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Purinergic receptor P2Y, G-protein coupled, 1
Symbols P2RY1; P2Y1
External IDs OMIM601167 MGI105049 HomoloGene1926 IUPHAR: P2Y1 GeneCards: P2RY1 Gene
RNA expression pattern
PBB GE P2RY1 207455 at tn.png
More reference expression data
Species Human Mouse
Entrez 5028 18441
Ensembl ENSG00000169860 ENSMUSG00000027765
UniProt P47900 Q544J5
RefSeq (mRNA) NM_002563 NM_008772
RefSeq (protein) NP_002554 NP_032798
Location (UCSC) Chr 3:
154.04 - 154.04 Mb
Chr 3:
61.09 - 61.1 Mb
PubMed search [1] [2]

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


  1. ^ 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): 783-8. doi:10.1006/bbrc.1996.0139. PMID 8579591.  
  2. ^ "Entrez Gene: P2RY1 purinergic receptor P2Y, G-protein coupled, 1".  

External links

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): 588–93. 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): 295–7. 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. 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): 419–24. 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): 2030–4. 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): 8496–501. 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. 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): 7617–22. doi:10.1073/pnas.121587098. 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): 33–6. 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. 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): 179–83. 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): 433–9. 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): 1400–8. 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): 16899–903. doi:10.1073/pnas.242603899. 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): 440–7. 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. 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): 1007–15. 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): 330–6. PMID 12871508.  

This article incorporates text from the United States National Library of Medicine, which is in the public domain.



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