CA2339871A1 - Acides nucleiques codant un purinorecepteur fonctionnel humain p2x2, et procedes de production et d'utilisation de ce dernier - Google Patents
Acides nucleiques codant un purinorecepteur fonctionnel humain p2x2, et procedes de production et d'utilisation de ce dernier Download PDFInfo
- Publication number
- CA2339871A1 CA2339871A1 CA002339871A CA2339871A CA2339871A1 CA 2339871 A1 CA2339871 A1 CA 2339871A1 CA 002339871 A CA002339871 A CA 002339871A CA 2339871 A CA2339871 A CA 2339871A CA 2339871 A1 CA2339871 A1 CA 2339871A1
- Authority
- CA
- Canada
- Prior art keywords
- seq
- receptor
- cell
- polynucleotide
- human
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Abandoned
Links
- 238000000034 method Methods 0.000 title claims abstract description 75
- 150000007523 nucleic acids Chemical class 0.000 title claims abstract description 13
- 102000039446 nucleic acids Human genes 0.000 title claims abstract description 9
- 108020004707 nucleic acids Proteins 0.000 title claims abstract description 9
- 102000008344 purinergic nucleotide receptor activity proteins Human genes 0.000 title 1
- 108040002778 purinergic nucleotide receptor activity proteins Proteins 0.000 title 1
- 102100040479 P2X purinoceptor 2 Human genes 0.000 claims abstract description 117
- 101710189968 P2X purinoceptor 2 Proteins 0.000 claims abstract description 76
- 102000005962 receptors Human genes 0.000 claims abstract description 76
- 108020003175 receptors Proteins 0.000 claims abstract description 76
- 102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 57
- 108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 57
- 229920001184 polypeptide Polymers 0.000 claims abstract description 54
- 101000614335 Homo sapiens P2X purinoceptor 2 Proteins 0.000 claims abstract description 43
- 150000001875 compounds Chemical class 0.000 claims abstract description 42
- 230000000694 effects Effects 0.000 claims abstract description 14
- 210000004027 cell Anatomy 0.000 claims description 110
- 108091033319 polynucleotide Proteins 0.000 claims description 56
- 102000040430 polynucleotide Human genes 0.000 claims description 56
- 239000002157 polynucleotide Substances 0.000 claims description 55
- 108020004414 DNA Proteins 0.000 claims description 41
- 239000002299 complementary DNA Substances 0.000 claims description 28
- 108091032973 (ribonucleotides)n+m Proteins 0.000 claims description 23
- 102000002294 Purinergic P2X Receptors Human genes 0.000 claims description 22
- 108010000836 Purinergic P2X Receptors Proteins 0.000 claims description 22
- 239000000556 agonist Substances 0.000 claims description 21
- 210000004962 mammalian cell Anatomy 0.000 claims description 20
- 239000012634 fragment Substances 0.000 claims description 19
- 150000001413 amino acids Chemical class 0.000 claims description 18
- 239000005557 antagonist Substances 0.000 claims description 17
- 239000000523 sample Substances 0.000 claims description 17
- 238000012360 testing method Methods 0.000 claims description 14
- 239000013604 expression vector Substances 0.000 claims description 12
- 230000027455 binding Effects 0.000 claims description 11
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 11
- 208000035475 disorder Diseases 0.000 claims description 10
- 230000015572 biosynthetic process Effects 0.000 claims description 8
- 239000003446 ligand Substances 0.000 claims description 8
- 230000004913 activation Effects 0.000 claims description 7
- 108020004999 messenger RNA Proteins 0.000 claims description 7
- 230000001580 bacterial effect Effects 0.000 claims description 6
- 210000005253 yeast cell Anatomy 0.000 claims description 6
- 102000004190 Enzymes Human genes 0.000 claims description 5
- 108090000790 Enzymes Proteins 0.000 claims description 5
- 238000004519 manufacturing process Methods 0.000 claims description 5
- 238000013518 transcription Methods 0.000 claims description 5
- 230000035897 transcription Effects 0.000 claims description 5
- 208000032041 Hearing impaired Diseases 0.000 claims description 4
- 208000027601 Inner ear disease Diseases 0.000 claims description 4
- 208000027491 vestibular disease Diseases 0.000 claims description 4
- 230000000295 complement effect Effects 0.000 claims description 3
- 210000001035 gastrointestinal tract Anatomy 0.000 claims description 3
- 238000005259 measurement Methods 0.000 claims description 3
- 238000001514 detection method Methods 0.000 claims description 2
- 238000002560 therapeutic procedure Methods 0.000 claims 8
- 230000001270 agonistic effect Effects 0.000 claims 4
- 230000003042 antagnostic effect Effects 0.000 claims 4
- 208000015706 neuroendocrine disease Diseases 0.000 claims 4
- 125000003275 alpha amino acid group Chemical group 0.000 claims 3
- 208000018522 Gastrointestinal disease Diseases 0.000 claims 2
- 238000012258 culturing Methods 0.000 claims 2
- 208000010643 digestive system disease Diseases 0.000 claims 2
- 239000007850 fluorescent dye Substances 0.000 claims 2
- 208000018685 gastrointestinal system disease Diseases 0.000 claims 2
- 238000010188 recombinant method Methods 0.000 claims 2
- 230000004071 biological effect Effects 0.000 claims 1
- 239000012916 chromogenic reagent Substances 0.000 claims 1
- 230000003993 interaction Effects 0.000 claims 1
- 238000010839 reverse transcription Methods 0.000 claims 1
- 239000013598 vector Substances 0.000 abstract description 22
- 230000001225 therapeutic effect Effects 0.000 abstract description 6
- 239000013615 primer Substances 0.000 description 24
- 108090000623 proteins and genes Proteins 0.000 description 20
- 125000003729 nucleotide group Chemical group 0.000 description 19
- 210000001519 tissue Anatomy 0.000 description 19
- 239000002773 nucleotide Substances 0.000 description 17
- 210000000287 oocyte Anatomy 0.000 description 14
