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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 (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 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 Related Article in Blood Online Social Bookmarking                   What's this?  Previous Article  |  Next Article  Submitted December 12, 2003 Accepted March 4, 2004 Monoclonal Antibody IAC-1 is Specific for Activated 21 and Binds to Amino Acid 199-201 of the Integrin 2 I-Domain Anne Schoolmeester, Karen Vanhoorelbeke, Shinya Katsutani, Hilde Depraetere, Hendrik B Feys, Johan M Heemskerk, Marc F Hoylaerts, and Hans Deckmyn* Laboratory for Thrombosis Research, K. U. Leuven Campus Kortrijk, Kortrijk, Belgium Department of Biochemistry, University of Maastricht, Maastricht, The Netherlands Center for Molecular and Vascular Biology, K. U. Leuven, Leuven, Belgium * Corresponding author; email: Hans.Deckmyn{at}kulak.ac.be. In this study we describe the first monoclonal antibody, IAC-1, to recognize the active form of the platelet collagen receptor, the integrin 21. IAC-1 has the following properties: (i) IAC-1 fails to bind to resting platelets but readily interacts with platelets stimulated by the GPVI-specific agonist, convulxin, and by other agonists; (ii) similar concentration response relationships for binding of IAC-1 and soluble collagen were observed in convulxin-stimulated platelets; (iii) the epitope for IAC-1 is T199Y200K201, which is located at the opposite site of the MIDAS in a region not involved in the I-domain 'shifts' that occur upon ligand binding; (iv) IAC-1 strongly binds to recombinant 2I-domain therefore suggesting that the neo-epitope appears to be exposed by an 'unmasking' of I-domain covering regions upon activation; (v) IAC-1 binds to platelets during adhesion to collagen under shear conditions, demonstrating activation of 21; (vi) 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 (CLIBS)' and the 'ligand mimetic' group. These characteristics make IAC-1 a very powerful tool to study 21 activation under dynamic and physiologically relevant conditions. 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: M. Mazzucato, M. R. Cozzi, M. Battiston, M. Jandrot-Perrus, M. Mongiat, P. Marchese, T. J. Kunicki, Z. M. Ruggeri, and L. De Marco Distinct spatio-temporal Ca2+ signaling elicited by integrin {alpha}2{beta}1 and glycoprotein VI under flow Blood, September 24, 2009; 114(13): 2793 - 2801. [Abstract] [Full Text] [PDF] 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. 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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] M. A. Cruz, J. Chen, J. L. Whitelock, L. D. Morales, and J. A. Lopez The platelet glycoprotein Ib-von Willebrand factor interaction activates the collagen receptor {alpha}2{beta}1 to bind collagen: activation-dependent conformational change of the {alpha}2-I domain Blood, March 1, 2005; 105(5): 1986 - 1991. [Abstract] [Full Text] [PDF] S. J. Shattil and P. J. Newman Integrins: dynamic scaffolds for adhesion and signaling in platelets Blood, September 15, 2004; 104(6): 1606 - 1615. 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