VIPR1

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Receptor vazoaktivnog intestinalnog peptida 1

Prikaz baziran na PDB 1OF2
Dostupne strukture
1OF2, 1OGT, 3B3I
Identifikatori
SimboliVIPR1; HVR1; II; PACAP-R-2; PACAP-R2; RDC1; V1RG; VAPC1; VIP-R-1; VIPR; VIRG; VPAC1; VPAC1R; VPCAP1R
Vanjski IDOMIM: 192321 MGI: 109272 HomoloGene: 3399 IUPHAR: VPAC1 GeneCards: VIPR1 Gene
Ontologija gena
Molekularna funkcija • aktivnost vazoaktivnog intestinalnog polipeptidnog receptora
Celularna komponenta • jedro
• nukleolus
• citoplazma
• ćelijska membrana
Biološki proces • mišićne kontrakcije
• imunski sistem
• signalni put G-protein spregnutog receptora
Pregled RNK izražavanja
podaci
Ortolozi
VrstaČovekMiš
Entrez743322354
EnsemblENSG00000114812ENSMUSG00000032528
UniProtP32241P97751
RefSeq (mRNA)NM_001251882.1NM_011703.4
RefSeq (protein)NP_001238811.1NP_035833.2
Lokacija (UCSC)Chr 3:
42.53 - 42.58 Mb		Chr 9:
121.55 - 121.58 Mb
PubMed pretraga[1][2]

Receptor vazoaktivnog intestinalnog peptida 1 (VPAC1) je protein koji je kod ljudi kodiran VIPR1 genom.[1] VPAC1 je izražen u mozgu (cerebralni korteks, hiokampus, amigdala), plućima, prostati, perifernim krvnim leukocitima, jetri, tankim crevima, srcu, slezini, posteljici, bubrezima, grudnoj žlezdi i testisima.[2][3][4]

Function

VPAC1 je receptor za neuropeptid vazoaktivni intestinalni peptid (VIP). Taj peptid učestvuje u relaksaciji glatkih mišića, egzokrinoj i endokrinoj sekreciji, i protoku vode i jona u plućima i intestinalnom epitelnom tkivu. Njegovo dejstvo se ispoljava putem integralnih membranskih receptora asociranih sa G proteinima koji aktiviraju adenilat ciklazu.[1]

VIP deluje na autokrini način putem VPAC11 da inhibira proliferaciju megakariocita i indukuje formiranje protrombocita.[5][6]

Reference

  1. ↑ 1,0 1,1 „Entrez Gene: VIPR1 vasoactive intestinal peptide receptor 1”. 
  2. ↑ Ishihara T, Shigemoto R, Mori K, Takahashi K, Nagata S. (1992). „Functional expression and tissue distribution of a novel receptor for vasoactive intestinal polypeptide.”. Neuron 8 (4): 811–819. DOI:10.1016/0896-6273(92)90101-I. PMID 1314625. 
  3. ↑ Usdin TB, Bonner TI, Mezey E. (1994). „Two receptors for vasoactive intestinal polypeptide with similar specificity and complementary distributions.”. Endocrinology 135 (6): 2662–2680. DOI:10.1210/en.135.6.2662. PMID 7988457. 
  4. ↑ Sreedharan SP, Huang JX, Cheung MC, Goetzl EJ. (1995). „Structure, expression, and chromosomal localization of the type I human vasoactive intestinal peptide receptor gene”. Proc Natl Acad Sci USA 92 (7): 2939–2943. DOI:10.1073/pnas.92.7.2939. PMC 42334. PMID 7708752. 
  5. ↑ Nam, C.; Case, A. J.; Hostager, B. S.; O’Dorisio, M. S. (2008). „The Role of Vasoactive Intestinal Peptide (VIP) in Megakaryocyte Proliferation”. Journal of Molecular Neuroscience 37 (2): 160–167. DOI:10.1007/s12031-008-9119-x. PMID 18663606. 
  6. ↑ Freson, K.; Peeters, K.; De Vos, R.; Wittevrongel, C.; Thys, C.; Hoylaerts, M. F.; Vermylen, J.; Van Geet, C. (2007). „PACAP and its receptor VPAC1 regulate megakaryocyte maturation: Therapeutic implications”. Blood 111 (4): 1885–1893. DOI:10.1182/blood-2007-06-098558. PMID 18000164. 

