Abstract
P2Y receptors are classified as P2 purinergic receptors that belong to the superfamily of G-protein coupled receptors. They are distinguishable from P1 (adenosine) receptors in that they bind adenine and/or uracil nucleotide triphosphates or diphosphates depending on the subtype. Over the past decade, P2Y receptors have been cloned from a variety of tissues and species. Eight functional subtypes have been characterized. Nucleotide binding produces activation of specific G-proteins that in turn regulate the function of membrane bound enzymes including phospholipase C and adenylyl cyclase. Certain P2Y receptor subtypes possess a PDZ domain located at the end of the C-terminal region of the receptor. PDZ domains have been established as sites for protein-protein interaction, thus providing a possible mechanism for receptor modulation of membrane protein function independent of G-protein activation. In this review we discuss recent findings that suggest that P2Y receptors can modulate the function of ion channels through multiple protein-protein interactions at the plasma membrane that do not directly involve G-protein activation.
Similar content being viewed by others
References
Abbracchio, M. P. and Burnstock, G. (1994) Purinoceptors: are there families of P2X and P2Y purinoceptors? Pharmacol. Ther. 64, 445–475.
Fredholm, B. B., Abbracchio, M. P., Burnstock, G., et al. (1994) Nomenclature and classification of purinoceptors. Pharmacol. Rev. 46, 143–156.
Boarder, M. R. and Hourani, S. M. (1998) The regulation of vascular function by P2 receptors: multiple sites and multiple receptors. Trends Pharmacol. Sci. 19, 99–107.
Boarder, M. R., Weisman, G. A., Turner, J. T., and Wilkinson, G. F. (1995) G protein-coupled P2 purinoceptors: from molecular biology to functional responses. Trends Pharmacol. Sci. 16, 133–139.
Dubyak, G. R. and el-Moatassim, C. (1993) Signal transduction via P2-purinergic receptors for extracellular ATP and other nucleotides. Am. J. Physiol. 265, C577-C606.
Ralevic, V. and Burnstock, G. (1998) Receptors for purines and pyrimidines. Pharmacol. Rev. 50, 413–492.
Nicholas, R. A. (2001) Identification of the P2Y(12) receptor: a novel member of the P2Y family of receptors activated by extracellular nucleotides. Mol. Pharmacol. 60, 416–420.
Chambers, J. K., Macdonald, L. E., Sarau, H. M., et al. (2000) A G protein-coupled receptor for UDP-glucose. J. Biol. Chem. 275, 10767–10771.
Sak, K. and Webb, T. E. (2002) A retrospective of recombinant P2Y receptor subtypes and their pharmacology. Arch. Biochem. Biophys. 397, 131–136.
von Kugelgen, I. and Wetter, A. (2000) Molecular pharmacology of P2Y-receptors. Naunyn Schmiedebergs Arch. Pharmacol. 362, 310–323.
Communi, D., Gonzalez, N. S., Detheux, M., et al. (2001) Identification of a novel human ADP receptor coupled to G(i). J. Biol. Chem. 276, 41479–41485.
Bogdanov, Y. D., Dale, L., King, B. F., Whittock, N., and Burnstock, G. (1997) Early expression of a novel nucleotide receptor in the neural plate of Xenopus embryos. J. Biol. Chem. 272, 12583–12590.
Webb, T. E., Henderson, D., King, B. F., et al. (1996) A novel G protein-coupled P2 purinoceptor (P2Y3) activated preferentially by nucleoside diphosphates. Mol. Pharmacol. 50, 258–265.
Herold, C. L., Li, Q., Schachter, J. B., Harden, T. K., and Nicholas, R. A. (1997) Lack of nucleotide-promoted second messenger signaling responses in 1321N1 cells expressing the proposed P2Y receptor, p2y7. Biochem. Biophys. Res. Commun. 235, 717–721.
Li, Q., Schachter, J. B., Harden, T. K., and Nicholas, R. A. (1997) The 6H1 orphan receptor, claimed to be the p2y5 receptor, does not mediate nucleotide-promoted second messenger responses. Biochem. Biophys. Res. Commun. 236, 455–460.
Janssens, R., Boeynaems, J. M., Godart, M., and Communi, D. (1997) Cloning of a human hepta-helical receptor closely related to the P2Y5 receptor. Biochem. Biophys. Res. Commun. 236, 106–112.