- 102000004169 proteins and genes Human genes 0.000 description 14
- 238000006243 chemical reaction Methods 0.000 description 13
- 235000018102 proteins Nutrition 0.000 description 13
- 235000001014 amino acid Nutrition 0.000 description 12
- 230000006870 function Effects 0.000 description 12
- 108091006146 Channels Proteins 0.000 description 10
- 108091026890 Coding region Proteins 0.000 description 10
- 229940024606 amino acid Drugs 0.000 description 10
- 108091028043 Nucleic acid sequence Proteins 0.000 description 9
- 238000003780 insertion Methods 0.000 description 9
- 230000037431 insertion Effects 0.000 description 9
- 239000000047 product Substances 0.000 description 9
- 102000053602 DNA Human genes 0.000 description 8
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 8
- 230000004044 response Effects 0.000 description 8
- 239000000243 solution Substances 0.000 description 8
- 229940088597 hormone Drugs 0.000 description 7
- 239000005556 hormone Substances 0.000 description 7
- 239000000203 mixture Substances 0.000 description 7
- 238000006467 substitution reaction Methods 0.000 description 7
- 108091034117 Oligonucleotide Proteins 0.000 description 6
- 101000614333 Rattus norvegicus P2X purinoceptor 2 Proteins 0.000 description 6
- 240000004808 Saccharomyces cerevisiae Species 0.000 description 6
- 235000014680 Saccharomyces cerevisiae Nutrition 0.000 description 6
- 230000010076 replication Effects 0.000 description 6
- 238000003786 synthesis reaction Methods 0.000 description 6
- 230000001720 vestibular Effects 0.000 description 6
- 108020004635 Complementary DNA Proteins 0.000 description 5
- 102100040460 P2X purinoceptor 3 Human genes 0.000 description 5
- 101710189970 P2X purinoceptor 3 Proteins 0.000 description 5
- 102100037601 P2X purinoceptor 4 Human genes 0.000 description 5
- 230000003321 amplification Effects 0.000 description 5
- 238000009396 hybridization Methods 0.000 description 5
- 238000003199 nucleic acid amplification method Methods 0.000 description 5
- 239000013612 plasmid Substances 0.000 description 5
- 239000000126 substance Substances 0.000 description 5
- 241000238631 Hexapoda Species 0.000 description 4
- 108700026244 Open Reading Frames Proteins 0.000 description 4
- 101710189967 P2X purinoceptor 4 Proteins 0.000 description 4
- 238000010240 RT-PCR analysis Methods 0.000 description 4
- 238000004458 analytical method Methods 0.000 description 4
- 238000010367 cloning Methods 0.000 description 4
- 238000012217 deletion Methods 0.000 description 4
- 230000037430 deletion Effects 0.000 description 4
- 239000003814 drug Substances 0.000 description 4
- 229940088598 enzyme Drugs 0.000 description 4
- 102000006602 glyceraldehyde-3-phosphate dehydrogenase Human genes 0.000 description 4
- 108020004445 glyceraldehyde-3-phosphate dehydrogenase Proteins 0.000 description 4
- 238000011534 incubation Methods 0.000 description 4
- 230000000977 initiatory effect Effects 0.000 description 4
- 238000002347 injection Methods 0.000 description 4
- 239000007924 injection Substances 0.000 description 4
- 229910001629 magnesium chloride Inorganic materials 0.000 description 4
- 230000035772 mutation Effects 0.000 description 4
- 238000010647 peptide synthesis reaction Methods 0.000 description 4
- 230000001817 pituitary effect Effects 0.000 description 4
- 108091008146 restriction endonucleases Proteins 0.000 description 4
- 230000028327 secretion Effects 0.000 description 4
- 230000001953 sensory effect Effects 0.000 description 4
- 210000000278 spinal cord Anatomy 0.000 description 4
- FIAFUQMPZJWCLV-UHFFFAOYSA-N suramin Chemical compound OS(=O)(=O)C1=CC(S(O)(=O)=O)=C2C(NC(=O)C3=CC=C(C(=C3)NC(=O)C=3C=C(NC(=O)NC=4C=C(C=CC=4)C(=O)NC=4C(=CC=C(C=4)C(=O)NC=4C5=C(C=C(C=C5C(=CC=4)S(O)(=O)=O)S(O)(=O)=O)S(O)(=O)=O)C)C=CC=3)C)=CC=C(S(O)(=O)=O)C2=C1 FIAFUQMPZJWCLV-UHFFFAOYSA-N 0.000 description 4
- 229960005314 suramin Drugs 0.000 description 4
- 238000001890 transfection Methods 0.000 description 4
- 238000013519 translation Methods 0.000 description 4
- 230000003612 virological effect Effects 0.000 description 4
- 239000003155 DNA primer Substances 0.000 description 3
- 241000588724 Escherichia coli Species 0.000 description 3
- 239000007995 HEPES buffer Substances 0.000 description 3
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 description 3
- 108010002747 Pfu DNA polymerase Proteins 0.000 description 3
- 108091081024 Start codon Proteins 0.000 description 3
- 230000003213 activating effect Effects 0.000 description 3
- 238000013459 approach Methods 0.000 description 3
- 230000003115 biocidal effect Effects 0.000 description 3
- 210000000170 cell membrane Anatomy 0.000 description 3
- 230000001413 cellular effect Effects 0.000 description 3
- 210000003169 central nervous system Anatomy 0.000 description 3
- 230000008859 change Effects 0.000 description 3
- 239000003153 chemical reaction reagent Substances 0.000 description 3
- 238000004587 chromatography analysis Methods 0.000 description 3
- 210000001072 colon Anatomy 0.000 description 3
- 238000007796 conventional method Methods 0.000 description 3
- 229940079593 drug Drugs 0.000 description 3
- 238000005516 engineering process Methods 0.000 description 3
- 210000003527 eukaryotic cell Anatomy 0.000 description 3
- 230000004941 influx Effects 0.000 description 3
- 239000012528 membrane Substances 0.000 description 3
- 230000028161 membrane depolarization Effects 0.000 description 3
- MYWUZJCMWCOHBA-VIFPVBQESA-N methamphetamine Chemical compound CN[C@@H](C)CC1=CC=CC=C1 MYWUZJCMWCOHBA-VIFPVBQESA-N 0.000 description 3
- 239000002858 neurotransmitter agent Substances 0.000 description 3
- 230000010412 perfusion Effects 0.000 description 3
- 230000000144 pharmacologic effect Effects 0.000 description 3
- 239000002464 receptor antagonist Substances 0.000 description 3
