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Solid-phase von Willebrand factor contains a conformationally active RGD
motif that mediates endothelial cell adhesion through the alpha v beta 3
receptor
C Denis, JA Williams, X Lu, D Meyer and D Baruch
INSERM U. 143, Hopital de Bicetre, Paris, France.
The interaction of von Willebrand factor (vWF) with the alpha v beta 3
integrin of human umbilical vein endothelial cells is dependent on the RGD
sequence present at residues 1744-1746 of the mature vWF subunit. We
compared vWF and its two dimeric fragments, SpIII (residues 1-1365) and
SpII (residues 1366-2050), as adhesion substrates. Solid-phase vWF and SpII
supported endothelial cell adhesion, whereas SpIII, which contains the
glycoprotein (GP) Ib binding domain, did not. Soluble SpII inhibited
adhesion to immobilized ligands, whereas soluble vWF did not, suggesting
that exposure of the cell attachment domain involves a conformational
modification of vWF. Dendroaspin and albolabrin, two RGD- containing
peptides of the disintegrin family, were potent inhibitors of cell adhesion
to vWF (IC50 approximately 15 nmol/L). Complete inhibition of endothelial
cell adhesion to vWF was obtained in the presence of F(ab')2 of monoclonal
antibody 9 to vWF, which blocks vWF binding to platelet GPIIb/IIIa. In
contrast, monoclonal antibody 713 to vWF, which blocks its binding to
platelet GPIb, did not inhibit cell adhesion to vWF. These results indicate
that endothelial cell adhesion to vWF is mediated by an RGD-dependent
interaction with alpha v beta 3, but does not seem to involve a GPIb-like
receptor, and show the importance of the conformation of the RGD sequence.
Volume 82,
Issue 12,
pp. 3622-3630,
12/15/1993
Copyright © 1993 by The American Society of Hematology
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