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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 (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 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 Social Bookmarking                   What's this? Submitted September 26, 2002 Accepted March 29, 2003 Platelet 21 integrin activation: contribution of ligand internalization and the 2 cytoplasmic domain Zhengyan Wang, Tina M Leisner, and Leslie V Parise* Oral Biology PhD Program-Dental Research Center, The University of North Carolina, Chapel Hill, NC, USA; Pharmacology, The University of North Carolina, Chapel Hill, NC, USA Pharmacology, The University of North Carolina, Chapel Hill, NC, USA Pharmacology, The University of North Carolina, Chapel Hill, NC, USA; Center for Thrombosis and Hemostasis, Lineberger Comprehensive Cancer Center, The University of North Carolina, Chapel Hill, NC, USA * Corresponding author; email: parise{at}med.unc.edu. The 21 integrin is a major collagen receptor on platelets. While 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 FITC-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 domain 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: Z. Zou, A. A. Schmaier, L. Cheng, P. Mericko, S. K. Dickeson, T. P. Stricker, S. A. Santoro, and M. L. Kahn Negative regulation of activated {alpha}2 integrins during thrombopoiesis Blood, June 18, 2009; 113(25): 6428 - 6439. [Abstract] [Full Text] [PDF] M. W. Miller, S. Basra, D. W. Kulp, P. C. Billings, S. Choi, M. P. Beavers, O. J. T. McCarty, Z. Zou, M. L. Kahn, J. S. Bennett, et al. Small-molecule inhibitors of integrin {alpha}2{beta}1 that prevent pathological thrombus formation via an allosteric mechanism PNAS, January 20, 2009; 106(3): 719 - 724. [Abstract] [Full Text] [PDF] X. Su, J. Mi, J. Yan, P. Flevaris, Y. Lu, H. Liu, Z. Ruan, X. Wang, N. Kieffer, S. 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