Role and initiation mechanism of the interaction of glycoprotein Ib with surface-immobilized von Willebrand factor in a solid-phase platelet cohesion process.

Abstract:

: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.

journal_name

Blood

journal_title

Blood

authors

Tsuji S,Sugimoto M,Kuwahara M,Nishio K,Takahashi Y,Fujimura Y,Ikeda Y,Yoshioka A

subject

Has Abstract

pub_date

1996-11-15 00:00:00

pages

3854-61

issue

10

eissn

0006-4971

issn

1528-0020

journal_volume

88

pub_type

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