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Gene Review

P2RX5  -  purinergic receptor P2X, ligand gated ion...

Homo sapiens

Synonyms: ATP receptor, LRH-1, P2X purinoceptor 5, P2X5, P2X5R, ...
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Disease relevance of P2RX5


High impact information on P2RX5

  • Here, we have used genetic linkage analysis to identify a novel mHAg, designated lymphoid-restricted histocompatibility antigen-1 (LRH-1), which is encoded by the P2X5 gene and elicited an allogeneic CTL response in a patient with chronic myeloid leukemia after donor lymphocyte infusion [3].
  • P2X5 Subunit Assembly Requires Scaffolding by the Second Transmembrane Domain and a Conserved Aspartate [4].
  • When expressed in Xenopus oocytes, hetero-oligomeric P2X1+5 ATP receptors were characterized by slowly desensitizing currents highly sensitive to the agonist alpha,beta-methylene ATP (EC50 = 1.1 microM) and to the antagonist trinitrophenyl ATP (IC50 = 64 nM), observed with neither P2X1 nor P2X5 alone [5].
  • Reversal potential measurements showed that the human P2X5 receptor was permeable to calcium (PCa/PNa = 1.5) and N-methyl-d-glucamine (NMDG) (PNMDG/PNa = 0.4); it was also permeable to chloride (PCl/PNa = 0.5) but not gluconate (Pgluc/PNa = 0.01) ions [6].
  • 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 [7].

Biological context of P2RX5


Anatomical context of P2RX5


Regulatory relationships of P2RX5

  • 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) [7].

Analytical, diagnostic and therapeutic context of P2RX5


  1. Expression of purinergic receptors in non-melanoma skin cancers and their functional roles in A431 cells. Greig, A.V., Linge, C., Healy, V., Lim, P., Clayton, E., Rustin, M.H., McGrouther, D.A., Burnstock, G. J. Invest. Dermatol. (2003) [Pubmed]
  2. Expression of P2 receptors in human B cells and Epstein-Barr virus-transformed lymphoblastoid cell lines. Lee, D.H., Park, K.S., Kong, I.D., Kim, J.W., Han, B.G. BMC Immunol. (2006) [Pubmed]
  3. A frameshift polymorphism in P2X5 elicits an allogeneic cytotoxic T lymphocyte response associated with remission of chronic myeloid leukemia. de Rijke, B., van Horssen-Zoetbrood, A., Beekman, J.M., Otterud, B., Maas, F., Woestenenk, R., Kester, M., Leppert, M., Schattenberg, A.V., de Witte, T., van de Wiel-van Kemenade, E., Dolstra, H. J. Clin. Invest. (2005) [Pubmed]
  4. P2X5 Subunit Assembly Requires Scaffolding by the Second Transmembrane Domain and a Conserved Aspartate. Duckwitz, W., Hausmann, R., Aschrafi, A., Schmalzing, G. J. Biol. Chem. (2006) [Pubmed]
  5. Functional and biochemical evidence for heteromeric ATP-gated channels composed of P2X1 and P2X5 subunits. Lê, K.T., Boué-Grabot, E., Archambault, V., Séguéla, P. J. Biol. Chem. (1999) [Pubmed]
  6. Pharmacological and biophysical properties of the human P2X5 receptor. Bo, X., Jiang, L.H., Wilson, H.L., Kim, M., Burnstock, G., Surprenant, A., North, R.A. Mol. Pharmacol. (2003) [Pubmed]
  7. 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]
  8. Purinergic receptors are part of a functional signaling system for proliferation and differentiation of human epidermal keratinocytes. Greig, A.V., Linge, C., Terenghi, G., McGrouther, D.A., Burnstock, G. J. Invest. Dermatol. (2003) [Pubmed]
  9. Purinergic receptors are part of a signaling system for keratinocyte proliferation, differentiation, and apoptosis in human fetal epidermis. Greig, A.V., Linge, C., Cambrey, A., Burnstock, G. J. Invest. Dermatol. (2003) [Pubmed]
  10. Expression of purinergic receptors (ionotropic P2X1-7 and metabotropic P2Y1-11) during myeloid differentiation of HL60 cells. Adrian, K., Bernhard, M.K., Breitinger, H.G., Ogilvie, A. Biochim. Biophys. Acta (2000) [Pubmed]
  11. P2X purinergic receptor channel expression and function in bovine aortic endothelium. Ramirez, A.N., Kunze, D.L. Am. J. Physiol. Heart Circ. Physiol. (2002) [Pubmed]
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