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Prepublished online as a Blood First Edition Paper on May 8, 2003; DOI 10.1182/blood-2002-09-2753. This Article Full Text Full Text (PDF) All Versions of this Article: 2002-09-2753v1 102/4/1307    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 Wang, Z. Articles by Parise, L. V. Search for Related Content PubMed PubMed Citation Articles by Wang, Z. Articles by Parise, L. V. Related Collections Hemostasis, Thrombosis, and Vascular Biology Cell Adhesion and Motility Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 August 2003, Vol. 102, No. 4, pp. 1307-1315 HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Platelet 21 integrin activation: contribution of ligand internalization and the 2-cytoplasmic domain Zhengyan Wang, Tina M. Leisner, and Leslie V. Parise From the Department of Pharmacology, Center for Thrombosis and Hemostasis, Lineberger Comprehensive Cancer Center, and Oral Biology PhD Program-Dental Research Center, University of North Carolina, Chapel Hill. The 21 integrin is a major collagen receptor on platelets. Although it has been proposed that 21, like IIb3, undergoes agonist-induced activation, neither the potential contributions of 21 receptor/ligand internalization to the increase in ligand binding nor the roles of the 2 and 1 cytoplasmic domains in activation of this integrin have been previously explored. Activation of 21 was assessed with fluorescein isothiocyanate–labeled soluble type I collagen binding to platelets by flow cytometry. Although collagen internalization in response to agonist activation of platelets was significant, agonist-induced collagen binding still occurred under conditions that block internalization, with minimal changes in cell surface 21 expression. Introduction of cell-permeable peptides containing the 2 cytoplasmic tail, and especially the membrane proximal KLGFFKR domain, induced 21 activation in resting platelets, whereas a cell-permeable peptide containing the 1 cytoplasmic tail was without effect. Thus, collagen binding to stimulated platelets is increased due to 21 activation, in addition to internalization, and the GFFKR motif appears to play an important role in the activation process. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: B. Bernardi, G. F. Guidetti, F. Campus, J. R. Crittenden, A. M. Graybiel, C. Balduini, and M. Torti The small GTPase Rap1b regulates the cross talk between platelet integrin {alpha}2beta1 and integrin {alpha}IIbbeta3 Blood, April 1, 2006; 107(7): 2728 - 2735. [Abstract] [Full Text] [PDF] G. R. Van de Walle, K. Vanhoorelbeke, Z. Majer, E. Illyes, J. Baert, I. Pareyn, and H. Deckmyn Two Functional Active Conformations of the Integrin {alpha}2{beta}1, Depending on Activation Condition and Cell Type J. Biol. Chem., November 4, 2005; 280(44): 36873 - 36882. [Abstract] [Full Text] [PDF] P. A. Jordan, J. M. Stevens, G. P. Hubbard, N. E. Barrett, T. Sage, K. S. Authi, and J. M. Gibbins A role for the thiol isomerase protein ERP5 in platelet function Blood, February 15, 2005; 105(4): 1500 - 1507. [Abstract] [Full Text] [PDF] C. Lecut, A. Schoolmeester, M. J.E. Kuijpers, J. L.V. Broers, M. A.M.J. van Zandvoort, K. Vanhoorelbeke, H. Deckmyn, M. Jandrot-Perrus, and J. W.M. Heemskerk Principal Role of Glycoprotein VI in {alpha}2{beta}1 and {alpha}IIb{beta}3 Activation During Collagen-Induced Thrombus Formation Arterioscler. Thromb. Vasc. Biol., September 1, 2004; 24(9): 1727 - 1733. [Abstract] [Full Text] [PDF] A. Schoolmeester, K. Vanhoorelbeke, S. Katsutani, H. Depraetere, H. B. Feys, J. M. W. Heemskerk, M. F. Hoylaerts, and H. Deckmyn Monoclonal antibody IAC-1 is specific for activated {alpha}2{beta}1 and binds to amino acids 199 to 201 of the integrin {alpha}2 I-domain Blood, July 15, 2004; 104(2): 390 - 396. [Abstract] [Full Text] [PDF] D. Larkin, D. Murphy, D. F. Reilly, M. Cahill, E. Sattler, P. Harriott, D. J. Cahill, and N. Moran ICln, a Novel Integrin {alpha}IIb{beta}3-Associated Protein, Functionally Regulates Platelet Activation J. Biol. Chem., June 25, 2004; 279(26): 27286 - 27293. [Abstract] [Full Text] [PDF] D. A. Calderwood Integrin activation J. Cell Sci., March 1, 2004; 117(5): 657 - 666. [Abstract] [Full Text] [PDF]

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