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Sequence 274-368 in the beta 3-subunit of the integrin alpha IIb beta 3
provides a ligand recognition and binding domain for the gamma-chain of
fibrinogen that is independent of platelet activation
M Alemany, E Concord, J Garin, M Vincon, A Giles, G Marguerie and D Gulino
INSERM 217, Departement de Biologie Moleculaire et Structurale (DBMS),
Centre d'Etudes Nucleaires (CEN)-Grenoble, France.
Several bacterial-expressed recombinant fragments encompassing the
extracellular part of the beta 3 subunit of the integrin alpha IIb beta 3
were shown to recognize and bind soluble and immobilized forms of
fibrinogen. Two of them, designated as rIII-11 (beta 3 274-368) and rIII-13
(beta 3 274-403), did not contain the established RGD-ligand binding
sequence. In fact, they interacted, in a Ca(2+)-independent manner, with
the C-terminal part of the fibrinogen gamma chain. Both beta 3 fragments
blocked the participation of fibrinogen in the induction of platelet
aggregation induced by adenosine diphosphate. Fragment rIII-13 was
recognized by the anti-beta 3 monoclonal antibody B2A. This antibody, which
possesses an epitope exposed on both resting and activated platelets,
inhibited fibrinogen binding as well as platelet adhesion and aggregation.
In conclusion, the results demonstrated that the 274-368 sequence of the
beta 3 subunit of integrin alpha IIb beta 3 constitutes a fibrinogen ligand
binding domain, distinct from the RGD-binding site, that is required for
both platelet adhesion and aggregation.
Volume 87,
Issue 2,
pp. 592-601,
01/15/1996
Copyright © 1996 by The American Society of Hematology
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