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Blood, 15 November 2003, Vol. 102, No. 10, pp. 3646-3651. Prepublished online as a Blood First Edition Paper on August 7, 2003; DOI 10.1182/blood-2003-06-1963. This Article Full Text Full Text (PDF) All Versions of this Article: 2003-06-1963v1 102/10/3646    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Vial, C. Articles by Evans, R. J. Search for Related Content PubMed PubMed Citation Articles by Vial, C. Articles by Evans, R. J. Related Collections Signal Transduction Hemostasis, Thrombosis, and Vascular Biology Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Lack of evidence for functional ADP-activated human P2X1 receptors supports a role for ATP during hemostasis and thrombosis Catherine Vial, Samantha J. Pitt, Jon Roberts, Michael G. Rolf, Martyn P. Mahaut-Smith, and Richard J. Evans From the Department of Cell Physiology and Pharmacology, University of Leicester, United Kingdom; and the Department of Physiology, University of Cambridge, United Kingdom. Purine nucleotides acting through P2 receptors play key roles in platelet signaling. The P2X1 receptor is an adenosine triphosphate (ATP)-gated ion channel that mediates a rapid calcium influx signal, but can also synergize with subsequent adenosine diphosphate (ADP)-evoked P2Y1 receptor-mediated responses and thus may contribute to platelet activation during hemostasis. Recent studies have shown that P2X1 receptors contribute to the formation of platelet thrombi, particularly under conditions of high shear stress. Based on intracellular Ca2+ measurements a previous report has suggested that a splice variant of the P2X1 receptor, P2X1del, is expressed in platelets and, in contrast to the full-length P2X1WT receptor, is activated by ADP. In the present study we show that the P2X1del receptor fails to form functional ion channels and is below the limit of detection in human platelets. Furthermore, ADP does not contribute to the rapid ionotropic P2X receptor-mediated response in platelets. These results support the notion that ATP is the principal physiologic agonist at P2X1 receptors and that it plays a role in the activation of platelets. (Blood. 2003;102:3646-3651) CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: C. N. Morrell, H. Sun, M. Ikeda, J.-C. Beique, A. M. Swaim, E. Mason, T. V. Martin, L. E. Thompson, O. Gozen, D. Ampagoomian, et al. Glutamate mediates platelet activation through the AMPA receptor J. Exp. Med., March 17, 2008; 205(3): 575 - 584. [Abstract] [Full Text] [PDF] M. W. Gorman, E. O. Feigl, and C. W. Buffington Human Plasma ATP Concentration Clin. Chem., February 1, 2007; 53(2): 318 - 325. [Abstract] [Full Text] [PDF] G. Tolhurst, C. Vial, C. Leon, C. Gachet, R. J. Evans, and M. P. Mahaut-Smith Interplay between P2Y1, P2Y12, and P2X1 receptors in the activation of megakaryocyte cation influx currents by ADP: evidence that the primary megakaryocyte represents a fully functional model of platelet P2 receptor signaling Blood, September 1, 2005; 106(5): 1644 - 1651. [Abstract] [Full Text] [PDF] L. G. Coleman Jr, R. K. Polanowska-Grabowska, M. Marcinkiewicz, and A. R. L. Gear LDL oxidized by hypochlorous acid causes irreversible platelet aggregation when combined with low levels of ADP, thrombin, epinephrine, or macrophage-derived chemokine (CCL22) Blood, July 15, 2004; 104(2): 380 - 389. [Abstract] [Full Text] [PDF]

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