SE505316C2 - Användning av proteinet S-100b för framställning av läkemedel för nervceller - Google Patents
Användning av proteinet S-100b för framställning av läkemedel för nervcellerInfo
- Publication number
- SE505316C2 SE505316C2 SE9503620A SE9503620A SE505316C2 SE 505316 C2 SE505316 C2 SE 505316C2 SE 9503620 A SE9503620 A SE 9503620A SE 9503620 A SE9503620 A SE 9503620A SE 505316 C2 SE505316 C2 SE 505316C2
- Authority
- SE
- Sweden
- Prior art keywords
- nerve
- protein
- nerve cells
- cells
- axons
- Prior art date
Links
- 210000002569 neuron Anatomy 0.000 title claims abstract description 20
- 239000003814 drug Substances 0.000 title claims abstract description 11
- 238000004519 manufacturing process Methods 0.000 title claims description 3
- 229940079593 drug Drugs 0.000 title abstract description 6
- 102100021487 Protein S100-B Human genes 0.000 title abstract description 4
- 101710122255 Protein S100-B Proteins 0.000 title abstract description 4
- 230000004083 survival effect Effects 0.000 claims abstract description 3
- 230000012010 growth Effects 0.000 claims description 7
- 102000004169 proteins and genes Human genes 0.000 claims description 4
- 108090000623 proteins and genes Proteins 0.000 claims description 4
- 206010002026 amyotrophic lateral sclerosis Diseases 0.000 claims description 2
- 201000010099 disease Diseases 0.000 claims description 2
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 2
- 201000006417 multiple sclerosis Diseases 0.000 claims description 2
- 230000004936 stimulating effect Effects 0.000 claims 1
- 102000011425 S100 Calcium Binding Protein beta Subunit Human genes 0.000 abstract description 20
- 108010023918 S100 Calcium Binding Protein beta Subunit Proteins 0.000 abstract description 20
- 239000000126 substance Substances 0.000 abstract description 6
- 239000007864 aqueous solution Substances 0.000 abstract description 2
- 230000017363 positive regulation of growth Effects 0.000 abstract description 2
- 210000003050 axon Anatomy 0.000 description 21
- 210000005036 nerve Anatomy 0.000 description 20
- 230000006378 damage Effects 0.000 description 18
- 241000700159 Rattus Species 0.000 description 13
- 230000008439 repair process Effects 0.000 description 13
- 208000027418 Wounds and injury Diseases 0.000 description 11
- 208000014674 injury Diseases 0.000 description 11
- 108010025020 Nerve Growth Factor Proteins 0.000 description 9
- 102000007072 Nerve Growth Factors Human genes 0.000 description 9
- 210000004027 cell Anatomy 0.000 description 9
- 239000003900 neurotrophic factor Substances 0.000 description 9
- 238000000034 method Methods 0.000 description 8
- 210000003205 muscle Anatomy 0.000 description 8
- 210000000278 spinal cord Anatomy 0.000 description 8
- 210000000578 peripheral nerve Anatomy 0.000 description 7
- 230000002490 cerebral effect Effects 0.000 description 6
- 210000000944 nerve tissue Anatomy 0.000 description 6
- 210000001519 tissue Anatomy 0.000 description 6
- 210000004556 brain Anatomy 0.000 description 5
- 230000002093 peripheral effect Effects 0.000 description 5
- 230000008929 regeneration Effects 0.000 description 5
- 238000011069 regeneration method Methods 0.000 description 5
- 206010061218 Inflammation Diseases 0.000 description 4
- 230000004054 inflammatory process Effects 0.000 description 4
- 230000001953 sensory effect Effects 0.000 description 4
- YBAFDPFAUTYYRW-UHFFFAOYSA-N N-L-alpha-glutamyl-L-leucine Natural products CC(C)CC(C(O)=O)NC(=O)C(N)CCC(O)=O YBAFDPFAUTYYRW-UHFFFAOYSA-N 0.000 description 3
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 3
