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On the role of von Willebrand factor in promoting platelet adhesion to
fibrin in flowing blood
SC Endenburg, RR Hantgan, L Lindeboom-Blokzijl, H Lankhof, WG Jerome, JC Lewis, JJ Sixma and PG de Groot
Department of Haematology, University of Utrecht, The Netherlands.
Platelet adhesion to fibrin at high shear rates depends on both the
glycoprotein (GP) IIb:IIIa complex and a secondary interaction between GPIb
and von Willebrand factor (vWF). This alternative link between platelets
and vWF in promoting platelet adhesion to fibrin has been examined in
flowing whole blood with a rectangular perfusion chamber. Optimal adhesion
required both platelets and vWF, as shown by the following observations. No
binding of vWF could be detected when plasma was perfused over a fibrin
surface or when coated fibrinogen was incubated with control plasma in an
enzyme-linked immunosorbent assay. However, when platelets were present
during perfusion, interactions between vWF and fibrin could be visualized
with immunoelectron microscopy. Exposure of fibrin surfaces to normal
plasma before perfusion with severe von Willebrand's disease blood did not
compensate for the presence of plasma vWF necessary for adhesion. vWF
mutants in which the GPIIb:IIIa binding site was mutated or the GPIb
binding site was deleted showed that vWF only interacts with GPIb on
platelets in supporting adhesion to fibrin and not with GPIIb:IIIa.
Complementary results were obtained with specific monoclonal antibodies
against vWF. Thus, vWF must first bind to platelets before it can interact
with fibrin and promote platelet adhesion. Furthermore, only GPIb, but not
GPIIb:IIIa is directly involved in this interaction of vWF with platelets.
Volume 86,
Issue 11,
pp. 4158-4165,
12/01/1995
Copyright © 1995 by The American Society of Hematology
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