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Regulation of von Willebrand factor-platelet interactions

Journal: Thrombosis and Haemostasis
ISSN: 0340-6245
Topic:

Theme Issue: Highlights from EMVBM 2009

DOI: http://dx.doi.org/10.1160/TH09-11-0777
Issue: 2010: 104/3 (Sep) pp. 421–653
Pages: 449-455

Regulation of von Willebrand factor-platelet interactions

P. J. Lenting (1), J. N. Pegon (1), E. Groot (2), P. G. de Groot (2)

(1) INSERM U.770 and Univ. Paris-Sud, 94276, Le Kremlin-Bicêtre, France; (2) Department of Clinical Chemistry and Haematology, University Medical Center Utrecht, Utrecht, The Netherlands

Keywords

thrombosis, von Willebrand factor, von Willebrand disease

Summary

The formation of thrombi is a multistep process involving several components, including von Willebrand factor (VWF). VWF is an adhesive multimeric protein, which acts as a molecular bridge between the subendothelial matrix and the glycoprotein Ib/IX/V receptor complex. Furthermore, VWF promotes the expansion of the platelet plug by cross-linking platelets via binding to integrin αIIbβ3. In terms of thrombus formation, it is essential that VWF-platelet interactions occur timely, that is: it should happen not too early or too late. Given the co-existence of VWF and platelets in the circulation, this implies that there must be regulatory mechanisms that prevent premature formation of VWF-rich platelet aggregates that could occlude the vasculature. Indeed, several mechanisms have been identified at the level of VWF, which are dedicated to the prevention of excessive VWF-platelet interactions following endothelial release of VWF (which may include limited exposure to shear stress, the presence of Mg2+ ions, inhibition of VWF-platelet interactions by endothelial proteins, ADAMTS13-mediated proteolysis) and of circulating VWF-platelet aggregates during normal circulation (shielding of the platelet-binding A1 domain by other regions of the VWF molecule, inhibition of VWF-platelet interactions by β2-glycoprotein I). In the present review an overview of these mechanisms will be discussed.

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