- 229940044551 receptor antagonist Drugs 0.000 description 3
- 239000007790 solid phase Substances 0.000 description 3
- 241000894007 species Species 0.000 description 3
- 238000012546 transfer Methods 0.000 description 3
- 241000701447 unidentified baculovirus Species 0.000 description 3
- KDCGOANMDULRCW-UHFFFAOYSA-N 7H-purine Chemical compound N1=CNC2=NC=NC2=C1 KDCGOANMDULRCW-UHFFFAOYSA-N 0.000 description 2
- 229930024421 Adenine Natural products 0.000 description 2
- GFFGJBXGBJISGV-UHFFFAOYSA-N Adenine Chemical compound NC1=NC=NC2=C1N=CN2 GFFGJBXGBJISGV-UHFFFAOYSA-N 0.000 description 2
- 102000007698 Alcohol dehydrogenase Human genes 0.000 description 2
- 108010021809 Alcohol dehydrogenase Proteins 0.000 description 2
- 241000894006 Bacteria Species 0.000 description 2
- 241000701822 Bovine papillomavirus Species 0.000 description 2
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 2
- 108020004705 Codon Proteins 0.000 description 2
- 206010010774 Constipation Diseases 0.000 description 2
- 241000701022 Cytomegalovirus Species 0.000 description 2
- 102000012410 DNA Ligases Human genes 0.000 description 2
- 108010061982 DNA Ligases Proteins 0.000 description 2
- 108010014303 DNA-directed DNA polymerase Proteins 0.000 description 2
- 102000016928 DNA-directed DNA polymerase Human genes 0.000 description 2
- 108091006027 G proteins Proteins 0.000 description 2
- 102000030782 GTP binding Human genes 0.000 description 2
- 108091000058 GTP-Binding Proteins 0.000 description 2
- 229930182566 Gentamicin Natural products 0.000 description 2
- CEAZRRDELHUEMR-URQXQFDESA-N Gentamicin Chemical compound O1[C@H](C(C)NC)CC[C@@H](N)[C@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](NC)[C@@](C)(O)CO2)O)[C@H](N)C[C@@H]1N CEAZRRDELHUEMR-URQXQFDESA-N 0.000 description 2
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 description 2
- DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
- 206010062767 Hypophysitis Diseases 0.000 description 2
- 102100034343 Integrase Human genes 0.000 description 2
- ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 2
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 2
- 102000004086 Ligand-Gated Ion Channels Human genes 0.000 description 2
- 108090000543 Ligand-Gated Ion Channels Proteins 0.000 description 2
- 241000829100 Macaca mulatta polyomavirus 1 Species 0.000 description 2
- 102100037606 P2X purinoceptor 6 Human genes 0.000 description 2
- 101710190089 P2X purinoceptor 6 Proteins 0.000 description 2
- 102000003946 Prolactin Human genes 0.000 description 2
- 108010057464 Prolactin Proteins 0.000 description 2
- 102000002298 Purinergic P2Y Receptors Human genes 0.000 description 2
- 108010000818 Purinergic P2Y Receptors Proteins 0.000 description 2
- 108010092799 RNA-directed DNA polymerase Proteins 0.000 description 2
- JQYMGXZJTCOARG-UHFFFAOYSA-N Reactive blue 2 Chemical compound C1=2C(=O)C3=CC=CC=C3C(=O)C=2C(N)=C(S(O)(=O)=O)C=C1NC(C=C1S(O)(=O)=O)=CC=C1NC(N=1)=NC(Cl)=NC=1NC1=CC=CC(S(O)(=O)=O)=C1 JQYMGXZJTCOARG-UHFFFAOYSA-N 0.000 description 2
- 241000714474 Rous sarcoma virus Species 0.000 description 2
- 238000012300 Sequence Analysis Methods 0.000 description 2
- 108020004682 Single-Stranded DNA Proteins 0.000 description 2
- 108020005038 Terminator Codon Proteins 0.000 description 2
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 2
- 241000700605 Viruses Species 0.000 description 2
- 241000269368 Xenopus laevis Species 0.000 description 2
- 229960000643 adenine Drugs 0.000 description 2
- OIRDTQYFTABQOQ-KQYNXXCUSA-N adenosine Chemical compound C1=NC=2C(N)=NC=NC=2N1[C@@H]1O[C@H](CO)[C@@H](O)[C@H]1O OIRDTQYFTABQOQ-KQYNXXCUSA-N 0.000 description 2
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 2
- 238000003556 assay Methods 0.000 description 2
- 229910001626 barium chloride Inorganic materials 0.000 description 2
- WDIHJSXYQDMJHN-UHFFFAOYSA-L barium chloride Chemical compound [Cl-].[Cl-].[Ba+2] WDIHJSXYQDMJHN-UHFFFAOYSA-L 0.000 description 2
- 230000005540 biological transmission Effects 0.000 description 2
- 210000004556 brain Anatomy 0.000 description 2
- 239000000872 buffer Substances 0.000 description 2
- 239000001110 calcium chloride Substances 0.000 description 2
- 229910001628 calcium chloride Inorganic materials 0.000 description 2
- 235000011148 calcium chloride Nutrition 0.000 description 2
- 238000012512 characterization method Methods 0.000 description 2
- 239000013599 cloning vector Substances 0.000 description 2
- 238000010276 construction Methods 0.000 description 2
- 230000001086 cytosolic effect Effects 0.000 description 2
- 238000013461 design Methods 0.000 description 2
- 238000009826 distribution Methods 0.000 description 2
- 231100000673 dose–response relationship Toxicity 0.000 description 2
- 206010015037 epilepsy Diseases 0.000 description 2
- 238000002474 experimental method Methods 0.000 description 2
- 238000000605 extraction Methods 0.000 description 2
- 230000001605 fetal effect Effects 0.000 description 2
- 230000002068 genetic effect Effects 0.000 description 2
- 229960002518 gentamicin Drugs 0.000 description 2
- 210000002768 hair cell Anatomy 0.000 description 2
- NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
- 230000001057 ionotropic effect Effects 0.000 description 2
- 210000003734 kidney Anatomy 0.000 description 2
- 230000007246 mechanism Effects 0.000 description 2
- 230000001404 mediated effect Effects 0.000 description 2
- 230000004048 modification Effects 0.000 description 2
- 238000012986 modification Methods 0.000 description 2
- 238000010369 molecular cloning Methods 0.000 description 2
- 210000005036 nerve Anatomy 0.000 description 2
- 208000015122 neurodegenerative disease Diseases 0.000 description 2
- 210000002569 neuron Anatomy 0.000 description 2
