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Gene Review

P2RX1  -  purinergic receptor P2X, ligand gated ion...

Homo sapiens

Synonyms: ATP receptor, P2X purinoceptor 1, P2X1, Purinergic receptor
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Disease relevance of P2RX1

  • Lack of evidence for functional ADP-activated human P2X1 receptors supports a role for ATP during hemostasis and thrombosis [1].
  • Feed forward cycle of hypotonic stress-induced ATP release, purinergic receptor activation, and growth stimulation of prostate cancer cells [2].
  • 1321N1 human astrocytoma cells expressing the cloned P2X1 cDNA exhibited both ATP- and ADP-stimulated Ca2+ influx that could be blocked by the purinoceptor antagonist pyridoxalphosphate-6-azophenyl-2',4'-disulfonic acid and suramin [3].
  • In the human breast cancer cell line MCF-7, the nucleotides ATP gamma S and UTP, acting extracellularly through the purinergic receptor P2Y(2), lead to elevated intracellular calcium levels and increased proliferation [4].
  • It may be clinically important for pharmacological intervention in gliomas to associate purinergic receptor antagonists and signal transduction pathways blockers [5].

High impact information on P2RX1


Chemical compound and disease context of P2RX1


Biological context of P2RX1


Anatomical context of P2RX1

  • We have mutated individual conserved glycine residues and determined their effect on the ATP sensitivity and time-course of P2X1 receptors expressed in Xenopus oocytes [13].
  • Human, rat, and mouse testicular smooth muscle demonstrated purinergic responsiveness, probably mediated through the P2X1 and/or P2X2 receptors [17].
  • Via transmission electron microscopy, we found that P2X1 mediates fast, reversible platelet shape change, secretory granule centralization, and pseudopodia formation [15].
  • CONCLUSION(S): This study demonstrated that ATP is a co-transmitter with noradrenaline in the contraction of the human vas deferens predominantly acting through the P2X1 receptor [18].
  • Treatment of platelet membranes with endoglycosidase-F causes the P2X1 receptor band to migrate as a 46-kD protein, verifying the highly glycosylated nature of the mature receptor protein [16].

Associations of P2RX1 with chemical compounds

  • Correspondingly, the P2X1-induced platelet shape change was inhibited by W-7 and by the MLC kinase inhibitor ML-7 but not by HA-1077 [15].
  • The P2X1 receptor, an adenosine triphosphate-gated cation channel, is expressed in human platelets but not in human blood leukocytes [16].
  • Structure-activity relationships of pyridoxal phosphate derivatives as potent and selective antagonists of P2X1 receptors [19].
  • Adenosine appears to act through P1 purinoceptors, although the subtype involved remains controversial, whereas ATP may involve both P2X1 and P2X7 purinoceptors [20].
  • 4. Affinity estimates of 15 other nucleotide analogues for the [35S]-ATP gamma S binding sites on the two recombinant P2X purinoceptor subtypes were surprisingly similar (less than 5 fold difference), the only exception being 2'-deoxy ATP which possessed 8 fold higher affinity for rat P2X2 than for human P2X1 purinoceptors [21].

Regulatory relationships of P2RX1

  • Further, the EC50 for alpha,beta-me-ATP was greater in cells expressing both P2X1 and P2X5 than in cells expressing P2X1 alone (5 and 1.6 microM, respectively) [22].

Other interactions of P2RX1

  • Each of the seven identified subunit proteins (P2X1 through P2X7) has been reported to form functional homo-oligomeric channels when expressed in heterologous systems [23].
  • We failed to clone P2X1 and P2X6 genes [24].
  • In bladder from symptomatic patients, the P2X1/calponin ratio was greater than that in controls (P = 0.016) [25].
  • In cells expressing the homomeric P2X1 receptor, 30 microM alpha,beta-methylene ATP (alpha,beta-me-ATP) evoked robust currents that completely desensitized in less than 1 sec, whereas alpha,beta-me-ATP failed to evoke current in cells expressing the homomeric P2X5 receptor [22].
  • In conclusion, P2X1, P2Y2, and P2Y6 are the most expressed P2 receptors in SMC and are thus probably mediating the contractile and mitogenic actions of extracellular nucleotides [26].

