Abstract
In this study it is demonstrated for the first time that shear stress induces the binding of exogenous von Willebrand factor (vWF) multimers to platelets. The vWF preparations used were:125I-vWF purified from human cryoprecipitate (and including all vWF multimers present in normal plasma); and35S-cysteine-vWF secreted by human umbilical vein endothelial cells (HUVECs) (and containing unusually large vWF forms, as well as all plasma-type vWF multimers). Direct shear-induced binding to washed platelets (300-360×103/μl) of radiolabeled vWF was maximum at 60-120 dynes/cm2 evaluated at 30 sec and was in extent about one-quarter of the binding stimulated by ristocetin after 3 min of incubation. The shear-induced binding of only a small percentage of added radiolabeled vWF was sufficient to initiate aggregation. Radiolabeled vWF attached to both glycoprotein (GP) Ib and GPIIb-IIIa receptors in the shear field, with complete inhibition of binding occurring with simultaneous blockade of both receptors. Binding was potentiated by ADP released from sheared platelets.
Original language | English (US) |
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Pages (from-to) | 787-793 |
Number of pages | 7 |
Journal | Annals of Biomedical Engineering |
Volume | 23 |
Issue number | 6 |
DOIs | |
State | Published - Nov 1995 |
Keywords
- Glycoproteins Ib and IIb-IIIa
- Platelets
- Shear stress
- von Willebrand factor
ASJC Scopus subject areas
- Biomedical Engineering