- 210000000584 nodose ganglion Anatomy 0.000 description 2
- 210000002985 organ of corti Anatomy 0.000 description 2
- 210000001672 ovary Anatomy 0.000 description 2
- 230000035699 permeability Effects 0.000 description 2
- 210000003635 pituitary gland Anatomy 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 229940097325 prolactin Drugs 0.000 description 2
- 238000000746 purification Methods 0.000 description 2
- 239000002287 radioligand Substances 0.000 description 2
- 239000011535 reaction buffer Substances 0.000 description 2
- 230000009257 reactivity Effects 0.000 description 2
- 239000000018 receptor agonist Substances 0.000 description 2
- 229940044601 receptor agonist Drugs 0.000 description 2
- 230000001105 regulatory effect Effects 0.000 description 2
- 230000002441 reversible effect Effects 0.000 description 2
- 238000012216 screening Methods 0.000 description 2
- 238000012163 sequencing technique Methods 0.000 description 2
- 238000002741 site-directed mutagenesis Methods 0.000 description 2
- 230000009870 specific binding Effects 0.000 description 2
- 210000003594 spinal ganglia Anatomy 0.000 description 2
- 230000000638 stimulation Effects 0.000 description 2
- 238000001356 surgical procedure Methods 0.000 description 2
- 230000002103 transcriptional effect Effects 0.000 description 2
- 230000009466 transformation Effects 0.000 description 2
- 230000001052 transient effect Effects 0.000 description 2
- 239000001226 triphosphate Substances 0.000 description 2
- 235000011178 triphosphate Nutrition 0.000 description 2
- 125000002264 triphosphate group Chemical class [H]OP(=O)(O[H])OP(=O)(O[H])OP(=O)(O[H])O* 0.000 description 2
- 241000701161 unidentified adenovirus Species 0.000 description 2
- PNFZSRRRZNXSMF-UHFFFAOYSA-N 5'-phosphopyridoxal-6-azobenzene-2,4-disulfonic acid Chemical compound O=CC1=C(O)C(C)=NC(N=NC=2C(=CC(=CC=2)S(O)(=O)=O)S(O)(=O)=O)=C1COP(O)(O)=O PNFZSRRRZNXSMF-UHFFFAOYSA-N 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- 102100034044 All-trans-retinol dehydrogenase [NAD(+)] ADH1B Human genes 0.000 description 1
- 101710193111 All-trans-retinol dehydrogenase [NAD(+)] ADH4 Proteins 0.000 description 1
- 241000269350 Anura Species 0.000 description 1
- 101100163849 Arabidopsis thaliana ARS1 gene Proteins 0.000 description 1
- 239000004475 Arginine Substances 0.000 description 1
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
- 206010003571 Astrocytoma Diseases 0.000 description 1
- 241000193830 Bacillus <bacterium> Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 239000002126 C01EB10 - Adenosine Substances 0.000 description 1
- 101100448444 Caenorhabditis elegans gsp-3 gene Proteins 0.000 description 1
- OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 description 1
- 241000700199 Cavia porcellus Species 0.000 description 1
- 102000029816 Collagenase Human genes 0.000 description 1
- 108060005980 Collagenase Proteins 0.000 description 1
- 241000699800 Cricetinae Species 0.000 description 1
- 241000699802 Cricetulus griseus Species 0.000 description 1
- 201000003883 Cystic fibrosis Diseases 0.000 description 1
- 108050009160 DNA polymerase 1 Proteins 0.000 description 1
- 230000007018 DNA scission Effects 0.000 description 1
- 206010012735 Diarrhoea Diseases 0.000 description 1
- 206010063602 Exposure to noise Diseases 0.000 description 1
- 101150092780 GSP1 gene Proteins 0.000 description 1
- 101150035751 GSP2 gene Proteins 0.000 description 1
- 108700028146 Genetic Enhancer Elements Proteins 0.000 description 1
- 108700007698 Genetic Terminator Regions Proteins 0.000 description 1
- 239000004471 Glycine Substances 0.000 description 1
- 108020005350 Initiator Codon Proteins 0.000 description 1
- 229930010555 Inosine Natural products 0.000 description 1
- UGQMRVRMYYASKQ-KQYNXXCUSA-N Inosine Chemical compound O[C@@H]1[C@H](O)[C@@H](CO)O[C@H]1N1C2=NC=NC(O)=C2N=C1 UGQMRVRMYYASKQ-KQYNXXCUSA-N 0.000 description 1
- 102000004877 Insulin Human genes 0.000 description 1
- 108090001061 Insulin Proteins 0.000 description 1
- 108090000862 Ion Channels Proteins 0.000 description 1
- 102000004310 Ion Channels Human genes 0.000 description 1
- 241000235058 Komagataella pastoris Species 0.000 description 1
- ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
- 125000000570 L-alpha-aspartyl group Chemical group [H]OC(=O)C([H])([H])[C@]([H])(N([H])[H])C(*)=O 0.000 description 1
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
- 125000000010 L-asparaginyl group Chemical group O=C([*])[C@](N([H])[H])([H])C([H])([H])C(=O)N([H])[H] 0.000 description 1
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 description 1
- AGPKZVBTJJNPAG-WHFBIAKZSA-N L-isoleucine Chemical compound CC[C@H](C)[C@H](N)C(O)=O AGPKZVBTJJNPAG-WHFBIAKZSA-N 0.000 description 1
- 125000002061 L-isoleucyl group Chemical group [H]N([H])[C@]([H])(C(=O)[*])[C@](C([H])([H])[H])([H])C(C([H])([H])[H])([H])[H] 0.000 description 1
- 125000001176 L-lysyl group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C([H])([H])C([H])([H])C([H])([H])C(N([H])[H])([H])[H] 0.000 description 1
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 description 1
- 125000003580 L-valyl group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C(C([H])([H])[H])(C([H])([H])[H])[H] 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- 102000004856 Lectins Human genes 0.000 description 1
- 108090001090 Lectins Proteins 0.000 description 1
- ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 1
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 1
- 239000004472 Lysine Substances 0.000 description 1
- 206010028980 Neoplasm Diseases 0.000 description 1
- 101710163270 Nuclease Proteins 0.000 description 1
- 108020005187 Oligonucleotide Probes Proteins 0.000 description 1
- 102000015636 Oligopeptides Human genes 0.000 description 1
