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Blood, 15 July 2004, Vol. 104, No. 2, pp. 390-396. Prepublished online as a Blood First Edition Paper on March 23, 2004; DOI 10.1182/blood-2003-12-4224. This Article Full Text Full Text (PDF) All Versions of this Article: 2003-12-4224v1 104/2/390    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 Schoolmeester, A. Articles by Deckmyn, H. Search for Related Content PubMed PubMed Citation Articles by Schoolmeester, A. Articles by Deckmyn, H. Related Collections Cell Adhesion and Motility Signal Transduction Hemostasis, Thrombosis, and Vascular Biology Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Monoclonal antibody IAC-1 is specific for activated 21 and binds to amino acids 199 to 201 of the integrin 2 I-domain Anne Schoolmeester, Karen Vanhoorelbeke, Shinya Katsutani, Hilde Depraetere, Hendrik B. Feys, Johan M. W. Heemskerk, Marc F. Hoylaerts, and Hans Deckmyn From the Laboratory for Thrombosis Research, Interdisciplinary Research Center (IRC), K.U. Leuven Campus Kortrijk, Belgium; the Department of Biochemistry, Cardiovascular Research Institute Maastricht (CARIM), University of Maastricht, The Netherlands; and the Center for Molecular and Vascular Biology, K.U. Leuven, Belgium. In this study we describe the first monoclonal antibody, integrin activated conformation-1 (IAC-1), to recognize the active form of the platelet-collagen receptor, the integrin 21. IAC-1 has the following properties: (1) IAC-1 fails to bind to resting platelets but readily interacts with platelets stimulated by the glycoprotein VI-specific agonist, convulxin, and by other agonists; (2) similar concentration response relationships for binding of IAC-1 and soluble collagen were observed in convulxin-stimulated platelets; (3) the epitope for IAC-1 is T199Y200K201, which is located at the opposite site of the metal ion-dependent adhesion site in a region not involved in the I-domain "shifts" that occur upon ligand binding; (4) IAC-1 strongly binds to recombinant 2 I-domain, therefore suggesting that the neo-epitope appears to be exposed by an "unmasking" of I-domain-covering regions upon activation; (5) IAC-1 binds to platelets during adhesion to collagen under shear conditions, demonstrating activation of 21; (6) as IAC-1 does not interfere with platelet-collagen binding, it defines a new class of antibodies that is distinct from those belonging to the "cation- and ligand-induced binding sites" (CLIBSs) and the "ligand mimetic" group. These characteristics make IAC-1 a very powerful tool to study 21 activation under dynamic and physiologically relevant conditions. (Blood. 2004;104:390-396) CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? Related Article in Blood Online: Dotting the I of an I-domain Joel S. Bennett Blood 2004 104: 299-300. [Full Text] [PDF] This article has been cited by other articles: V. Tchesnokova, P. Aprikian, O. Yakovenko, C. LaRock, B. Kidd, V. Vogel, W. Thomas, and E. Sokurenko Integrin-like Allosteric Properties of the Catch Bond-forming FimH Adhesin of Escherichia coli J. Biol. Chem., March 21, 2008; 283(12): 7823 - 7833. [Abstract] [Full Text] [PDF] G. R. Van de Walle, A. Schoolmeester, B. F. Iserbyt, J. M. E. M. Cosemans, J. W. M. Heemskerk, M. F. Hoylaerts, A. Nurden, K. Vanhoorelbeke, and H. 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