Literatura

  • „Quaternary structure of rabbit skeletal muscle glycogen synthetase” [Quaternary structure of rabbit skeletal muscle glycogen synthetase]. Doklady Akademii Nauk SSSR 222 (4): 997–1000. 1975. PMID 807467. 
  • Sreedharan SP, Huang JX, Cheung MC, Goetzl EJ (1995). „Structure, expression, and chromosomal localization of the type I human vasoactive intestinal peptide receptor gene”. Proc. Natl. Acad. Sci. U.S.A. 92 (7): 2939–43. DOI:10.1073/pnas.92.7.2939. PMC 42334. PMID 7708752. 
  • Couvineau A, Gaudin P, Maoret JJ, et al. (1995). „Highly conserved aspartate 68, tryptophane 73 and glycine 109 in the N-terminal extracellular domain of the human VIP receptor are essential for its ability to bind VIP”. Biochem. Biophys. Res. Commun. 206 (1): 246–52. DOI:10.1006/bbrc.1995.1034. PMID 7818527. 
  • Gagnon AW, Aiyar N, Elshourbagy NA (1994). „Molecular cloning and functional characterization of a human liver vasoactive intestinal peptide receptor”. Cell. Signal. 6 (3): 321–33. DOI:10.1016/0898-6568(94)90037-X. PMID 7917790. 
  • Sreedharan SP, Patel DR, Xia M, et al. (1994). „Human vasoactive intestinal peptide1 receptors expressed by stable transfectants couple to two distinct signaling pathways”. Biochem. Biophys. Res. Commun. 203 (1): 141–8. DOI:10.1006/bbrc.1994.2160. PMID 8074647. 
  • Couvineau A, Rouyer-Fessard C, Darmoul D, et al. (1994). „Human intestinal VIP receptor: cloning and functional expression of two cDNA encoding proteins with different N-terminal domains”. Biochem. Biophys. Res. Commun. 200 (2): 769–76. DOI:10.1006/bbrc.1994.1517. PMID 8179610. 
  • Moody TW, Zia F, Draoui M, et al. (1993). „A vasoactive intestinal peptide antagonist inhibits non-small cell lung cancer growth”. Proc. Natl. Acad. Sci. U.S.A. 90 (10): 4345–9. DOI:10.1073/pnas.90.10.4345. PMC 46507. PMID 8389448. 
  • Sreedharan SP, Patel DR, Huang JX, Goetzl EJ (1993). „Cloning and functional expression of a human neuroendocrine vasoactive intestinal peptide receptor”. Biochem. Biophys. Res. Commun. 193 (2): 546–53. DOI:10.1006/bbrc.1993.1658. PMID 8390245. 
  • Couvineau A, Fabre C, Gaudin P, et al. (1996). „Mutagenesis of N-glycosylation sites in the human vasoactive intestinal peptide 1 receptor. Evidence that asparagine 58 or 69 is crucial for correct delivery of the receptor to plasma membrane”. Biochemistry 35 (6): 1745–52. DOI:10.1021/bi952022h. PMID 8639654. 
  • Pozo D, Guerrero JM, Segura JJ, Calvo JR (1997). „Thymosin alpha 1 interacts with the VIP receptor-effector system in rat and mouse immunocompetent cells”. Immunopharmacology 34 (2–3): 113–23. DOI:10.1016/0162-3109(96)00131-2. PMID 8886855. 