- 230000036755 cellular response Effects 0.000 description 3
- 230000000694 effects Effects 0.000 description 3
- 238000002474 experimental method Methods 0.000 description 3
- 229920003063 hydroxymethyl cellulose Polymers 0.000 description 3
- 229940031574 hydroxymethyl cellulose Drugs 0.000 description 3
- 239000000463 material Substances 0.000 description 3
- 230000008569 process Effects 0.000 description 3
- XKJMBINCVNINCA-UHFFFAOYSA-N Alfalone Chemical compound CON(C)C(=O)NC1=CC=C(Cl)C(Cl)=C1 XKJMBINCVNINCA-UHFFFAOYSA-N 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 2
- 206010028980 Neoplasm Diseases 0.000 description 2
- 108700020796 Oncogene Proteins 0.000 description 2
- 239000000427 antigen Substances 0.000 description 2
- 102000036639 antigens Human genes 0.000 description 2
- 108091007433 antigens Proteins 0.000 description 2
- 210000000988 bone and bone Anatomy 0.000 description 2
- 229940098773 bovine serum albumin Drugs 0.000 description 2
- 230000001413 cellular effect Effects 0.000 description 2
- 210000003792 cranial nerve Anatomy 0.000 description 2
- 238000011161 development Methods 0.000 description 2
- 230000018109 developmental process Effects 0.000 description 2
- 230000035876 healing Effects 0.000 description 2
- 230000006872 improvement Effects 0.000 description 2
- 210000005171 mammalian brain Anatomy 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 239000012528 membrane Substances 0.000 description 2
- 210000004379 membrane Anatomy 0.000 description 2
- 230000001537 neural effect Effects 0.000 description 2
- 210000000056 organ Anatomy 0.000 description 2
- 229920001296 polysiloxane Polymers 0.000 description 2
- 108090000765 processed proteins & peptides Proteins 0.000 description 2
- 210000001202 rhombencephalon Anatomy 0.000 description 2
- 210000003497 sciatic nerve Anatomy 0.000 description 2
- 210000003491 skin Anatomy 0.000 description 2
- 239000011780 sodium chloride Substances 0.000 description 2
- 239000000243 solution Substances 0.000 description 2
- 210000003594 spinal ganglia Anatomy 0.000 description 2
- 210000002435 tendon Anatomy 0.000 description 2
- 230000001720 vestibular Effects 0.000 description 2
- QNRATNLHPGXHMA-XZHTYLCXSA-N (r)-(6-ethoxyquinolin-4-yl)-[(2s,4s,5r)-5-ethyl-1-azabicyclo[2.2.2]octan-2-yl]methanol;hydrochloride Chemical compound Cl.C([C@H]([C@H](C1)CC)C2)CN1[C@@H]2[C@H](O)C1=CC=NC2=CC=C(OCC)C=C21 QNRATNLHPGXHMA-XZHTYLCXSA-N 0.000 description 1
- HWPXGQCMZITGFN-XVYDVKMFSA-N Ala-Cys-His Chemical compound C[C@@H](C(=O)N[C@@H](CS)C(=O)N[C@@H](CC1=CN=CN1)C(=O)O)N HWPXGQCMZITGFN-XVYDVKMFSA-N 0.000 description 1
- DRARURMRLANNLS-GUBZILKMSA-N Ala-Met-Val Chemical compound [H]N[C@@H](C)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](C(C)C)C(O)=O DRARURMRLANNLS-GUBZILKMSA-N 0.000 description 1
- 102000000412 Annexin Human genes 0.000 description 1
- 108050008874 Annexin Proteins 0.000 description 1
- PBSOQGZLPFVXPU-YUMQZZPRSA-N Arg-Glu-Gly Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCC(O)=O)C(=O)NCC(O)=O PBSOQGZLPFVXPU-YUMQZZPRSA-N 0.000 description 1
- JREOBWLIZLXRIS-GUBZILKMSA-N Asn-Glu-Leu Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(C)C)C(O)=O JREOBWLIZLXRIS-GUBZILKMSA-N 0.000 description 1
- VIRHEUMYXXLCBF-WDSKDSINSA-N Asp-Gly-Glu Chemical compound [H]N[C@@H](CC(O)=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(O)=O VIRHEUMYXXLCBF-WDSKDSINSA-N 0.000 description 1
- AKKUDRZKFZWPBH-SRVKXCTJSA-N Asp-Lys-His Chemical compound C1=C(NC=N1)C[C@@H](C(=O)O)NC(=O)[C@H](CCCCN)NC(=O)[C@H](CC(=O)O)N AKKUDRZKFZWPBH-SRVKXCTJSA-N 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- 102000005701 Calcium-Binding Proteins Human genes 0.000 description 1