Jiang, Q., Guo, D., Lee, B. X., et al. (1997) A mutational analysis of residues essential for ligand recognition at the human P2Y1 receptor. Mol. Pharmacol. 52, 499–507.
Van Rhee, A. M., Fischer, B., Van Galen, P. J., and Jacobson, K. A. (1995) Modelling the P2Y purinoceptor using rhodopsin as template. Drug Des. Discov. 13, 133–154.
Moro, S., Guo, D., Camaioni, E., Boyer, J. L., Harden, T. K., and Jacobson, K. A. (1998) Human P2Y1 receptor: molecular modeling and site-directed mutagenesis as tools to identify agonist and antagonist recognition sites. J. Med. Chem. 41, 1456–1466.
Moro, S., Hoffmann, C., and Jacobson, K. A. (1999) Role of the extracellular loops of G protein-coupled receptors in ligand recognition: a molecular modeling study of the human P2Y1 receptor. Biochemistry 38, 3498–3507.
Hoffmann, C., Moro, S., Nicholas, R. A., Harden, T. K., and Jacobson, K. A. (1999) The role of amino acids in extracellular loops of the human P2Y1 receptor in surface expression and activation processes. J. Biol. Chem. 274, 14639–14647.
Abbracchio, M. P., Boeynaems, J. M., Barnard, E. A., et al. (2003) Characterization of the UDP-glucose receptor (re-named here the P2Y(14) receptor) adds diversity to the P2Y receptor family. Trends Pharmacol. Sci. 24, 52–55.
Schachter, J. B., Li, Q., Boyer, J. L., Nicholas, R. A., and Harden, T. K. (1996) Second messenger cascade specificity and pharmacological selectivity of the human P2Y1-purinoceptor. Br. J. Pharmacol. 118, 167–173.
Parr, C. E., Sullivan, D. M., Paradiso, A. M., et al. (1994) Cloning and expression of a human P2U nucleotide receptor, a target for cystic fibrosis pharmacotherapy. Proc. Natl. Acad. Sci. USA. 91, 13067.
Communi, D., Pirotton, S., Parmentier, M., and Boeynaems, J. M. (1995) Cloning and functional expression of a human uridine nucleotide receptor. J. Biol. Chem. 270, 30849–30852.
Lazarowski, E. R., Rochelle, L. G., O’Neal, W. K., et al. (2001) Cloning and functional characterization of two murine uridine nucleotide receptors reveal a potential target for correcting ion transport deficiency in cystic fibrosis gallbladder. J. Pharmacol. Exp. Ther. 297, 43–49.
Communi, D., Govaerts, C., Parmentier, M., and Boeynaems, J. M. (1997) Cloning of a human purinergic P2Y receptor coupled to phospholipase C and adenylyl cyclase. J. Biol. Chem. 272, 31969–31973.
van der Weyden, L., Adams, D. J., Luttrell, B. M., Conigrave, A. D., and Morris, M. B. (2000) Pharmacological characterisation of the P2Y11 receptor in stably transfected haematological cell lines. Mol. Cell. Biochem. 213, 75–81.
Hourani, S. M. and Hall, D. A. (1994) Receptors for ADP on human blood platelets. Trends Pharmacol. Sci. 15, 103–108.
Gachet, C., Hechler, B., Leon, C., et al. (1997) Activation of ADP receptors and platelet function. Thromb. Haemost. 78, 271–275.
Savi, P., Beauverger, P., Labouret, C., et al. (1998) Role of P2Y1 purinoceptor in ADP-induced platelet activation. FEBS Lett. 422, 291–295.
Hollopeter, G., Jantzen, H. M., Vincent, D., et al. (2001) Identification of the platelet ADP receptor targeted by antithrombotic drugs. Nature 409, 202–207.
Daniel, J. L., Dangelmaier, C., Jin, J., Ashby, B., Smith, J. B., and Kunapuli, S. P. (1998) Molecular basis for ADP-induced platelet activation. I. Evidence for three distinct ADP receptors on human platelets. J. Biol. Chem. 273, 2024–2029.
Hechler, B., Leon, C., Vial, C., et al. (1998) The P2Y1 receptor is necessary for adenosine 5′-diphosphate-induced platelet aggregation. Blood 92, 152–159.
