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Title: Monoclonal antibody IAC-1 is specific for activated alpha2beta1 and binds to amino acids 199 to 201 of the integrin alpha2 I-domain
Authors: Schoolmeester, Anne
Vanhoorelbeke, Karen
Katsutani, Shinya
Depraetere, Hilde
Feys, Hendrik
Heemskerk, Johan M W
Hoylaerts, Marc
Deckmyn, Hans # ×
Issue Date: Jul-2004
Series Title: Blood vol:104 issue:2 pages:390-396
Abstract: 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 alpha(2)beta(1). 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 alpha(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 alpha(2)beta(1); (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 alpha(2)beta(1) activation under dynamic and physiologically relevant conditions.
Description: Centrum voor Moleculaire en vasculaire biologie. Interdisciplinair Research centrum Campus Kortrijk (IRC) Subfaculteit Wetenschappen Campus Kortrijk.
ISSN: 0006-4971
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Interdisciplinary Research Facility Life Sciences, Campus Kulak Kortrijk
Molecular and Vascular Biology
Chemistry, Campus Kulak Kortrijk
× corresponding author
# (joint) last author

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