- 108010045403 Calcium-Binding Proteins Proteins 0.000 description 1
- 101710091342 Chemotactic peptide Proteins 0.000 description 1
- 102000008186 Collagen Human genes 0.000 description 1
- 108010035532 Collagen Proteins 0.000 description 1
- IIGHQOPGMGKDMT-SRVKXCTJSA-N Cys-Asp-Phe Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)O)NC(=O)[C@H](CC(=O)O)NC(=O)[C@H](CS)N IIGHQOPGMGKDMT-SRVKXCTJSA-N 0.000 description 1
- 206010063560 Excessive granulation tissue Diseases 0.000 description 1
- LFIVHGMKWFGUGK-IHRRRGAJSA-N Gln-Glu-Phe Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)O)NC(=O)[C@H](CCC(=O)O)NC(=O)[C@H](CCC(=O)N)N LFIVHGMKWFGUGK-IHRRRGAJSA-N 0.000 description 1
- DSPQRJXOIXHOHK-WDSKDSINSA-N Glu-Asp-Gly Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)NCC(O)=O DSPQRJXOIXHOHK-WDSKDSINSA-N 0.000 description 1
- XHUCVVHRLNPZSZ-CIUDSAMLSA-N Glu-Gln-Glu Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCC(O)=O)C(O)=O XHUCVVHRLNPZSZ-CIUDSAMLSA-N 0.000 description 1
- JGHNIWVNCAOVRO-DCAQKATOSA-N Glu-His-Glu Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC1=CNC=N1)C(=O)N[C@@H](CCC(O)=O)C(O)=O JGHNIWVNCAOVRO-DCAQKATOSA-N 0.000 description 1
- XTZDZAXYPDISRR-MNXVOIDGSA-N Glu-Ile-Lys Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CCCCN)C(=O)O)NC(=O)[C@H](CCC(=O)O)N XTZDZAXYPDISRR-MNXVOIDGSA-N 0.000 description 1
- YTRBQAQSUDSIQE-FHWLQOOXSA-N Glu-Phe-Phe Chemical compound C([C@H](NC(=O)[C@H](CCC(O)=O)N)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)C1=CC=CC=C1 YTRBQAQSUDSIQE-FHWLQOOXSA-N 0.000 description 1
- LLZLRXBTOOFODM-QSFUFRPTSA-N Ile-Asp-Val Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](C(C)C)C(=O)O)N LLZLRXBTOOFODM-QSFUFRPTSA-N 0.000 description 1
- HQUXQAMSWFIRET-AVGNSLFASA-N Leu-Glu-Lys Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@H](C(O)=O)CCCCN HQUXQAMSWFIRET-AVGNSLFASA-N 0.000 description 1
- USLNHQZCDQJBOV-ZPFDUUQYSA-N Leu-Ile-Asn Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CC(N)=O)C(O)=O USLNHQZCDQJBOV-ZPFDUUQYSA-N 0.000 description 1
- HVHRPWQEQHIQJF-AVGNSLFASA-N Leu-Lys-Glu Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(O)=O HVHRPWQEQHIQJF-AVGNSLFASA-N 0.000 description 1
- RBEATVHTWHTHTJ-KKUMJFAQSA-N Lys-Leu-Lys Chemical compound NCCCC[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCCCN)C(O)=O RBEATVHTWHTHTJ-KKUMJFAQSA-N 0.000 description 1
- JMNRXRPBHFGXQX-GUBZILKMSA-N Lys-Ser-Glu Chemical compound NCCCC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@H](C(O)=O)CCC(O)=O JMNRXRPBHFGXQX-GUBZILKMSA-N 0.000 description 1
- WYEXWKAWMNJKPN-UBHSHLNASA-N Met-Ala-Phe Chemical compound C[C@@H](C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)O)NC(=O)[C@H](CCSC)N WYEXWKAWMNJKPN-UBHSHLNASA-N 0.000 description 1
- RMLLCGYYVZKKRT-CIUDSAMLSA-N Met-Ser-Glu Chemical compound CSCC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@H](C(O)=O)CCC(O)=O RMLLCGYYVZKKRT-CIUDSAMLSA-N 0.000 description 1
- SITLTJHOQZFJGG-UHFFFAOYSA-N N-L-alpha-glutamyl-L-valine Natural products CC(C)C(C(O)=O)NC(=O)C(N)CCC(O)=O SITLTJHOQZFJGG-UHFFFAOYSA-N 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 206010033799 Paralysis Diseases 0.000 description 1
- PPHFTNABKQRAJV-JYJNAYRXSA-N Phe-His-Gln Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)N[C@@H](CC2=CN=CN2)C(=O)N[C@@H](CCC(=O)N)C(=O)O)N PPHFTNABKQRAJV-JYJNAYRXSA-N 0.000 description 1
- 102000001708 Protein Isoforms Human genes 0.000 description 1
- 108010029485 Protein Isoforms Proteins 0.000 description 1
