P2Y receptors (nomenclature as agreed by the NC-IUPHAR Subcommittee on P2Y Receptors [1-2,41]) are activated by the endogenous ligands ATP, ADP, uridine triphosphate, uridine diphosphate and UDP-glucose. The relationship of many of the cloned receptors to endogenously expressed receptors is not yet established and so it might be appropriate to use wording such as 'uridine triphosphate-preferring (or ATP-, etc.) P2Y receptor' or 'P2Y₁-like', etc., until further, as yet undefined, corroborative criteria can be applied [12,26,39,70,73]. Clinically used drugs acting on these receptors include the dinucleoside polyphosphate diquafosol, agonist of the P2Y₂ receptor subtype, approved in Japan for the management of dry eye disease [53], and the P2Y₁₂ receptor antagonists prasugrel, ticagrelor and cangrelor, all approved as antiplatelet drugs [14,65].

A series of 4-alkyloxyimino derivatives of uridine-5'-triphosphate which could be useful for derivatization as fluorescent P2Y_2/4/6 receptor probes has been recently synthesized [45].

Single nucleotide polymorphisms of the P2YR₁ gene have been associated to different platelet reactivity to ADP ADP [32]. Three frequent nonsynonymous P2Y₂ receptor polymorphisms have been identified, one of which was significantly more common in cystic fibrosis patients. This polymorphism is linked to increases in Ca²⁺ influx in transfected cells, and might therefore play a role in disease development [13]. Although uridine triphosphate (UTP) was also shown to be a biased agonist at P2Y₁₁, this is still under debate [61,74]. A group of single nucleotide polymorphisms in the P2Y₁₂ gene, forming the so called P2Y₁₂ H2 haplotype, has been associated with increased platelet responsiveness to ADP, increased risk of peripheral arterial disease and with coronary artery disease [18]. The platelet-type bleeding disorder due to P2Y₁₂ receptor defects is an autosomal recessive condition characterized by mild to moderate mucocutaneous bleeding and excessive bleeding after surgery or trauma. The defect is due to the inability of ADP to induce platelet aggregation [17]. The P2Y₁₃ receptor Met-158-Thr polymorphism, which is in linkage disequilibrium with the P2Y₁₂ locus, is not associated with acute myocardial infarction, diabetes mellitus or related risk factors [3]. The P2Y₁₄ receptor was previously considered to exclusively bind sugar nucleotides such as UDP-glucose and UDP-galactose [19]. However, more recent evidence with several cell lines has demonstrated that uridine diphosphate (UDP) is 5-fold more potent than UDP-glucose [15]. UDP was also shown to competitively antagonise the UDP-glucose response at the human recombinant P2Y₁₄ receptor [27].

* Key recommended reading is highlighted with an asterisk

* Abbracchio MP, Burnstock G, Boeynaems JM, Barnard EA, Boyer JL, Kennedy C, Knight GE, Fumagalli M, Gachet C, Jacobson KA et al.. (2006) International Union of Pharmacology LVIII: update on the P2Y G protein-coupled nucleotide receptors: from molecular mechanisms and pathophysiology to therapy. Pharmacol Rev, 58 (3): 281-341. [PMID:16968944]

Burnstock G. (2007) Purine and pyrimidine receptors. Cell Mol Life Sci, 64 (12): 1471-83. [PMID:17375261]

Burnstock G, Verkhratsky A. (2012) Purinergic signalling and the nervous system. In  (Springer) 1-715.

