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J. Biol. Chem., Vol. 262, Issue 21, 9935-9938, Jul, 1987
Platelet glycoprotein IIb-IIIa-like proteins mediate endothelial cell attachment to adhesive proteins and the extracellular matrix
IF Charo, LS Bekeart and DR Phillips
The adherence of human umbilical vein endothelial (HUVE) cells to adhesive
matrix proteins was examined to determine if cell attachment and spreading
were mediated by the glycoprotein (GP) IIb-IIIa complex on endothelial
cells. The HUVE cells adhered well to glass slides that had been coated
with fibronectin, vitronectin, fibrinogen, or von Willebrand factor but
failed to adhere to albumin-coated or to uncoated slides. The HUVE cell
attachment and spreading on vitronectin, fibrinogen, and von Willebrand
factor were greatly inhibited by a GP IIb-IIIa monoclonal antibody (7E3).
In contrast, HUVE cell attachment to fibronectin was not inhibited by 7E3
but was inhibited by a fibronectin-receptor antibody (alpha GP140), which
had no effect on cell attachment to the other adhesive proteins. The 7E3
antibody, but not alpha GP140, disrupted HUVE cell monolayers by detaching
cells from their naturally occurring extracellular matrix. These data
indicate that platelet GP IIb-IIIa-like proteins mediate the adherence of
HUVE cells to specific adhesive proteins and to the extracellular matrix.

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Copyright © 1987 by the American Society for Biochemistry and Molecular Biology.
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