Neary, J. T., Kang, Y., Bu, Y., Yu, E., Akong, K., and Peters, C. M. (1999) Mitogenic signaling by ATP/P2Y purinergic receptors in astrocytes: involvement of a calcium-independent protein kinase C, extracellular signal-regulated protein kinase pathway distinct from the phosphatidylinositol-specific phospholipase C/calcium pathway. J. Neurosci. 19, 4211–4220.
Lenz, G., Gottfried, C., Luo, Z., et al. (2000) P(2Y) purinoceptor subtypes recruit different MEK activators in astrocytes. Br. J. Pharmacol. 129, 927–936.
Patel, V., Brown, C., Goodwin, A., Wilkie, N., and Boarder, M. R. (1996) Phosphorylation and activation of p42 and p44 mitogen-activated protein kinase are required for the P2 purinoceptor stimulation of endothelial prostacyclin production. Biochem. J. 320(Pt 1), 221–226.
Albert, J. L., Boyle, J. P., Roberts, J. A., Challiss, R. A., Gubby, S. E., and Boarder, M. R. (1997) Regulation of brain capillary endothelial cells by P2Y receptors coupled to Ca2+, phospholipase C and mitogen-activated protein kinase. Br. J. Pharmacol. 122, 935–941.
Harper, S., Webb, T. E., Charlton, S. J., Ng, L. L., and Boarder, M. R. (1998) Evidence that P2Y4 nucleotide receptors are involved in the regulation of rat aortic smooth muscle cells by UTP and ATP. Br. J. Pharmacol. 124, 703–710.
Huwiler, A., and Pfeilschifter, J. (1994) Stimulation by extracellular ATP and UTP of the mitogen-activated protein kinase cascade and proliferation of rat renal mesangial cells. Br. J. Pharmacol. 113, 1455–1463.
Gao, Z., Chen, T., Weber, M. J., and Linden, J. (1999) A2B adenosine and P2Y2 receptors stimulate mitogen-activated protein kinase in human embryonic kidney-293 cells. Cross-talk between cyclic AMP and protein kinase c pathways. J. Biol. Chem. 274, 5972–5980.
Graham, A., McLees, A., Kennedy, C., Gould, G. W., and Plevin, R. (1996) Stimulation by the nucleotides, ATP and UTP of mitogen-activated protein kinase in EAhy 926 endothelial cells. Br. J. Pharmacol. 117, 1341–1347.
Soltoff, S. P., Avraham, H., Avraham, S., and Cantley, L. C. (1998) Activation of P2Y2 receptors by UTP and ATP stimulates mitogen-activated kinase activity through a pathway that involves related adhesion focal tyrosine kinase and protein kinase C. J. Biol. Chem. 273, 2653–2660.
Sellers, L. A., Simon, J., Lundahl, T. S., Cousens, D. J., Humphrey, P. P., and Barnard, E. A. (2001) Adenosine nucleotides acting at the human P2Y1 receptor stimulate mitogen-activated protein kinases and induce apoptosis. J. Biol. Chem. 276, 16379–16390.
Neary, J. T. and Zhu, Q. (1994) Signaling by ATP receptors in astrocytes. Neuroreport 5, 1617–1620.
Widmann, C., Gibson, S., Jarpe, M. B., and Johnson, G. L. (1999) Mitogen-activated protein kinase: conservation of a three-kinase module from yeast to human. Physiol. Rev. 79, 143–180.
Seger, R. and Krebs, E. G. (1995) The MAPK signaling cascade. FASEB J. 9, 726–735.
Neary, J. T. (2000) Trophic actions of extracellular ATP: gene expression profiling by DNA array analysis. J. Auton. Nerv. Syst. 81, 200–204.
Brambilla, R., Neary, J. T., Cattabeni, F., et al. (2002) Induction of COX-2 and reactive gliosis by P2Y receptors in rat cortical astrocytes is dependent on ERK1/2 but independent of calcium signalling. J. Neurochem. 83, 1285–1296.
Brambilla, R., Cottini, L., Cattabeni, F., et al. (2001) ATP induces gliosis by activating a novel P2Y receptor coupled to COX-2 upregulation via a calcium-independent RAS/ERK1/2 Pathway. Soc. Neurosci. 38, 5(Abstract).