Erlinge D. (2011) P2Y receptors in health and disease. Adv Pharmacol, 61: 417-39. [PMID:21586366]

Jacobson KA. (2013) Structure-based approaches to ligands for G-protein-coupled adenosine and P2Y receptors, from small molecules to nanoconjugates. J Med Chem, 56 (10): 3749-67. [PMID:23597047]

* Jacobson KA, Delicado EG, Gachet C, Kennedy C, von Kügelgen I, Li B, Miras-Portugal MT, Novak I, Schöneberg T, Perez-Sen R et al.. (2020) Update of P2Y receptor pharmacology: IUPHAR Review 27. Br J Pharmacol, 177 (11): 2413-2433. [PMID:32037507]

Jacobson KA, Ivanov AA, de Castro S, Harden TK, Ko H. (2009) Development of selective agonists and antagonists of P2Y receptors. Purinergic Signal, 5 (1): 75-89. [PMID:18600475]

* Jacobson KA, Paoletta S, Katritch V, Wu B, Gao ZG, Zhao Q, Stevens RC, Kiselev E. (2015) Nucleotides Acting at P2Y Receptors: Connecting Structure and Function. Mol Pharmacol, 88 (2): 220-30. [PMID:25837834]

von Kügelgen I, Harden TK. (2011) Molecular pharmacology, physiology, and structure of the P2Y receptors. Adv Pharmacol, 61: 373-415. [PMID:21586365]

* von Kügelgen I, Hoffmann K. (2016) Pharmacology and structure of P2Y receptors. Neuropharmacology, 104: 50-61. [PMID:26519900]

Weisman GA, Woods LT, Erb L, Seye CI. (2012) P2Y receptors in the mammalian nervous system: pharmacology, ligands and therapeutic potential. CNS Neurol Disord Drug Targets, 11 (6): 722-38. [PMID:22963441]

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Subcommittee members: Maria-Pia Abbracchio (Chairperson) Institute of Pharmacological Sciences Via Balzaretti 9 Milan 20133 Italy Kenneth A. Jacobson (Co-chairperson) Molecular Recognition Section National Institutes of Health Building 8A, Room BIA-17 Bethesda, MD, 20892, USA Geoffrey Burnstock (Past chairperson) (1929-2020) Formerly President of the Autonomic Neuroscience Centre of the UCL Medical School Jean-Marie Boeynaems Institute of Interdisciplinary Research School of Medicine and Department of Medical Chemistry Erasme Hospital Université Libre de Bruxelles 808 Route de Lennik Brussels B-1070 Belgium Stefania Ceruti Laboratory of Molecular and Cellular Pharmacology of Purinergic Transmission Department of Pharmacological Sciences University of Milan Via Balzaretti 9 Milan 20133 Italy Marta Fumagalli Laboratory of Molecular and Cellular Pharmacology of Purinergic Transmission Department of Pharmacological Sciences University of Milan via Balzaretti, 9 MILAN 20133 Italy Christian Gachet INSERM U311 ETS Strasbourg 10 rue Spielmann Strasbourg 67065 France Charles Kennedy Strathclyde Institute of Pharmacy and Biomedical Sciences University of Strathclyde 161 Cathedral Street Glasgow, G4 0RE UK Brian F. King Department of Neuroscience, Physiology & Pharmacology 74 Huntley Street University College London, London WC1E 6BT United Kingdom Davide Lecca Laboratory of Molecular and Cellular Pharmacology of Purinergic Transmission Department of Pharmacological Sciences University of Milan Via Balzaretti 9, 20133 Milan 20133 Italy Christa E. Müller Pharmazeutisches Institut Pharmazeutische Chemie I An der Immenburg 4 D-53121 Bonn, Germany Gary A. Weisman Department of Biochemistry University of Missouri M121 Medical Sciences Building Columbia MO 65212 USA

Other contributors: José L. Boyer Department of Pharmacology 1021 Mary Ellen Jones Building University of North Carolina Chapel Hill NC 27599 USA Rebecca Hills (Past curator) Robert G. Humphries Astra Charnwood Bakewell Road Loughborough LE11 0RH UK Kazu Inoue Department of Molecular and System Pharmacology Graduate School of Pharmaceutical Sciences University of Kyushu Fukuoka Japan Maria Teresa Miras-Portugal Departamento de Bioquimica Facultad de Veterinaria Universidad Complutense de Madrid Madrid 28040 Spain Vera Ralevic The University of Nottingham Medical School Queen's Medical Centre Nottingham NG7 2UH UK