- 208000008765 Sciatica Diseases 0.000 description 1
- MOQDPPUMFSMYOM-KKUMJFAQSA-N Ser-His-Phe Chemical compound C1=CC=C(C=C1)C[C@@H](C(=O)O)NC(=O)[C@H](CC2=CN=CN2)NC(=O)[C@H](CO)N MOQDPPUMFSMYOM-KKUMJFAQSA-N 0.000 description 1
- RRRRCRYTLZVCEN-HJGDQZAQSA-N Thr-Leu-Asp Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC(O)=O)C(O)=O RRRRCRYTLZVCEN-HJGDQZAQSA-N 0.000 description 1
- ZPFLBLFITJCBTP-QWRGUYRKSA-N Tyr-Ser-Gly Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CO)C(=O)NCC(O)=O ZPFLBLFITJCBTP-QWRGUYRKSA-N 0.000 description 1
- BMGOFDMKDVVGJG-NHCYSSNCSA-N Val-Asp-Lys Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CC(=O)O)C(=O)N[C@@H](CCCCN)C(=O)O)N BMGOFDMKDVVGJG-NHCYSSNCSA-N 0.000 description 1
- VENKIVFKIPGEJN-NHCYSSNCSA-N Val-Met-Glu Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(=O)O)C(=O)O)N VENKIVFKIPGEJN-NHCYSSNCSA-N 0.000 description 1
- DLLRRUDLMSJTMB-GUBZILKMSA-N Val-Ser-Met Chemical compound CC(C)[C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CCSC)C(=O)O)N DLLRRUDLMSJTMB-GUBZILKMSA-N 0.000 description 1
- JAIZPWVHPQRYOU-ZJDVBMNYSA-N Val-Thr-Thr Chemical compound C[C@H]([C@@H](C(=O)N[C@@H]([C@@H](C)O)C(=O)O)NC(=O)[C@H](C(C)C)N)O JAIZPWVHPQRYOU-ZJDVBMNYSA-N 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 150000001413 amino acids Chemical group 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 230000000890 antigenic effect Effects 0.000 description 1
- 230000001174 ascending effect Effects 0.000 description 1
- 108010038633 aspartylglutamate Proteins 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 238000010352 biotechnological method Methods 0.000 description 1
- 210000004958 brain cell Anatomy 0.000 description 1
- 239000007975 buffered saline Substances 0.000 description 1
- 102000014823 calbindin Human genes 0.000 description 1
- 108060001061 calbindin Proteins 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 235000011148 calcium chloride Nutrition 0.000 description 1
- 210000000845 cartilage Anatomy 0.000 description 1
- 210000005056 cell body Anatomy 0.000 description 1
- 230000024245 cell differentiation Effects 0.000 description 1
- 210000001638 cerebellum Anatomy 0.000 description 1
- 238000006243 chemical reaction Methods 0.000 description 1
- 229920001436 collagen Polymers 0.000 description 1
- 230000008602 contraction Effects 0.000 description 1
- 238000005520 cutting process Methods 0.000 description 1
- 210000004292 cytoskeleton Anatomy 0.000 description 1
- 230000003247 decreasing effect Effects 0.000 description 1
- 230000007547 defect Effects 0.000 description 1
- 230000007850 degeneration Effects 0.000 description 1
- 230000002996 emotional effect Effects 0.000 description 1
- 210000000256 facial nerve Anatomy 0.000 description 1
- 210000002950 fibroblast Anatomy 0.000 description 1
- 230000003176 fibrotic effect Effects 0.000 description 1
- 125000002485 formyl group Chemical class [H]C(*)=O 0.000 description 1
- 230000008014 freezing Effects 0.000 description 1
- 238000007710 freezing Methods 0.000 description 1
- 210000001126 granulation tissue Anatomy 0.000 description 1
- 239000003102 growth factor Substances 0.000 description 1
- 230000001771 impaired effect Effects 0.000 description 1
- 238000001802 infusion Methods 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 230000003993 interaction Effects 0.000 description 1
- 210000001503 joint Anatomy 0.000 description 1
- 210000000281 joint capsule Anatomy 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 230000004807 localization Effects 0.000 description 1
- 108010009298 lysylglutamic acid Proteins 0.000 description 1