Santiago-Perez, L. I., Flores R. V., Santos-Berrios C., et al. (2001) P2Y(2) nucleotide receptor signaling in human monocytic cells: activation, desensitization and coupling to mitogen-activated protein kinases. J. Cell. Physiol. 187, 196–208.
Pillois, X., Chaulet, H., Belloc, I., Dupuch, F., Desgranges, C., and Gadeau, A. P. (2002) Nucleotide receptors involved in UTP-induced rat arterial smooth muscle cell migration. Circ. Res. 90, 678–681.
Chaulet, H., Desgranges, C., Renault, M. A., et al. (2001) Extracellular nucleotides induce arterial smooth muscle cell migration via osteopontin. Circ. Res. 89, 772–778.
Sauzeau, V., Le Jeune, H., Cario-Toumaniantz, C., et al. (2000) P2Y(1), P2Y(2), P2Y(4), and P2Y(6) receptors are coupled to Rho and Rho kinase activation in vascular myocytes. Am. J. Physiol. Heart Circ. Physiol. 278, H1751-H1761.
Ikeuchi, Y. and Nishizaki, T. (1996) P2 purinoceptor-operated potassium channel in rat cerebellar neurons. Biochem. Biophys. Res. Commun. 218, 67–71.
Ikeuchi, Y., Nishizaki, T., Mori, M., and Okada, Y. (1996) Regulation of the potassium current and cytosolic Ca2+ release induced by 2-methylthio ATP in hippocampal neurons. Biochem. Biophys. Res. Commun. 218, 428–433.
Ikeuchi, Y. and Nishizaki, T. (1995) ATP-evoked potassium currents in rat striatal neurons are mediated by a P2 purinergic receptor. Neurosci. Lett. 190, 89–92.
Nakamura, F. and Strittmatter, S. M. (1996) P2Y1 purinergic receptors in sensory neurons: contribution to touch- induced impulse generation. Proc. Natl. Acad. Sci. USA. 93, 10465–10470.
Nakazawa, K., Inoue, K., and Inoue, K. (1994) ATP reduces voltage-activated K+ current in cultured rat hippocampal neurons. Pflugers Arch. 429, 143–145.
Boehm, S. (1998) Selective inhibition of M-type potassium channels in rat sympathetic neurons by uridine nucleotide preferring receptors. Br. J. Pharmacol. 124, 1261–1269.
Xu, L. and Enyeart, J. J. (1999) Purine and pyrimidine nucleotides inhibit a noninactivating K+ current and depolarize adrenal cortical cells through a G protein-coupled receptor. Mol. Pharmacol. 55, 364–376.
Wilson, S. M. and Pappone, P. A. (1999) P2 receptor modulation of voltage-gated potassium currents in brown adipocytes. J. Gen. Physiol. 113, 125–138.
Parker, K. E. and Scarpa, A. (1995) An ATP-activated nonselective cation channel in guinea pig ventricular myocytes. Am. J. Physiol. 269, H789-H797.
Filippov, A. K., Webb, T. E., Barnard, E. A., and Brown, D. A. (1997) Inhibition by heterologously-expressed P2Y2 nucleotide receptors of N-type calcium currents in rat sympathetic neurones. Br. J. Pharmacol. 121, 849–851.
Filippov, A. K., Webb, T. E., Barnard, E. A., and Brown, D. A. (1998) P2Y2 nucleotide receptors expressed heterologously in sympathetic neurons inhibit both N-type Ca2+ and M-type K+ currents. J. Neurosci. 18, 5170–5179.
Qu, Y., Campbell, D. L., and Strauss, H. C. (1993) Modulation of L-type Ca2+ current by extracellular ATP in ferret isolated right ventricular myocytes. J. Physiol. 471, 295–317.
Filippov, A. K., Brown, D. A., and Barnard, E. A. (2000) The P2Y(1) receptor closes the N-type Ca(2+) channel in neurones, with both adenosine triphosphates and diphosphates as potent agonists. Br. J. Pharmacol. 129, 1063–1066.
Fleischhauer, J. C., Mitchell, C. H., Peterson-Yantorno, K., Coca-Prados, M., and Civan, M. M. (2001) PGE(2), Ca(2+), and cAMP mediate ATP activation of Cl(−) channels in pigmented ciliary epithelial cells. Am. J. Physiol. Cell. Physiol. 281, C1614-C1623.
