PMID: 9166847Jun 1, 1997Paper

Cytokine treatment of endothelial cells increases glycoprotein Ib alpha-dependent adhesion to von Willebrand factor.

Blood
D A BeachamS S Shapiro

Abstract

Endothelial cells (EC) possess at least two membrane receptors for von Willebrand factor (vWF), the vitronectin receptor (VNR, alpha(v)beta3), which recognizes an Arg-Gly-Asp (RGD) sequence in the C-terminus of vWF, and glycoprotein Ib alpha (GP Ib alpha), which interacts with a region in the N-terminal A1 domain of vWF. In the absence of added cytokines, EC attachment to a vWF substratum is mediated largely through the alpha(v)beta3, with a smaller contribution by GP Ib alpha. In the present study, we have examined the effect of cytokines on the receptor specificity of EC attachment to wild-type vWF (WT-vWF) and to vWF, which had been mutated in the C-terminal RGDS sequence (RADS-vWF). Exposure of human umbilical vein EC (HUVEC) to tumor necrosis factor-alpha (TNF-alpha) or to TNF-alpha in combination with interferon-gamma (IFN-gamma), but not to interleukin-1beta (IL-1), increased attachment to RADS-vWF by about twofold. The TNF-alpha-induced increase in EC attachment was accompanied by an increase in cell surface GP Ib alpha expression; GP Ib alpha surface expression was not increased by IL-1. Attachment of untreated HUVEC to WT-vWF could be inhibited 60% to 70% by a monoclonal antibody (MoAb) (LM609) to the VNR and 30% to 4...Continue Reading

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