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Fibrinogen competes with von Willebrand factor for binding to the
glycoprotein IIb/IIIa complex when platelets are stimulated with thrombin
HR Gralnick, SB Williams and BS Coller
Two monoclonal antibodies--one that blocks ristocetin-induced platelet
binding of von Willebrand factor to glycoprotein Ib and one that blocks
adenosine diphosphate-induced binding of fibrinogen to the glycoprotein
IIb/IIIa complex--were used to assess the binding site(s) for von
Willebrand factor when platelets are stimulated with thrombin or adenosine
diphosphate (ADP). Neither agonist induced binding of von Willebrand factor
to glycoprotein Ib. ADP and thrombin induced von Willebrand factor binding
exclusively to the glycoprotein IIb/IIIa complex. The results of the site
of binding of von Willebrand factor with thrombasthenic platelets were
consistent with the data obtained with the monoclonal antibodies and normal
platelets. Human fibrinogen caused complete inhibition of thrombin-induced
von Willebrand factor binding to normal platelets at concentrations
considerably below that found in normal plasma. We conclude that thrombin
induces very little binding of exogenous von Willebrand factor to platelets
at normal plasma fibrinogen levels.
Volume 64,
Issue 4,
pp. 797-800,
10/01/1984
Copyright © 1984 by The American Society of Hematology
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