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Platelet adhesion to fibronectin in flow: the importance of von Willebrand
factor and glycoprotein Ib
S Beumer, HF Heijnen, MJ IJsseldijk, E Orlando, PG de Groot and JJ Sixma
Department of Haematology, University Hospital Utrecht, The Netherlands.
We describe glycoprotein (GP) Ib as a mediator of adhesion to fibronectin,
specifically in flow. A monoclonal antibody (MoAb) directed to the von
Willebrand factor (vWF)-binding site on this receptor or the absence of
this receptor on the platelet membrane, in the case of a patient with the
Bernard-Soulier syndrome, reduced platelet coverage to fibronectin to
approximately 30% of the control value. A MoAb directed to the GP
Ib-binding site on vWF showed a similar effect. With washed platelets in
the absence of plasma vWF, the inhibitory effect of the anti-GP Ib antibody
was the same as with whole blood. No inhibition with the anti-GP Ib
antibody was observed when we used blood from patients with severe von
Willebrand disease (vWD) or from a patient with vWD type I (platelet low).
Addition of vWF to vWD blood resulted in restoration of adhesion.
Immunoelectron microscopy on platelets adhering to fibronectin showed that
GP Ib was homogeneously distributed over the entire surface of the
platelet. vWF was present at the central zone and the edges of the platelet
and at the basal interface between the platelet and the fibronectin
surface. No direct binding of vWF to fibronectin could be demonstrated.
These data indicate that GP Ib-mediated adhesion to fibronectin fully
depends on vWF and that normal levels of plasma or platelet vWF are
sufficient for optimal adhesion to fibronectin. The data suggest that the
presence of platelets during perfusion is a prerequisite for vWF to support
platelet adhesion to fibronectin.
Volume 86,
Issue 9,
pp. 3452-3460,
11/01/1995
Copyright © 1995 by The American Society of Hematology
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