  • Couvineau A, Maoret JJ, Rouyer-Fessard C, et al. (1999). „Cloning and functional characterization of the human VIP1/PACAP receptor promoter”. Ann. N. Y. Acad. Sci. 865: 59–63. DOI:10.1111/j.1749-6632.1998.tb11163.x. PMID 9927997. 
  • Knudsen SM, Tams JW, Wulff BS, Fahrenkrug J (1999). „Importance of conserved cysteines in the extracellular loops of human PACAP/VIP1 receptor for ligand binding and stimulation of cAMP production”. Ann. N. Y. Acad. Sci. 865: 259–65. DOI:10.1111/j.1749-6632.1998.tb11186.x. PMID 9928020. 
  • Marie J, Wakkach A, Coudray A, et al. (1999). „Functional expression of receptors for calcitonin gene-related peptide, calcitonin, and vasoactive intestinal peptide in the human thymus and thymomas from myasthenia gravis patients”. J. Immunol. 162 (4): 2103–12. PMID 9973484. 
  • Mimuro H, Suzuki T, Suetsugu S, et al. (2000). „Profilin is required for sustaining efficient intra- and intercellular spreading of Shigella flexneri”. J. Biol. Chem. 275 (37): 28893–901. DOI:10.1074/jbc.M003882200. PMID 10867004. 
  • Nicole P, Maoret JJ, Couvineau A, et al. (2000). „Tryptophan 67 in the human VPAC(1) receptor: crucial role for VIP binding”. Biochem. Biophys. Res. Commun. 276 (2): 654–9. DOI:10.1006/bbrc.2000.3375. PMID 11027527. 
  • Bajo AM, Juarranz MG, Valenzuela P, et al. (2001). „Expression of vasoactive intestinal peptide (VIP) receptors in human uterus”. Peptides 21 (9): 1383–8. DOI:10.1016/S0196-9781(00)00282-5. PMID 11072126. 
  • Lara-Marquez M, O'Dorisio M, O'Dorisio T, et al. (2001). „Selective gene expression and activation-dependent regulation of vasoactive intestinal peptide receptor type 1 and type 2 in human T cells”. J. Immunol. 166 (4): 2522–30. PMID 11160313. 
  • Martin Shreeve S (2002). „Identification of G-proteins coupling to the vasoactive intestinal peptide receptor VPAC(1) using immunoaffinity chromatography: evidence for precoupling”. Biochem. Biophys. Res. Commun. 290 (4): 1300–7. DOI:10.1006/bbrc.2002.6342. PMID 11812005. 
  • Dorsam G, Goetzl EJ (2002). „Vasoactive intestinal peptide receptor-1 (VPAC-1) is a novel gene target of the hemolymphopoietic transcription factor Ikaros”. J. Biol. Chem. 277 (16): 13488–93. DOI:10.1074/jbc.M107922200. PMID 11812772. 
  • Branch DR, Valenta LJ, Yousefi S, et al. (2002). „VPAC1 is a cellular neuroendocrine receptor expressed on T cells that actively facilitates productive HIV-1 infection”. AIDS 16 (3): 309–19. DOI:10.1097/00002030-200202150-00001. PMID 11834941. 

