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Characterization of 25 monoclonal antibodies to factor VIII-von Willebrand
factor: relationship between ristocetin-induced platelet aggregation and
platelet adherence to subendothelium
HV Stel, KS Sakariassen, BJ Scholte, EC Veerman, TH van der Kwast, PG de Groot, JJ Sixma and JA van Mourik
We have studied the role of factor VIII-von Willebrand factor (FVIII- vWF)
in both platelet adherence to subendothelium and ristocetin- induced
platelet aggregation using monoclonal antibodies to human FVIII- vWF.
Twenty-five monoclonal antibodies were obtained, two of which were directed
to the factor VIII moiety of FVIII-vWF; one of these two completely
inhibited the procoagulant activity (FVIII:C). The remaining 23 monoclonal
antibodies were directed to the von Willebrand factor moiety of FVIII-vWF.
The ability of the latter monoclonal antibodies to inhibit platelet
adherence to arterial subendothelium was investigated with a perfusion
model. According to the number of platelets adhering to the subendothelium,
three groups of monoclonal antibodies could be discerned: (A) antibodies
not affecting platelet adherence; (B) antibodies that inhibited platelet
adherence to the level as observed when von Willebrand's disease plasma was
tested; and (C) antibodies that completely inhibited both platelet
adherence to subendothelium and ristocetin-induced platelet aggregation.
The two antibodies present in group C competed for the same or closely
related epitope(s) present on FVIII-vWF. These results demonstrate that a
domain is present on the FVIII-vWF molecule that is associated both with
ristocetin-induced aggregation and with the ability of FVIII-vWF to support
platelet adherence to the subendothelium. Based on these observations, it
is concluded that ristocetin-induced binding of FVIII-vWF to platelets
reflects, at least in part, a physiologic mechanism regulating the function
of FVIII-vWF in primary hemostasis.
Volume 63,
Issue 6,
pp. 1408-1415,
06/01/1984
Copyright © 1984 by The American Society of Hematology
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