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Updated: Jun 16, 2026

A Uniform Shear Assay for Human Platelet and Cell Surface Receptors via Cone-plate Viscometry
Published on: June 5, 2019
The interaction of recombinant factor VIIa with platelet glycoprotein Ib
Ton Lisman1, Philip G de Groot
1Surgical Research Laboratory, Department of Surgery, University Medical Center Groningen, University of Groningen, Groningen, The Netherlands. j.a.lisman@chir.umcg.nl
Abstract:
Recombinant factor VIIa (rFVIIa) exerts potent prohemostatic activities via both tissue factor-dependent and -independent mechanisms. Tissue factor-independent enhancement of hemostasis involves a direct interaction of rFVIIa with the activated platelet membrane resulting in factor X activation. We have recently shown that rFVIIa binds to the platelet glycoprotein Ib/IX/V complex in addition to the negatively charged membrane surface. This interaction appears to slightly enhance tissue factor-independent thrombin generation. These findings add to our understanding of the mechanism of action of rFVIIa and may lead to improved therapeutic use of the drug.
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