Wu, D. and Mori, N. (1999) Extracellular ATP-induced inward current in isolated epithelial cells of the endolymphatic sac. Biochim. Biophys. Acta. 1419, 33–42.
Banderali, U., Brochiero, E., Lindenthal, S., Raschi, C., Bogliolo, S., and Ehrenfeld, J. (1999) Control of apical membrane chloride permeability in the renal A6 cell line by nucleotides. J. Physiol. 519(Pt 3), 737–751.
Land, S. C. and Collett, A. (2001) Detection of Cl- flux in the apical microenvironment of cultured foetal distal lung epithelial cells. J. Exp. Biol. 204, 785–795.
Devor, D. C. and Pilewski, J. M. (1999) UTP inhibits Na+ absorption in wild-type and DeltaF508 CFTR-expressing human bronchial epithelia. Am. J. Physiol. 276, C827-C837.
Mall, M., Wissner, A., Gonska, T., et al. (2000) Inhibition of amiloride-sensitive epithelial Na(+) absorption by extracellular nucleotides in human normal and cystic fibrosis airways. Am. J. Respir. Cell Mol. Biol. 23, 755–761.
Jetten, A. M., Yankaskas, J. R., Stutts, M. J., Willumsen, N. J., and Boucher, R. C. (1989) Persistence of abnormal chloride conductance regulation in transformed cystic fibrosis epithelia. Science 244, 1472–1475.
Mason, S. J., Paradiso, A. M., and Boucher, R. C. (1991) Regulation of transepithelial ion transport and intracellular calcium by extracellular ATP in human normal and cystic fibrosis airway epithelium. Br. J. Pharmacol. 103, 1649–1656.
Sheng, M. (1996) PDZs and receptor/channel clustering: rounding up the latest suspects. Neuron 17, 575–578.
Saras, J. and Heldin, C. H. (1996) PDZ domains bind carboxy-terminal sequences of target proteins. Trends Biochem. Sci. 21, 455–458.
Kornau, H. C., Seeburg, P. H., and Kennedy, M. B. (1997) Interaction of ion channels and receptors with PDZ domain proteins. Curr. Opin. Neurobiol. 7, 368–373.
Hall, R. A., Ostedgaard, L. S., Premont, R. T., 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. USA. 95, 8496–8501.
Hall R. A., Premont R. T., Chow C. W., et al. (1998) The beta2-adrenergic receptor interacts with the Na+/H+-exchanger regulatory factor to control Na+/H+ exchange. Nature 392, 626–630.
Bagorda, A., Guerra, L., Di Sole, F., et al. (2002) Reciprocal protein kinase A regulatory interactions between cystic fibrosis transmembrane conductance regulator and Na+/H+ exchanger isoform 3 in a renal polarized epithelial cell model. J. Biol. Chem. 277, 21480–21488.
Reczek, D., Berryman, M., and Bretscher, A. (1997) Identification of EBP50: a PDZ-containing phosphoprotein that associates with members of the ezrin-radixin-moesin family. J. Cell Biol. 139, 169–179.
Lamprecht, G., Weinman, E. J., and Yun, C. H. (1998) The role of NHERF and E3KARP in the cAMP-mediated inhibition of NHE3. J. Biol. Chem. 273, 29972–29978.
Bretscher, A., Chambers, D., Nguyen, R., and Reczek, D. (2000) ERM-Merlin and EBP50 protein families in plasma membrane organization and function. Annu. Rev. Cell Dev. Biol. 16, 113–143.
Sun, F., Hug, M. J., Lewarchik, C. M., Yun, C. H., Bradbury, N. A., and Frizzell, R. A. (2000) E3KARP mediates the association of ezrin and protein kinase A with the cystic fibrosis transmembrane conductance regulator in airway cells. J. Biol. Chem. 275, 29539–29546.
Short, D. B., Trotter, K. W., Reczek, D., et al. (1998) An apical PDZ protein anchors the cystic fibrosis transmembrane conductance regulator to the cytoskeleton. J. Biol. Chem. 273, 19797–19801.
Wei, L., Vankeerberghen, A., Cuppens, H., Cassiman, J. J., Droogmans, G., and Nilius, B. (2001) The C-terminal part of the R-domain, but not the PDZ binding motif, of CFTR is involved in interaction with Ca(2+)-activated Cl- channels. Pflugers Arch. 442, 280–285.
