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(Received for publication, July 2, 1997, and in revised form, August 27, 1997)
From the Joseph J. Jacobs Center for Thrombosis and Vascular
Biology, Department of Molecular Cardiology, Cleveland Clinic
Foundation, Cleveland, Ohio 44195
Prothrombin activation is a pivotal event in
thrombosis and hemostasis because thrombin can mediate fibrin formation
and can activate and aggregate platelets. Platelet aggregation depends upon the binding of adhesive proteins to integrin
Volume 272, Number 43,
Issue of October 24, 1997
pp. 27183-27188
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Networking in the Hemostatic System
INTEGRIN 
IIb
3 BINDS PROTHROMBIN
AND INFLUENCES ITS ACTIVATION
IIb3 on the platelet surface. In
the present study, a novel interface between the blood coagulation
system and platelets is demonstrated by showing that 1) prothrombin
binds to IIb3 and 2) this interaction accelerates prothrombin activation. Prothrombin bound to purified IIb3 in a specific, saturable, and
divalent cation-dependent manner. This interaction was
inhibited by certain monoclonal antibodies to
IIb3, by the
IIb3 ligands fibrinogen and RGD peptides, but not by thrombin or unrelated proteins. Prothrombin also interacted with IIb3 on resting and stimulated
platelets as demonstrated by soluble ligand binding and platelet
adhesion assays. Activation of prothrombin by Factor Xa alone or Factor
Xa-Va was accelerated by IIb3, and this
enhancement was blocked by a monoclonal antibody that inhibited
prothrombin binding to the receptor. Taken together, these data
identify a previously unrecognized linkage between platelets and the
blood coagulation system that may have a significant regulatory
consequence.
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