Analytical, diagnostic and therapeutic context of P2RX1


  1. Lack of evidence for functional ADP-activated human P2X1 receptors supports a role for ATP during hemostasis and thrombosis. Vial, C., Pitt, S.J., Roberts, J., Rolf, M.G., Mahaut-Smith, M.P., Evans, R.J. Blood (2003) [Pubmed]
  2. Feed forward cycle of hypotonic stress-induced ATP release, purinergic receptor activation, and growth stimulation of prostate cancer cells. Nandigama, R., Padmasekar, M., Wartenberg, M., Sauer, H. J. Biol. Chem. (2006) [Pubmed]
  3. P2X1 purinoceptor in human platelets. Molecular cloning and functional characterization after heterologous expression. Sun, B., Li, J., Okahara, K., Kambayashi, J. J. Biol. Chem. (1998) [Pubmed]
  4. Extracellular ATP activates multiple signalling pathways and potentiates growth factor-induced c-fos gene expression in MCF-7 breast cancer cells. Wagstaff, S.C., Bowler, W.B., Gallagher, J.A., Hipskind, R.A. Carcinogenesis (2000) [Pubmed]
  5. ERK, PKC and PI3K/Akt pathways mediate extracellular ATP and adenosine-induced proliferation of U138-MG human glioma cell line. Jacques-Silva, M.C., Bernardi, A., Rodnight, R., Lenz, G. Oncology (2004) [Pubmed]
  6. Molecular physiology of P2X receptors. North, R.A. Physiol. Rev. (2002) [Pubmed]
  7. Reduced vas deferens contraction and male infertility in mice lacking P2X1 receptors. Mulryan, K., Gitterman, D.P., Lewis, C.J., Vial, C., Leckie, B.J., Cobb, A.L., Brown, J.E., Conley, E.C., Buell, G., Pritchard, C.A., Evans, R.J. Nature (2000) [Pubmed]
  8. A G protein mutant that inhibits thrombin and purinergic receptor activation of phospholipase A2. Gupta, S.K., Diez, E., Heasley, L.E., Osawa, S., Johnson, G.L. Science (1990) [Pubmed]
  9. ATP receptor regulation of adenylate cyclase and protein kinase C activity in cultured renal LLC-PK1 cells. Anderson, R.J., Breckon, R., Dixon, B.S. J. Clin. Invest. (1991) [Pubmed]
  10. Calcium-dependent regulation of secretion in biliary epithelial cells: the role of apamin-sensitive SK channels. Feranchak, A.P., Doctor, R.B., Troetsch, M., Brookman, K., Johnson, S.M., Fitz, J.G. Gastroenterology (2004) [Pubmed]
  11. Markers for the development of early prostate cancer. Slater, M.D., Lauer, C., Gidley-Baird, A., Barden, J.A. J. Pathol. (2003) [Pubmed]
  12. P2X1 stimulation promotes thrombin receptor-mediated platelet aggregation. Erhardt, J.A., Toomey, J.R., Douglas, S.A., Johns, D.G. J. Thromb. Haemost. (2006) [Pubmed]
  13. Contribution of conserved glycine residues to ATP action at human P2X1 receptors: mutagenesis indicates that the glycine at position 250 is important for channel function. Digby, H.R., Roberts, J.A., Sutcliffe, M.J., Evans, R.J. J. Neurochem. (2005) [Pubmed]
  14. Overexpression of the platelet P2X1 ion channel in transgenic mice generates a novel prothrombotic phenotype. Oury, C., Kuijpers, M.J., Toth-Zsamboki, E., Bonnefoy, A., Danloy, S., Vreys, I., Feijge, M.A., De Vos, R., Vermylen, J., Heemskerk, J.W., Hoylaerts, M.F. Blood (2003) [Pubmed]
  15. P2X1-mediated ERK2 activation amplifies the collagen-induced platelet secretion by enhancing myosin light chain kinase activation. Toth-Zsamboki, E., Oury, C., Cornelissen, H., De Vos, R., Vermylen, J., Hoylaerts, M.F. J. Biol. Chem. (2003) [Pubmed]
  16. The P2X1 receptor, an adenosine triphosphate-gated cation channel, is expressed in human platelets but not in human blood leukocytes. Clifford, E.E., Parker, K., Humphreys, B.D., Kertesy, S.B., Dubyak, G.R. Blood (1998) [Pubmed]
  17. Smooth muscle and purinergic contraction of the human, rabbit, rat, and mouse testicular capsule. Banks, F.C., Knight, G.E., Calvert, R.C., Turmaine, M., Thompson, C.S., Mikhailidis, D.P., Morgan, R.J., Burnstock, G. Biol. Reprod. (2006) [Pubmed]
  18. The purinergic component of human vas deferens contraction. Banks, F.C., Knight, G.E., Calvert, R.C., Thompson, C.S., Morgan, R.J., Burnstock, G. Fertil. Steril. (2006) [Pubmed]
  19. Structure-activity relationships of pyridoxal phosphate derivatives as potent and selective antagonists of P2X1 receptors. Kim, Y.C., Brown, S.G., Harden, T.K., Boyer, J.L., Dubyak, G., King, B.F., Burnstock, G., Jacobson, K.A. J. Med. Chem. (2001) [Pubmed]
  20. Purines and their roles in apoptosis. Chow, S.C., Kass, G.E., Orrenius, S. Neuropharmacology (1997) [Pubmed]
  21. A comparison of the binding characteristics of recombinant P2X1 and P2X2 purinoceptors. Michel, A.D., Lundström, K., Buell, G.N., Surprenant, A., Valera, S., Humphrey, P.P. Br. J. Pharmacol. (1996) [Pubmed]
  22. Co-expression of P2X1 and P2X5 receptor subunits reveals a novel ATP-gated ion channel. Torres, G.E., Haines, W.R., Egan, T.M., Voigt, M.M. Mol. Pharmacol. (1998) [Pubmed]
  23. Hetero-oligomeric assembly of P2X receptor subunits. Specificities exist with regard to possible partners. Torres, G.E., Egan, T.M., Voigt, M.M. J. Biol. Chem. (1999) [Pubmed]
  24. Differential expression of P2X-purinoceptor subtypes in circular and longitudinal muscle of canine colon. Lee, H.K., Ro, S., Keef, K.D., Kathy, K.D., Kim, Y.H., Kim, H.W., Horowitz, B., Sanders, K.M. Neurogastroenterol. Motil. (2005) [Pubmed]
  25. A quantitative analysis of purinoceptor expression in the bladders of patients with symptomatic outlet obstruction. O'Reilly, B.A., Kosaka, A.H., Chang, T.K., Ford, A.P., Popert, R., McMahon, S.B. BJU international. (2001) [Pubmed]
  26. P2 receptor expression profiles in human vascular smooth muscle and endothelial cells. Wang, L., Karlsson, L., Moses, S., Hultgårdh-Nilsson, A., Andersson, M., Borna, C., Gudbjartsson, T., Jern, S., Erlinge, D. J. Cardiovasc. Pharmacol. (2002) [Pubmed]
  27. P2X7 receptor activation-induced contraction and lysis in human saphenous vein smooth muscle. Cario-Toumaniantz, C., Loirand, G., Ladoux, A., Pacaud, P. Circ. Res. (1998) [Pubmed]
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