- 210000002540 macrophage Anatomy 0.000 description 1
- 229940126601 medicinal product Drugs 0.000 description 1
- 210000001767 medulla oblongata Anatomy 0.000 description 1
- 210000001259 mesencephalon Anatomy 0.000 description 1
- 210000002161 motor neuron Anatomy 0.000 description 1
- 230000004118 muscle contraction Effects 0.000 description 1
- 210000003007 myelin sheath Anatomy 0.000 description 1
- 210000000653 nervous system Anatomy 0.000 description 1
- 210000004498 neuroglial cell Anatomy 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 230000003565 oculomotor Effects 0.000 description 1
- 231100000590 oncogenic Toxicity 0.000 description 1
- 230000002246 oncogenic effect Effects 0.000 description 1
- 230000008520 organization Effects 0.000 description 1
- 229940094443 oxytocics prostaglandins Drugs 0.000 description 1
- 108010069184 phenylalanyl-leucyl-glutamyl-glutamyl-isoleucine Proteins 0.000 description 1
- NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 150000003180 prostaglandins Chemical class 0.000 description 1
- 238000011160 research Methods 0.000 description 1
- 210000001044 sensory neuron Anatomy 0.000 description 1
- 208000037974 severe injury Diseases 0.000 description 1
- 230000009528 severe injury Effects 0.000 description 1
- 238000004904 shortening Methods 0.000 description 1
- 238000003786 synthesis reaction Methods 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 238000010257 thawing Methods 0.000 description 1
- 230000017423 tissue regeneration Effects 0.000 description 1
- 238000011200 topical administration Methods 0.000 description 1
- 230000009466 transformation Effects 0.000 description 1
- 238000000844 transformation Methods 0.000 description 1
- 238000002054 transplantation Methods 0.000 description 1
- 230000004865 vascular response Effects 0.000 description 1
Classifications
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/18—Growth factors; Growth regulators
- A61K38/185—Nerve growth factor [NGF]; Brain derived neurotrophic factor [BDNF]; Ciliary neurotrophic factor [CNTF]; Glial derived neurotrophic factor [GDNF]; Neurotrophins, e.g. NT-3
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
- A61K38/16—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- A61K38/17—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- A61K38/1703—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates
- A61K38/1709—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans from vertebrates from mammals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P25/00—Drugs for disorders of the nervous system
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Engineering & Computer Science (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Veterinary Medicine (AREA)
- Chemical & Material Sciences (AREA)
- Public Health (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Epidemiology (AREA)
- Immunology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Biomedical Technology (AREA)
- Neurology (AREA)
- Neurosurgery (AREA)
- Psychology (AREA)
- Marine Sciences & Fisheries (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Organic Chemistry (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Peptides Or Proteins (AREA)
Priority Applications (11)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SE9503620A SE505316C2 (sv) | 1995-10-17 | 1995-10-17 | Användning av proteinet S-100b för framställning av läkemedel för nervceller |
| PCT/SE1996/001305 WO1997014427A1 (fr) | 1995-10-17 | 1996-10-15 | UTILISATION DE LA PROTEINE S-100b DANS DES MEDICAMENTS, ET MEDICAMENTS CONTENANT LA PROTEINE S-100b |