- 108010038807 Oligopeptides Proteins 0.000 description 1
- 102100037603 P2X purinoceptor 5 Human genes 0.000 description 1
- 101710189969 P2X purinoceptor 5 Proteins 0.000 description 1
- 102100037602 P2X purinoceptor 7 Human genes 0.000 description 1
- 101710189965 P2X purinoceptor 7 Proteins 0.000 description 1
- 108091000080 Phosphotransferase Proteins 0.000 description 1
- 108010021757 Polynucleotide 5'-Hydroxyl-Kinase Proteins 0.000 description 1
- 102000008422 Polynucleotide 5'-hydroxyl-kinase Human genes 0.000 description 1
- ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
- 241000589516 Pseudomonas Species 0.000 description 1
- 108010080192 Purinergic Receptors Proteins 0.000 description 1
- 108020004511 Recombinant DNA Proteins 0.000 description 1
- 102000007056 Recombinant Fusion Proteins Human genes 0.000 description 1
- 108010008281 Recombinant Fusion Proteins Proteins 0.000 description 1
- 108091028664 Ribonucleotide Proteins 0.000 description 1
- 241001123227 Saccharomyces pastorianus Species 0.000 description 1
- 101100097319 Schizosaccharomyces pombe (strain 972 / ATCC 24843) ala1 gene Proteins 0.000 description 1
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
- 239000004098 Tetracycline Substances 0.000 description 1
- AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 1
- 239000004473 Threonine Substances 0.000 description 1
- 229920004890 Triton X-100 Polymers 0.000 description 1
- 239000013504 Triton X-100 Substances 0.000 description 1
- IXKSXJFAGXLQOQ-XISFHERQSA-N WHWLQLKPGQPMY Chemical compound C([C@@H](C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N1CCC[C@H]1C(=O)NCC(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)NC(=O)[C@@H](N)CC=1C2=CC=CC=C2NC=1)C1=CNC=N1 IXKSXJFAGXLQOQ-XISFHERQSA-N 0.000 description 1
- 241000269370 Xenopus <genus> Species 0.000 description 1
- JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 1
- XNOBOKJVOTYSJV-KQYNXXCUSA-N [[(2r,3s,4r,5r)-5-(6-amino-2-methylsulfanylpurin-9-yl)-3,4-dihydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl] phosphono hydrogen phosphate Chemical compound C12=NC(SC)=NC(N)=C2N=CN1[C@@H]1O[C@H](COP(O)(=O)OP(O)(=O)OP(O)(O)=O)[C@@H](O)[C@H]1O XNOBOKJVOTYSJV-KQYNXXCUSA-N 0.000 description 1
- 230000021736 acetylation Effects 0.000 description 1
- 238000006640 acetylation reaction Methods 0.000 description 1
- 239000002253 acid Substances 0.000 description 1
- 230000036982 action potential Effects 0.000 description 1
- 229960005305 adenosine Drugs 0.000 description 1
- 230000001919 adrenal effect Effects 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 239000011543 agarose gel Substances 0.000 description 1
- 238000000246 agarose gel electrophoresis Methods 0.000 description 1
- 230000032683 aging Effects 0.000 description 1
- 238000013019 agitation Methods 0.000 description 1
- 235000004279 alanine Nutrition 0.000 description 1
- VREFGVBLTWBCJP-UHFFFAOYSA-N alprazolam Chemical compound C12=CC(Cl)=CC=C2N2C(C)=NN=C2CN=C1C1=CC=CC=C1 VREFGVBLTWBCJP-UHFFFAOYSA-N 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 238000012870 ammonium sulfate precipitation Methods 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 229960000723 ampicillin Drugs 0.000 description 1
- AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
- 230000000202 analgesic effect Effects 0.000 description 1
- 229940035676 analgesics Drugs 0.000 description 1
- 238000010171 animal model Methods 0.000 description 1
- 238000005571 anion exchange chromatography Methods 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 239000000730 antalgic agent Substances 0.000 description 1
- 230000009118 appropriate response Effects 0.000 description 1
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 description 1
- 235000009582 asparagine Nutrition 0.000 description 1
- 229960001230 asparagine Drugs 0.000 description 1
- 235000003704 aspartic acid Nutrition 0.000 description 1
- 210000003050 axon Anatomy 0.000 description 1
- 230000003542 behavioural effect Effects 0.000 description 1
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 description 1
- 239000012472 biological sample Substances 0.000 description 1
- 210000004369 blood Anatomy 0.000 description 1
- 239000008280 blood Substances 0.000 description 1
- 210000001124 body fluid Anatomy 0.000 description 1
- 239000010839 body fluid Substances 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 210000005013 brain tissue Anatomy 0.000 description 1
- 239000006227 byproduct Substances 0.000 description 1
- 229910052791 calcium Inorganic materials 0.000 description 1
- 239000011575 calcium Substances 0.000 description 1
- 230000010221 calcium permeability Effects 0.000 description 1
- 201000011510 cancer Diseases 0.000 description 1
- 150000003943 catecholamines Chemical class 0.000 description 1
- 238000005277 cation exchange chromatography Methods 0.000 description 1
- 125000002091 cationic group Chemical group 0.000 description 1
- 150000001768 cations Chemical class 0.000 description 1
- 238000004113 cell culture Methods 0.000 description 1
- 230000009134 cell regulation Effects 0.000 description 1
- 239000007795 chemical reaction product Substances 0.000 description 1
- 239000003795 chemical substances by application Substances 0.000 description 1
- 229960005091 chloramphenicol Drugs 0.000 description 1
- WIIZWVCIJKGZOK-RKDXNWHRSA-N chloramphenicol Chemical compound ClC(Cl)C(=O)N[C@H](CO)[C@H](O)C1=CC=C([N+]([O-])=O)C=C1 WIIZWVCIJKGZOK-RKDXNWHRSA-N 0.000 description 1
- 210000003737 chromaffin cell Anatomy 0.000 description 1
- 210000000349 chromosome Anatomy 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 210000003477 cochlea Anatomy 0.000 description 1
- 210000000860 cochlear nerve Anatomy 0.000 description 1
- 229960002424 collagenase Drugs 0.000 description 1
- 230000006835 compression Effects 0.000 description 1
