P2RY1
From Wikipedia, the free encyclopedia
P2Y purinoceptor 1 is a protein that in humans is encoded by the P2RY1 gene.[1]
The product of this gene, P2Y1 belongs to the family of G-protein coupled receptors. This family has several receptor subtypes with different pharmacological selectivity, which overlaps in some cases, for various adenosine and uridine nucleotides. This receptor functions as a receptor for extracellular ATP and ADP. In platelets binding to ADP leads to mobilization of intracellular calcium ions via activation of phospholipase C, a change in platelet shape, and probably to platelet aggregation.[2]
See also
References
- ↑ Ayyanathan K, Webbs TE, Sandhu AK, Athwal RS, Barnard EA, Kunapuli SP (Mar 1996). "Cloning and chromosomal localization of the human P2Y1 purinoceptor". Biochem Biophys Res Commun 218 (3): 783–788. doi:10.1006/bbrc.1996.0139. PMID 8579591.
- ↑ "Entrez Gene: P2RY1 purinergic receptor P2Y, G-protein coupled, 1".
External links
- "P2Y Receptors: P2Y1". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology.
Further reading
- Janssens R, Communi D, Pirotton S et al. (1996). "Cloning and tissue distribution of the human P2Y1 receptor". Biochem. Biophys. Res. Commun. 221 (3): 588–593. doi:10.1006/bbrc.1996.0640. PMID 8630005.
- Léon C, Vial C, Cazenave JP, Gachet C (1996). "Cloning and sequencing of a human cDNA encoding endothelial P2Y1 purinoceptor". Gene 171 (2): 295–297. doi:10.1016/0378-1119(96)00027-3. PMID 8666290.
- Léon C, Hechler B, Vial C et al. (1997). "The P2Y1 receptor is an ADP receptor antagonized by ATP and expressed in platelets and megakaryoblastic cells". FEBS Lett. 403 (1): 26–30. doi:10.1016/S0014-5793(97)00022-7. PMID 9038354.
- Ayyanathan K, Naylor SL, Kunapuli SP (1997). "Structural characterization and fine chromosomal mapping of the human P2Y1 purinergic receptor gene (P2RY1)". Somat. Cell Mol. Genet. 22 (5): 419–424. doi:10.1007/BF02369897. PMID 9039850.
- Maier R, Glatz A, Mosbacher J, Bilbe G (1997). "Cloning of P2Y6 cDNAs and identification of a pseudogene: comparison of P2Y receptor subtype expression in bone and brain tissues". Biochem. Biophys. Res. Commun. 237 (2): 297–302. doi:10.1006/bbrc.1997.7135. PMID 9268704.
- Jin J, Daniel JL, Kunapuli SP (1998). "Molecular basis for ADP-induced platelet activation. II. The P2Y1 receptor mediates ADP-induced intracellular calcium mobilization and shape change in platelets". J. Biol. Chem. 273 (4): 2030–2034. doi:10.1074/jbc.273.4.2030. PMID 9442040.
- Hall RA, Ostedgaard LS, Premont RT et al. (1998). "A C-terminal motif found in the beta2-adrenergic receptor, P2Y1 receptor and cystic fibrosis transmembrane conductance regulator determines binding to the Na+/H+ exchanger regulatory factor family of PDZ proteins". Proc. Natl. Acad. Sci. U.S.A. 95 (15): 8496–8501. doi:10.1073/pnas.95.15.8496. PMC 21104. PMID 9671706.
- Sabala P, Czajkowski R, Przybyłek K et al. (2001). "Two subtypes of G protein-coupled nucleotide receptors, P2Y(1) and P2Y(2) are involved in calcium signalling in glioma C6 cells". Br. J. Pharmacol. 132 (2): 393–402. doi:10.1038/sj.bjp.0703843. PMC 1572584. PMID 11159687.
- Yoshioka K, Saitoh O, Nakata H (2001). "Heteromeric association creates a P2Y-like adenosine receptor". Proc. Natl. Acad. Sci. U.S.A. 98 (13): 7617–7622. doi:10.1073/pnas.121587098. PMC 34717. PMID 11390975.
- James G, Butt AM (2001). "Changes in P2Y and P2X purinoceptors in reactive glia following axonal degeneration in the rat optic nerve". Neurosci. Lett. 312 (1): 33–36. doi:10.1016/S0304-3940(01)02189-9. PMID 11578839.
- Moore DJ, Chambers JK, Wahlin JP et al. (2001). "Expression pattern of human P2Y receptor subtypes: a quantitative reverse transcription-polymerase chain reaction study". Biochim. Biophys. Acta 1521 (1–3): 107–19. doi:10.1016/S0167-4781(01)00291-3. PMID 11690642.
- Czajkowski R, Lei L, Sabała P, Barańska J (2002). "ADP-evoked phospholipase C stimulation and adenylyl cyclase inhibition in glioma C6 cells occur through two distinct nucleotide receptors, P2Y(1) and P2Y(12)". FEBS Lett. 513 (2–3): 179–183. doi:10.1016/S0014-5793(02)02255-X. PMID 11904146.
- Aktas B, Hönig-Liedl P, Walter U, Geiger J (2002). "Inhibition of platelet P2Y12 and alpha2A receptor signaling by cGMP-dependent protein kinase". Biochem. Pharmacol. 64 (3): 433–439. doi:10.1016/S0006-2952(02)01113-9. PMID 12147294.
- Nurden P, Poujol C, Winckler J et al. (2003). "Immunolocalization of P2Y1 and TPalpha receptors in platelets showed a major pool associated with the membranes of alpha -granules and the open canalicular system". Blood 101 (4): 1400–1408. doi:10.1182/blood-2002-02-0642. PMID 12393588.
- Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Burrell HE, Bowler WB, Gallagher JA, Sharpe GR (2003). "Human keratinocytes express multiple P2Y-receptors: evidence for functional P2Y1, P2Y2, and P2Y4 receptors". J. Invest. Dermatol. 120 (3): 440–447. doi:10.1046/j.1523-1747.2003.12050.x. PMID 12603858.
- Jagroop IA, Burnstock G, Mikhailidis DP (2003). "Both the ADP receptors P2Y1 and P2Y12, play a role in controlling shape change in human platelets". Platelets 14 (1): 15–20. doi:10.1080/0953710021000062914. PMID 12623443.
- Greig AV, Linge C, Terenghi G et al. (2003). "Purinergic receptors are part of a functional signaling system for proliferation and differentiation of human epidermal keratinocytes". J. Invest. Dermatol. 120 (6): 1007–1015. doi:10.1046/j.1523-1747.2003.12261.x. PMID 12787128.
- Wang L, Ostberg O, Wihlborg AK et al. (2003). "Quantification of ADP and ATP receptor expression in human platelets". J. Thromb. Haemost. 1 (2): 330–336. doi:10.1046/j.1538-7836.2003.00070.x. PMID 12871508.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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