Vidi još

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Klasa A: Rodopsinu slični
α1 (A, B, D) • α2 (A, B, C) • β1 • β2 • β3
Adenozinski (A1, A2A, A2B, A3) • P2Y (1, 2, 4, 5, 6, 8, 9, 10, 11, 12, 13, 14)
(svi osim 5-HT3) 5-HT1 (A, B, D, E, F) • 5-HT2 (A, B, C) • 5-HT (4, 5A, 6, 7)
Drugi
Acetilholin (M1, M2, M3, M4, M5) • Dopamin (D1, D2, D3, D4, D5) • Histamin (H1, H2, H3, H4) • Melatonin (1A, 1B, 1C) • TAAR (1, 2, 3, 5, 6, 8, 9)
Metaboliti i
signalni molekuli
CysLT (1, 2) • LTB4 (1, 2) • FPRL1 • OXE • Prostaglandin (DP (1, 2), EP (1, 2, 3, 4), FP) • Prostaciklin • Tromboksan
Drugi
Žučna kiselina • Kanabinoidni (CB1, CB2, GPR (18, 55, 119)) • EBI2 • Estrogen • Slobodna masna kiselina (1, 2, 3, 4) • Laktat  • Lizofosfatidna kiselina (1, 2, 3, 4, 5, 6)  • Lizofosfolipid (1, 2, 3, 4, 5, 6, 7, 8) • Niacin (1, 2) • Oksoglutarat • PAF • Sfingozin-1-fosfat (1, 2, 3, 4, 5) • Sukcinat
Peptid
B/W (1, 2) • FF (1, 2) • S • Y (1, 2, 4, 5) • Neuromedin (B, U (1, 2)) • Neurotenzin (1, 2)
Drugi
Anafilatoksin (C3a, C5a) • Angiotenzin (1, 2) • Apelin • Bombezin (BRS3, GRPR, NMBR) • Bradikinin (B1, B2) • Hemokin • Holecistokinin (A, B) • Endotelin (A, B) • Formil peptid (1, 2, 3) • FSH • Galanin (1, 2, 3) • GHB receptor • Gonadotropin-oslobađajući hormon (1, 2) • Grelin • Kispeptin • Luteinizirajući hormon/horiogonadotropin • MAS (1, 1L, D, E, F, G, X1, X2, X3, X4) • Melanokortin (1, 2, 3, 4, 5) • MCHR (1, 2) • Motilin • Opioidni (δ, κ, μ, Nociceptin & ζ, ali ne σ) • Oreksin (1, 2) • Oksitocin • Prokineticin (1, 2) • Prolaktin-oslobađajući peptid • Relaksin (1, 2, 3, 4) • Somatostatin (1, 2, 3, 4, 5) • Tahikinin (1, 2, 3) • Tirotropin • Tirotropin-oslobađajući hormon • Urotenzin-II • Vazopresin (1A, 1B, 2)
Razno
GPR (1, 3, 4, 6, 12, 15, 17, 18, 19, 20, 21, 22, 23, 25, 26, 27, 31, 32, 33, 34, 35, 37, 39, 42, 44, 45, 50, 52, 55, 61, 62, 63, 65, 68, 75, 77, 78, 81, 82, 83, 84, 85, 87, 88, 92, 101, 103, 109A, 109B, 119, 120, 132, 135, 137B, 139, 141, 142, 146, 148, 149, 150, 151, 152, 153, 160, 161, 162, 171, 173, 174, 176, 177, 182, 183)
Drugi
Adrenomedulin • Mirisni • Opsin (3, 4, 5, 1LW, 1MW, 1SW, RGR, RRH) • Proteazom-aktivirani (1, 2, 3, 4) • SREB (1, 2, 3)
Klasa B: Sekretinu slični
GPR (56, 64, 97, 98, 110, 111, 112, 113, 114, 115, 116, 123, 124, 125, 126, 128, 133, 143, 144, 155, 157)
Drugi
Klasa C: Metabotropni
glutamat / feromon
TAS1R (1, 2, 3) • TAS2R (1, 3, 4, 5, 8, 9, 10, 12, 13, 14, 16, 19, 20, 30, 31, 38, 39, 40, 41, 42, 43, 45, 46, 50)
Drugi
Klasa F:
Frizzled / Zaglađeni
Uvojiti
Frizzled (1, 2, 3, 4, 5, 6, 7, 8, 9, 10)
Zaglađeni
B trdu: peptidi (nrpl/grfl/cytl/horl), receptori (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd, signalni putevi (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)
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Neuropeptidni receptori
Hormonski receptori
Drugi
Opioidni receptori
Drugi neuropeptidni receptori
B trdu: peptidi (nrpl/grfl/cytl/horl), receptori (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd, signalni putevi (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)