- 238000007906 compression Methods 0.000 description 1
- 230000008878 coupling Effects 0.000 description 1
- 238000010168 coupling process Methods 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 230000001351 cycling effect Effects 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 239000005547 deoxyribonucleotide Substances 0.000 description 1
- 125000002637 deoxyribonucleotide group Chemical group 0.000 description 1
- 230000001419 dependent effect Effects 0.000 description 1
- 206010012601 diabetes mellitus Diseases 0.000 description 1
- 201000010099 disease Diseases 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- 210000003027 ear inner Anatomy 0.000 description 1
- 238000002001 electrophysiology Methods 0.000 description 1
- 230000007831 electrophysiology Effects 0.000 description 1
- 210000003060 endolymph Anatomy 0.000 description 1
- 210000005216 enteric neuron Anatomy 0.000 description 1
- 238000009585 enzyme analysis Methods 0.000 description 1
- 238000001976 enzyme digestion Methods 0.000 description 1
- 210000002919 epithelial cell Anatomy 0.000 description 1
- 238000012869 ethanol precipitation Methods 0.000 description 1
- 230000002964 excitative effect Effects 0.000 description 1
- 210000004186 follicle cell Anatomy 0.000 description 1
- 102000037865 fusion proteins Human genes 0.000 description 1
- 108020001507 fusion proteins Proteins 0.000 description 1
- 230000007661 gastrointestinal function Effects 0.000 description 1
- 239000000499 gel Substances 0.000 description 1
- 210000004907 gland Anatomy 0.000 description 1
- 239000011521 glass Substances 0.000 description 1
- 229930195712 glutamate Natural products 0.000 description 1
- 235000013922 glutamic acid Nutrition 0.000 description 1
- 239000004220 glutamic acid Substances 0.000 description 1
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
- 230000002414 glycolytic effect Effects 0.000 description 1
- 230000013595 glycosylation Effects 0.000 description 1
- 238000006206 glycosylation reaction Methods 0.000 description 1
- 125000003630 glycyl group Chemical group [H]N([H])C([H])([H])C(*)=O 0.000 description 1
- XMHIUKTWLZUKEX-UHFFFAOYSA-N hexacosanoic acid Chemical compound CCCCCCCCCCCCCCCCCCCCCCCCCC(O)=O XMHIUKTWLZUKEX-UHFFFAOYSA-N 0.000 description 1
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 description 1
- 230000003054 hormonal effect Effects 0.000 description 1
- 230000007062 hydrolysis Effects 0.000 description 1
- 238000006460 hydrolysis reaction Methods 0.000 description 1
- 238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 1
- 208000026278 immune system disease Diseases 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000000099 in vitro assay Methods 0.000 description 1
- 238000001727 in vivo Methods 0.000 description 1
- 238000010348 incorporation Methods 0.000 description 1
- 230000006698 induction Effects 0.000 description 1
- 208000015181 infectious disease Diseases 0.000 description 1
- 230000036512 infertility Effects 0.000 description 1
- 208000027866 inflammatory disease Diseases 0.000 description 1
- 230000005764 inhibitory process Effects 0.000 description 1
- 229960003786 inosine Drugs 0.000 description 1
- 229940125396 insulin Drugs 0.000 description 1
- 230000010354 integration Effects 0.000 description 1
- 150000002500 ions Chemical class 0.000 description 1
- 238000002955 isolation Methods 0.000 description 1
- AGPKZVBTJJNPAG-UHFFFAOYSA-N isoleucine Natural products CCC(C)C(N)C(O)=O AGPKZVBTJJNPAG-UHFFFAOYSA-N 0.000 description 1
- 229960000310 isoleucine Drugs 0.000 description 1
- 238000005304 joining Methods 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 239000002523 lectin Substances 0.000 description 1
- 238000004811 liquid chromatography Methods 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 229920002521 macromolecule Polymers 0.000 description 1
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 150000002739 metals Chemical class 0.000 description 1
- 229930182817 methionine Natural products 0.000 description 1
- 244000005700 microbiome Species 0.000 description 1
- 239000003068 molecular probe Substances 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 210000002464 muscle smooth vascular Anatomy 0.000 description 1
- 210000001640 nerve ending Anatomy 0.000 description 1
- 230000001537 neural effect Effects 0.000 description 1
- 230000004770 neurodegeneration Effects 0.000 description 1
- 230000000955 neuroendocrine Effects 0.000 description 1
- 208000018360 neuromuscular disease Diseases 0.000 description 1
- 210000000607 neurosecretory system Anatomy 0.000 description 1
- 230000003040 nociceptive effect Effects 0.000 description 1
- 230000008055 nociceptive signaling Effects 0.000 description 1
- 238000007899 nucleic acid hybridization Methods 0.000 description 1
- 235000015097 nutrients Nutrition 0.000 description 1
- 239000002751 oligonucleotide probe Substances 0.000 description 1
- 238000004806 packaging method and process Methods 0.000 description 1
- 230000003076 paracrine Effects 0.000 description 1
- 239000002245 particle Substances 0.000 description 1
- 230000001575 pathological effect Effects 0.000 description 1
- 230000007310 pathophysiology Effects 0.000 description 1
- XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 description 1
- 210000001428 peripheral nervous system Anatomy 0.000 description 1
- 239000008177 pharmaceutical agent Substances 0.000 description 1
- 239000012071 phase Substances 0.000 description 1
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 description 1
- 229940080469 phosphocellulose Drugs 0.000 description 1
- 230000026731 phosphorylation Effects 0.000 description 1
- 238000006366 phosphorylation reaction Methods 0.000 description 1
- 102000020233 phosphotransferase Human genes 0.000 description 1
