a vaccine comprising a peptide of any one of Claims 1 to 6, an immunologically active fragment thereof, or a polynucleotide encoding said peptide or immunologically active fragment.

21. The pharmaceutical composition of Claim 7 or the method of claim 20, wherein the disease associated with over-expression of the genes of SEQ ID NO: 1, 3, 5, and/or 13 is cancer.

22. The pharmaceutical composition of Claim 21, the vaccine of Claim 19 or the method of Claim 21, wherein the cancer is selected from the group consisting of bladder cancer, breast cancer, cervical cancer, cholangiocellular carcinoma, CML, colorectal cancer, endometriosis, esophageal cancer, gastric cancer, diffused type gastric cancer, liver cancer, NSCLC, lymphoma, osteosarcoma, ovarian cancer, pancreatic cancer, prostate cancer, renal carcinoma, SCLC, soft tissue tumor and testicular tumor.

23. The vaccine of any one of Claims 18, 19 and 22, formulated for administration to a subject whose HLA antigen is HLA-A24 or HLA-A2. C: \DOCUME- I \MELFAC- I LOCALS-I\Temp\20I30307111154490ArnoDocSent I 5597890.doc-7 03 2013 - 84

24. A method of identifying for a peptide having an ability to induce CTL against cells expressing CDH3, EPHA4, ECT2, and/or KNTC2, said method comprising the steps of: (i) providing at least one candidate sequence which consists of an amino acid sequence modified by substituting, deleting, or adding one, two or several amino acid residues to an original amino acid sequence, wherein the original amino acid sequence is selected from the group consisting of SEQ ID NO: 30,19,22,34,344,358,41,44,46,48,78,80,100,101,196,202,210,213,214, 217 and 223; (ii) selecting the candidate sequence that does not have substantial significant homology with the peptides derived from any known human gene products other than CDH3, EPHA4, ECT2, or KNTC2; (iii) contacting a peptide consisting of the candidate sequence selected in step (ii) with antigen presenting cells; (iv) contacting the antigen presenting cells of step (iii) with T-cells to evaluate the ability of the peptide to stimulate the T-cells; and (v) identifying the peptide of which CTL inducibility is same as or higher than a peptide consisting of the original amino acid sequence.

25. An isolated peptide according to any one of Claims 1 to 6, a pharmaceutical composition according to Claim 7, 21 or 22, an exosome according to any one of Claims 8 to 13, a method according to any one of Claims 14, 15, 20 to 22, 24, an isolated cytotoxic T cell of Claim 16, an antigen-presenting cell of Claim 17, or a vaccine of Claim 18, 19, 22 or 23 substantially as herein described with reference to the Figures and/or Examples.