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Role and initiation mechanism of the interaction of glycoprotein Ib with
surface-immobilized von Willebrand factor in a solid-phase platelet
cohesion process
S Tsuji, M Sugimoto, M Kuwahara, K Nishio, Y Takahashi, Y Fujimura, Y Ikeda and A Yoshioka
Department of Pediatrics, Nara Medical University, Japan.
To know the role and initiation mechanism of the interaction of
glycoprotein (GP) Ib with surface-immobilized von Willebrand factor (vWF),
we examined the effect of shear stress levels on platelet binding to
vWF-coated plates using a cone-and-plate type viscometer capable of loading
various levels of shear stress. The extent of platelet binding to
immobilized vWF reached a plateau at the shortest period tested (20
seconds) under high shear stress (90 dyne/cm2), whereas 9 to 12 minutes was
necessary for saturable platelet binding under static conditions. This
shear effect, which was found to be dependent on the vWF-GP Ib interaction,
was observed even under the lowest shear stress (1.5 dyne/cm2) examined. In
contrast with the high shear effect previously reported to initiate the
interaction of GP Ib with soluble vWF, these results indicate that
relatively low levels of shear stress can promote the interaction of GP Ib
with surface- immobilized vWF. This effect of shear stress was observed
regardless of the manner in which vWF was immobilized, suggesting that
immobilization itself and not, as previously hypothesized, a conformational
change in vWF induced by direct adsorption to the surface is responsible
for the enhanced GPIb binding. Thus, the present findings suggest that the
vWF- GP Ib interaction contributes optimally to rapid platelet cohesion on
a thrombogenic surface when vWF is in a static state and when platelets are
moved by an appropriate rheological force such as low shear stress.
Volume 88,
Issue 10,
pp. 3854-3861,
11/15/1996
Copyright © 1996 by The American Society of Hematology
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