- 230000001766 physiological effect Effects 0.000 description 1
- 230000035479 physiological effects, processes and functions Effects 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
- 238000003752 polymerase chain reaction Methods 0.000 description 1
- 239000011148 porous material Substances 0.000 description 1
- 230000004481 post-translational protein modification Effects 0.000 description 1
- 229940124606 potential therapeutic agent Drugs 0.000 description 1
- 230000003389 potentiating effect Effects 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 238000012545 processing Methods 0.000 description 1
- 210000001236 prokaryotic cell Anatomy 0.000 description 1
- 230000001915 proofreading effect Effects 0.000 description 1
- 238000001742 protein purification Methods 0.000 description 1
- 230000030788 protein refolding Effects 0.000 description 1
- 239000002213 purine nucleotide Substances 0.000 description 1
- 239000002719 pyrimidine nucleotide Substances 0.000 description 1
- 150000003230 pyrimidines Chemical class 0.000 description 1
- 230000002285 radioactive effect Effects 0.000 description 1
- 239000011541 reaction mixture Substances 0.000 description 1
- 238000003757 reverse transcription PCR Methods 0.000 description 1
- 239000002336 ribonucleotide Substances 0.000 description 1
- 125000002652 ribonucleotide group Chemical group 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 238000005204 segregation Methods 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 210000000413 sensory ganglia Anatomy 0.000 description 1
- 210000001044 sensory neuron Anatomy 0.000 description 1
- 230000020341 sensory perception of pain Effects 0.000 description 1
- 230000019491 signal transduction Effects 0.000 description 1
- 210000002027 skeletal muscle Anatomy 0.000 description 1
- 210000002460 smooth muscle Anatomy 0.000 description 1
- 229910000030 sodium bicarbonate Inorganic materials 0.000 description 1
- VWDWKYIASSYTQR-UHFFFAOYSA-N sodium nitrate Inorganic materials [Na+].[O-][N+]([O-])=O VWDWKYIASSYTQR-UHFFFAOYSA-N 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 210000001323 spiral ganglion Anatomy 0.000 description 1
- 238000010561 standard procedure Methods 0.000 description 1
- 239000011550 stock solution Substances 0.000 description 1
- 238000001308 synthesis method Methods 0.000 description 1
- 229960002180 tetracycline Drugs 0.000 description 1
- 229930101283 tetracycline Natural products 0.000 description 1
- 235000019364 tetracycline Nutrition 0.000 description 1
- 150000003522 tetracyclines Chemical class 0.000 description 1
- QQJLHRRUATVHED-UHFFFAOYSA-N tramazoline Chemical compound N1CCN=C1NC1=CC=CC2=C1CCCC2 QQJLHRRUATVHED-UHFFFAOYSA-N 0.000 description 1
- 229960001262 tramazoline Drugs 0.000 description 1
- 230000002463 transducing effect Effects 0.000 description 1
- 238000010361 transduction Methods 0.000 description 1
- 230000026683 transduction Effects 0.000 description 1
- 229940072040 tricaine Drugs 0.000 description 1
- FQZJYWMRQDKBQN-UHFFFAOYSA-N tricaine methanesulfonate Chemical compound CS([O-])(=O)=O.CCOC(=O)C1=CC=CC([NH3+])=C1 FQZJYWMRQDKBQN-UHFFFAOYSA-N 0.000 description 1
- 231100000588 tumorigenic Toxicity 0.000 description 1
- 230000000381 tumorigenic effect Effects 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 241001515965 unidentified phage Species 0.000 description 1
- 210000004291 uterus Anatomy 0.000 description 1
- 210000001177 vas deferen Anatomy 0.000 description 1
- 230000006442 vascular tone Effects 0.000 description 1
- 230000029663 wound healing Effects 0.000 description 1
Classifications
-
- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/705—Receptors; Cell surface antigens; Cell surface determinants
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
-
- 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
-
- 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
- A61P25/04—Centrally acting analgesics, e.g. opioids
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P27/00—Drugs for disorders of the senses
- A61P27/16—Otologicals
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P43/00—Drugs for specific purposes, not provided for in groups A61P1/00-A61P41/00
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P5/00—Drugs for disorders of the endocrine system
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Medicinal Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Public Health (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Veterinary Medicine (AREA)
- Pharmacology & Pharmacy (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Animal Behavior & Ethology (AREA)
- Engineering & Computer Science (AREA)
- Neurology (AREA)
- Neurosurgery (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- Biophysics (AREA)
- Pain & Pain Management (AREA)
- Cell Biology (AREA)
- Immunology (AREA)
- Toxicology (AREA)
- Zoology (AREA)
- Gastroenterology & Hepatology (AREA)
- Endocrinology (AREA)
- Diabetes (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Peptides Or Proteins (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Investigating Or Analysing Biological Materials (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
L'invention concerne un polypeptide de récepteur purinergique P2X¿2? de l'homme. L'invention traite aussi des molécules d'acide nucléique codant ledit polypeptide et des vecteurs et des cellules hôtes contenant ces molécules d'acide nucléique. En outre, l'invention a pour objet des procédés de production du polypeptide du récepteur P2X¿2?, et des procédés d'utilisation de ces polypeptides et des cellules hôtes qui expriment ces derniers afin de détecter les composés présentant une activé sur le récepteur P2X¿2?. En outre, l'invention concerne les utilisations thérapeutiques ce de récepteur.
