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A Fifty Percent Reduction of Platelet Surface Glycoprotein Ib
Does Not Affect Platelet Adhesion Under Flow Conditions
G. Henrita van Zanten,
Harry F.G. Heijnen,
Yaping Wu,
Karin M. Schut-Hese,
Pieter J. Slootweg,
Philip G. de Groot,
Jan J. Sixma, and
Rienk Nieuwland
From the Departments of Hematology and Pathology, University Hospital
Utrecht, and Graduate School of Biomembranes, Utrecht University,
Utrecht; and the Department of Clinical Chemistry, Leiden University
Medical Centre, Leiden, The Netherlands.
Glycoprotein (GP) Ib is an adhesion receptor on the platelet surface
that binds to von Willebrand Factor (vWF). vWF becomes attached to
collagens and other adhesive proteins that become exposed when the
vessel wall is damaged. Several investigators have shown that during
cardiopulmonary bypass (CPB) surgery and also during platelet
activation in vitro by thrombin or thrombin receptor activating peptide
(TRAP) GPIb disappears from the platelet surface. Such a disappearance
is presumed to lead to a decreased adhesive capacity. In the present
study, we show that a 65% decrease in platelet surface expression of
GPIb, due to stimulation of platelets in Orgaran anticoagulated whole
blood with 15 µmol/L TRAP, had no effect on platelet adhesion to both
collagen type III and the extracellular matrix (ECM) of human umbilical
vein endothelial cells under flow conditions in a single-pass perfusion system. In contrast to adhesion, ristocetin-induced platelet
agglutination was highly dependent on the presence of GPIb.
Immunoelectron microscopic studies showed that GPIb almost immediately
returned to the platelet surface once platelets had attached to
collagen. In a subsequent series of experiments, we showed that when
less than 50% of GPIb was blocked by an inhibitory monoclonal antibody
against GPIb (6D1), platelet adhesion under flow conditions remained
unaffected.
Blood, Vol. 91 No. 7 (April 1), 1998:
pp. 2353-2359
© 1998 by The American Society of Hematology.
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