Boucher, R. C., Stutts, M. J., Knowles, M. R., Cantley, L., and Gatzy, J. T. (1986) Na+ transport in cystic fibrosis respiratory epithelia. Abnormal basal rate and response to adenylate cyclase activation. J. Clin. Invest. 78, 1245–1252.
Mall, M., Bleich, M., Kuehr, J., Brandis, M., Greger, R., and Kunzelmann, K. (1999) CFTR-mediated inhibition of epithelial Na+ conductance in human colon is defective in cystic fibrosis. Am. J. Physiol. 277, G709-G716.
Boucherot, A., Schreiber, R., and Kunzelmann, K. (2001) Role of CFTR’s PDZ1-binding domain, NBF1 and Cl(−) conductance in inhibition of epithelial Na(+) channels in Xenopus oocytes. Biochim. Biophys. Acta. 1515, 64–71.
O’Grady, S. M., Elmquist, E., Filtz, T. M., Nicholas, R. A., and Harden, T. K. (1996) A guanine nucleotide-independent inwardly rectifying cation permeability is associated with P2Y1 receptor expression in Xenopus oocytes. J. Biol. Chem. 271, 29080–29087.
Lee, S. Y., Nicholas, R. A., and O’Grady, S. M. (2002) P2Y(2) and P2Y(6) receptors expression in Xenopus oocytes modulates activation and inactivation gating of an endogenous ion channel. FASEB J 16(4), A191-A191 (Abstract).
Lee, S. Y., Wolff, S. C., Nicholas, R. A., and O’Grady, S. M. (2003) P2Y receptors modulate ion channel function through interactions involving their C-terminal domain. Mol. Pharmacol. 63, 878–885.
Parker, I., Gundersen, C. B., and Miledi, R. (1985) A transient inward current elicited by hyperpolarization during serotonin activation in Xenopus oocytes. Proc. R. Soc. Lond. B Biol. Sci. 223, 279–292.
Ni, Y. G., Panicker, M. M., and Miledi, R. (1997) Efficient coupling of 5-HT1a receptors to the phospholipase C pathway in Xenopus oocytes. Brain Res. Mol. Brain Res. 51, 115–122.
Guttridge, K. L., Smith, L. D., and Miledi, R. (1995) Xenopus Gq alpha subunit activates the phosphatidylinositol pathway in Xenopus oocytes but does not consistently induce oocyte maturation. Proc. Natl. Acad. Sci. USA. 92, 1297–1301.
Lee, S. Y. and O’Grady, S. M. (2001) Ion channel function associated with human P2Y(11) receptor expression in Xenopus oocytes. FASEB J. 15(5), A928-A928. (Abstract)
Giblin, J. P., Quinn, K., and Tinker, A. (2002) The cytoplasmic C-terminus of the sulfonylurea receptor is important for KATP channel function but is not key for complex assembly or trafficking. Eur. J. Biochem. 269, 5303–5313.
Schwanstecher, M., Loser, S., Chudziak, F., and Panten, U. (1994) Identification of a 38-kDa high affinity sulfonylurea-binding peptide in insulin-secreting cells and cerebral cortex. J. Biol. Chem. 269, 17768–17771.
Clement, J. P. 4th, Kunjilwar, K., Gonzalez, G., et al. (1997) Association and stoichiometry of K(ATP) channel subunits. Neuron 18, 827–838.
Reimann, F., Tucker, S. J., Proks, P., and Ashcroft, F. M. (1999) Involvement of the N-terminus of Kir6.2 in coupling to the sulphonylurea receptor. J. Physiol. 518 (Pt 2), 325–336.
Seino, S. (1999) ATP-sensitive potassium channels: a model of heteromultimeric potassium channel/receptor assemblies. Annu. Rev. Physiol. 61, 337–362.
Blum, R., Kafitz, K. W., and Konnerth, A. (2002) Neurotrophin-evoked depolarization requires the sodium channel Na(V)1.9. Nature 419, 687–693.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Lee, S.Y., O’Grady, S.M. Modulation of ion channel function by P2Y receptors. Cell Biochem Biophys 39, 75–88 (2003). https://doi.org/10.1385/CBB:39:1:75
Issue Date:
DOI: https://doi.org/10.1385/CBB:39:1:75