| JP9515742A JPH11515003A (ja) | 1995-10-17 | 1996-10-15 | タンパク質Ｓ−１００ｂの薬剤への使用法、および該タンパク質Ｓ−１００ｂを含む薬剤 |
| NZ320721A NZ320721A (en) | 1995-10-17 | 1996-10-15 | Use of the S-100b protein as a medicine to treat amyotrophic lateral sclerosis or multiple sclerosis |
| EP96935706A EP0952844A1 (fr) | 1995-10-17 | 1996-10-15 | UTILISATION DE LA PROTEINE S-100b DANS DES MEDICAMENTS, ET MEDICAMENTS CONTENANT LA PROTEINE S-100b |
| US09/051,589 US5990080A (en) | 1995-10-17 | 1996-10-15 | Use of protein S-100-b in medicines containing the protein S-100b |
| CA002235278A CA2235278A1 (fr) | 1995-10-17 | 1996-10-15 | Utilisation de la proteine s-100b dans des medicaments, et medicaments contenant la proteine s-100b |
| EE9800108A EE9800108A (et) | 1995-10-17 | 1996-10-15 | Valgu S-100b kasutamine ravimites ja valku S-100b sisaldavad ravimid |
| CZ981166A CZ116698A3 (cs) | 1995-10-17 | 1996-10-15 | Použití proteinu S-100 v medicíně a léčivo obsahující protein S100-b |
| AU73523/96A AU713332B2 (en) | 1995-10-17 | 1996-10-15 | Use of protein S-100b in medicines and medicines containing the protein S-100-b |
| NO981719A NO981719L (no) | 1995-10-17 | 1998-04-16 | Anvendelse av protein S-100b i medisiner og medisiner inneholdende protein S-100b |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| SE9503620A SE505316C2 (sv) | 1995-10-17 | 1995-10-17 | Användning av proteinet S-100b för framställning av läkemedel för nervceller |
Publications (4)
| Publication Number | Publication Date |
|---|---|
| SE9503620D0 SE9503620D0 (sv) | 1995-10-17 |
| SE9503620L SE9503620L (sv) | 1997-04-18 |
| SE505316C3 SE505316C3 (sv) | 1997-04-18 |
| SE505316C2 true SE505316C2 (sv) | 1997-08-04 |
Family
ID=20399846
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| SE9503620A SE505316C2 (sv) | 1995-10-17 | 1995-10-17 | Användning av proteinet S-100b för framställning av läkemedel för nervceller |
Country Status (11)
| Country | Link |
|---|---|
| US (1) | US5990080A (fr) |
| EP (1) | EP0952844A1 (fr) |
| JP (1) | JPH11515003A (fr) |
| AU (1) | AU713332B2 (fr) |
| CA (1) | CA2235278A1 (fr) |
| CZ (1) | CZ116698A3 (fr) |
| EE (1) | EE9800108A (fr) |
| NO (1) | NO981719L (fr) |
| NZ (1) | NZ320721A (fr) |
| SE (1) | SE505316C2 (fr) |
| WO (1) | WO1997014427A1 (fr) |
Families Citing this family (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US6258776B1 (en) * | 1997-08-12 | 2001-07-10 | Novartis Ag | Calcium-regulated kinase |
| US20030108528A1 (en) * | 1998-05-19 | 2003-06-12 | Michal Eisenbach-Schwartz | Activated t-cells, nervous system-specific antigens and their uses |
| US20020072493A1 (en) | 1998-05-19 | 2002-06-13 | Yeda Research And Development Co. Ltd. | Activated T cells, nervous system-specific antigens and their uses |
| JP2003532618A (ja) * | 1998-05-19 | 2003-11-05 | イエダ リサーチ アンド デベロプメント カンパニイ リミテッド | 細胞、神経系−特異的抗原およびそれらの用途 |
| DE19915485A1 (de) | 1999-04-07 | 2000-10-19 | Hugo A Katus | Therapie der Herzinsuffizienz |
| PL205469B1 (pl) | 2001-12-06 | 2010-04-30 | Yeda Res & Dev | Zastosowanie Cop 1 |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1992010200A1 (fr) * | 1990-12-14 | 1992-06-25 | New York University | Interactions fonctionnelles entre un glial s-100b et des neurones serotoninergiques du systeme nerveux central |
-
1995
- 1995-10-17 SE SE9503620A patent/SE505316C2/sv not_active IP Right Cessation
-
1996
- 1996-10-15 JP JP9515742A patent/JPH11515003A/ja not_active Withdrawn
- 1996-10-15 CZ CZ981166A patent/CZ116698A3/cs unknown
- 1996-10-15 EE EE9800108A patent/EE9800108A/xx unknown