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US13745898A | 1998-08-20 | 1998-08-20 | |
| US09/137,458 | 1998-08-20 | ||
| PCT/US1999/019042 WO2000011167A2 (fr) | 1998-08-20 | 1999-08-20 | Acides nucleiques codant un purinorecepteur fonctionnel humain p2x2, et procedes de production et d'utilisation de ce dernier |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CA2339871A1 true CA2339871A1 (fr) | 2000-03-02 |
Family
ID=22477523
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CA002339871A Abandoned CA2339871A1 (fr) | 1998-08-20 | 1999-08-20 | Acides nucleiques codant un purinorecepteur fonctionnel humain p2x2, et procedes de production et d'utilisation de ce dernier |
Country Status (4)
| Country | Link |
|---|---|
| EP (1) | EP1104464A2 (fr) |
| JP (1) | JP2002523043A (fr) |
| CA (1) | CA2339871A1 (fr) |
| WO (1) | WO2000011167A2 (fr) |
Families Citing this family (3)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| DE10102050A1 (de) | 2001-01-17 | 2002-07-18 | Basf Ag | Zubereitung zur Verbesserung der Nahrungsverwertung |
| WO2003057898A2 (fr) * | 2001-12-31 | 2003-07-17 | Algos Therapeutics, Inc. | Methodes et materiels destines a la modulation de p2x2 |
| JP2005525112A (ja) * | 2002-02-28 | 2005-08-25 | ミレニアム・ファーマシューティカルズ・インコーポレイテッド | ジアシルグリセロールキナーゼεを使用して疼痛を処置する際の方法および組成物 |
Family Cites Families (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPH10501122A (ja) * | 1994-05-27 | 1998-02-03 | グラクソ、グループ、リミテッド | Ｐ▲下２ｘ▼レセプター（プリノセプターファミリー） |
| JP3885177B2 (ja) * | 1997-03-26 | 2007-02-21 | 大塚製薬株式会社 | ヒト遺伝子 |
-
1999
- 1999-08-20 JP JP2000566421A patent/JP2002523043A/ja active Pending
- 1999-08-20 EP EP99942377A patent/EP1104464A2/fr not_active Withdrawn
- 1999-08-20 CA CA002339871A patent/CA2339871A1/fr not_active Abandoned
- 1999-08-20 WO PCT/US1999/019042 patent/WO2000011167A2/fr not_active Ceased
Also Published As
| Publication number | Publication date |
|---|---|
| EP1104464A2 (fr) | 2001-06-06 |
| WO2000011167A2 (fr) | 2000-03-02 |
| WO2000011167A3 (fr) | 2000-10-05 |
| JP2002523043A (ja) | 2002-07-30 |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| US6323000B2 (en) | Variant human α7 acetylcholine receptor subunit, and methods of production and uses thereof | |
| US5728808A (en) | Human Prostaglandin receptor IP | |
| US6358694B1 (en) | Methods of identifying modulators of a prostaglandin receptor | |
| JPH10179178A (ja) | ヒト７回膜貫通型レセプター | |
| JPH10262687A (ja) | 新規ヒト１１ｃｂスプライス変種 | |
| US6391561B1 (en) | Protein that enhances expression of potassium channels on cell surfaces and nucleic acids that encode the same | |
| JP2002500633A (ja) | Ｅｄｇ−１様受容体 | |
| US6242216B1 (en) | Nucleic acids encoding a functional human purinoreceptor P2X2 and P2X4, and methods of production and use thereof | |
| JP2002505872A (ja) | ７回膜貫通ｇタンパク質共役受容体ｅｃｒ６７３ | |
| US6214581B1 (en) | Nucleic acids encoding a functional human purinoreceptor P2X3 and P2X6, and methods of production and use thereof | |
| CA2339871A1 (fr) | Acides nucleiques codant un purinorecepteur fonctionnel humain p2x2, et procedes de production et d'utilisation de ce dernier | |
| WO1999055901A2 (fr) | Technique de criblage fonctionnel de grande capacite servant a identifier des ligands de purinorecepteurs humains | |
| US7547521B2 (en) | Heteromultimeric ion channel receptor and uses thereof | |
| US20100221773A1 (en) | Nucleic Acids Encoding a Functional Mammalin Purinoreceptor, P2X3, Methods of Production and Use Thereof | |
| EP1045903A1 (fr) | Acides nucleiques codant un purinorecepteur fonctionnel humain p2x3 et procedes de production et d'utilisation de ces derniers | |
| MXPA01001855A (en) | Nucleic acids encoding a functional human purinoreceptor p2x2 | |
| US20020004222A1 (en) | Cloning of a monkey 7TM receptor (AXOR8) | |
| US7229779B2 (en) | Variant human α7 acetylcholine receptor subunit, and methods of production and use thereof | |
| US6355452B1 (en) | Human histamine H3 gene variant-2 | |
| CA2370659A1 (fr) | Recepteur p2x3, methodes destinees a modifier l'activite d'un recepteur p2x3 et leurs utilisations | |
| GB2345487A (en) | Polynucleotide and polypeptide sequence encoding rat mdr1a and screening methods thereof | |
| MXPA00006974A (en) | Nucleic acids encoding a functional human purinoreceptor p2x3 | |
| JPH10117791A (ja) | ヒトｇタンパク質結合受容体ｈｌｙａｚ６１ | |
| WO2001016298A1 (fr) | Clonage du recepteur gpr10 de la souris | |
| US20040106149A1 (en) | Novel gpcr hfrbn63 |
Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| EEER | Examination request | ||
| FZDE | Dead |