Integrin alpha(v)beta(3) on human endothelial cells binds von Willebrand factor strings under fluid shear stress.

ABSTRACT: Acutely secreted von Willebrand factor (VWF) multimers adhere to endothelial cells, support platelet adhesion, and may induce microvascular thrombosis. Immunofluorescence microscopy of live human umbilical vein endothelial cells showed that VWF multimers rapidly formed strings several hundred micrometers long on the cell surface after stimulation with histamine. Unexpectedly, only a subset of VWF strings supported platelet binding, which depended on platelet glycoprotein Ib. Electron microscopy showed that VWF strings often consisted of bundles and networks of VWF multimers, and each string was tethered to the cell surface by a limited number of sites. Several approaches implicated P-selectin and integrin alpha(v)beta(3) in anchoring VWF strings. An RGDS peptide or a function-blocking anti

SUBMITTER: Huang J 

PROVIDER: S-EPMC2644087 | biostudies-literature | 2009 Feb

REPOSITORIES: biostudies-literature