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Prepublished online as a Blood First Edition Paper on October 10, 2002; DOI 10.1182/blood-2002-02-0642. This Article Full Text (PDF) All Versions of this Article: 2002-02-0642v1 101/4/1400    most recent Alert me when this article is cited Alert me if a correction is posted 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 Nurden, P. Articles by Nurden, A. T Search for Related Content PubMed PubMed Citation Articles by Nurden, P. Articles by Nurden, A. T Social Bookmarking                   What's this? Submitted February 28, 2002 Accepted September 27, 2002 Immunolocalization of P2Y1 and TP Receptors in Platelets Showed a Major Pool Associated with the Membranes of -Granules and the Open Canalicular System Paquita Nurden*, Christel Poujol, Joelle Winckler, Robert Combrie, Nathalie Pousseau, Pamela B Conley, Sylviane Levy-Toledano, Aida Habib, and Alan T Nurden Laboratoire d'Hemobiologie, UMR 5533 Centre National de la Recherche Scientifique, Pessac Cedex, France COR Millennium, South San Francisco, CA, USA Hopital Lariboisiere, INSERM U 348, Paris, France * Corresponding author; email: Paquita.Nurden{at}cnrshl.u-bordeaux2.fr. P2Y1 and TP receptors on platelets belong to the G-protein coupled seven transmembrane domain family. They transmit signals for shape change, mobilization of calcium, and platelet aggregation. Immunogold labeling with a monoclonal antibody (MoAb) to the amino-terminal domain of P2Y1 and a polyclonal antibody to the C-terminal domain of TP revealed that while present at the platelet surface, both receptors were abundantly represented inside the platelet. Specifically, receptors were found in membranes of -granules and elements of the open-canalicular system. A similar organization was found in mature megakaryocytes.Activation of platelets by ADP and the TXA2 analog, I-BOP, increased both the labeling of P2Y1 and TP at the surface and in intracellular pools, suggesting that activation resulted in greater antibody accessibility to the receptor. A return to a platelet discoid shape and to basal values of labeling accompanied receptor desensitization. Platelets lacking the P2Y12 ADP receptor normally expressed P2Y1 and TP, both before and after activation. Studies with the anti-LIBS MoAb, AP6, confirmed that stored fibrinogen associated with internal pools of IIbß3 at the start of secretion in a microenvironment containing agonist receptors. Pharmacological antagonism of ADP or TXA2 receptors in antithrombotic therapy may need to take into account blockade of internal receptor pools. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: P. Nurden, M. Jandrot-Perrus, R. Combrie, J. Winckler, V. Arocas, C. Lecut, J.-M. Pasquet, T. J. Kunicki, and A. T. Nurden Severe deficiency of glycoprotein VI in a patient with gray platelet syndrome Blood, July 1, 2004; 104(1): 107 - 114. [Abstract] [Full Text] [PDF] L. Fang, Y. Yan, L. G. Komuves, S. Yonkovich, C. M. Sullivan, B. Stringer, S. Galbraith, N. A. Lokker, S. S. Hwang, P. Nurden, et al. PDGF C Is A Selective {alpha} Platelet-Derived Growth Factor Receptor Agonist That Is Highly Expressed in Platelet {alpha} Granules and Vascular Smooth Muscle Arterioscler Thromb Vasc Biol, April 1, 2004; 24(4): 787 - 792. [Abstract] [Full Text] [PDF]

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