- 1996-10-15 AU AU73523/96A patent/AU713332B2/en not_active Ceased
- 1996-10-15 CA CA002235278A patent/CA2235278A1/fr not_active Abandoned
- 1996-10-15 WO PCT/SE1996/001305 patent/WO1997014427A1/fr not_active Ceased
- 1996-10-15 US US09/051,589 patent/US5990080A/en not_active Expired - Fee Related
- 1996-10-15 NZ NZ320721A patent/NZ320721A/en unknown
- 1996-10-15 EP EP96935706A patent/EP0952844A1/fr not_active Ceased
-
1998
- 1998-04-16 NO NO981719A patent/NO981719L/no not_active Application Discontinuation
Also Published As
| Publication number | Publication date |
|---|---|
| SE9503620L (sv) | 1997-04-18 |
| AU713332B2 (en) | 1999-12-02 |
| SE9503620D0 (sv) | 1995-10-17 |
| NZ320721A (en) | 2000-07-28 |
| CA2235278A1 (fr) | 1997-04-24 |
| CZ116698A3 (cs) | 1998-09-16 |
| JPH11515003A (ja) | 1999-12-21 |
| AU7352396A (en) | 1997-05-07 |
| NO981719D0 (no) | 1998-04-16 |
| NO981719L (no) | 1998-06-16 |
| WO1997014427A1 (fr) | 1997-04-24 |
| US5990080A (en) | 1999-11-23 |
| EE9800108A (et) | 1998-10-15 |
| EP0952844A1 (fr) | 1999-11-03 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| DE69532996T2 (de) | Peptidanaloge des menschlichen basischen myelinproteins | |
| DE60029304T2 (de) | Aktivierung von regulatorischen t zellen durch ein alpha-melanocyten stimulierendes hormon | |
| Anderson et al. | Ciliary neurotrophic factor protects striatal output neurons in an animal model of Huntington disease. | |
| Ren et al. | Time window of intracisternal osteogenic protein-1 in enhancing functional recovery after stroke | |
| CN108503690B (zh) | 一种促进创伤后组织修复与再生的修复肽及其应用 | |
| EA028343B1 (ru) | Лечение дегенеративного заболевания сустава | |
| CA2709007A1 (fr) | Methodes empechant la cicatrisation | |
| US11260101B2 (en) | Repair peptide for use in promoting post-traumatic tissue repair and regeneration, and application thereof | |
| EA027343B1 (ru) | Имплантируемые устройства медицинского назначения с повышенной иммунной толерантностью и способы изготовления и имплантирования | |
| US6262024B1 (en) | Neuron regulatory factor for promoting neuron survival | |
| US6680295B1 (en) | Method and pharmaceutical composition for prevention and treatment of brain damage | |
| KR20190067219A (ko) | 통증 예방, 경감 또는 치료에서의 신경 흥분성 상해 관련 폴리펩타이드의 용도 | |
| PT89573B (pt) | Metodo para a reducao de respostas mediadas por imunoglobulina e | |
| Christ et al. | The application of gene therapy to the treatment of erectile dysfunction | |
| SE505316C2 (sv) | Användning av proteinet S-100b för framställning av läkemedel för nervceller | |
| SE505316C3 (sv) | Användning av proteinet S-100b för framställning av läkemedel för nervceller | |
| EP0756605B1 (fr) | Peptides utilise comme agents therapeutiques dans le traitement de maladies auto-immunes | |
| US5830857A (en) | Method of treating epilepsy | |
| DE60036638T2 (de) | Verwendung von colostrinin, dessen peptidbestandteile und deren analoga zur förderung der neuronalen zelldifferenzierung | |
| RU2095067C1 (ru) | Способ стимуляции репаративных и трофических процессов в тканях организма | |
| MX2007000144A (es) | Medicamento. | |
| JPH072692A (ja) | 目の疾病の治療または予防用の薬学的組成物 | |
| RU2262945C1 (ru) | Способ снижения массы тела в эксперименте на животных | |
| RU2302237C2 (ru) | Способ получения биологически активной фракции s-1-10, фармацевтическая композиция, снижающая тремор при паркинсонизме и судорожную активность при эпилепсии | |
| JP2009504636A (ja) | 血漿または血清を含む神経損傷治療用の医薬組成物 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| NUG | Patent has lapsed |
Ref document number: 9503620-8 Format of ref document f/p: F |