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Attachment of cultured human endothelial cells is promoted by specific
association with S protein (vitronectin) as well as with the ternary S
protein-thrombin-antithrombin III complex
KT Preissner, E Anders, J Grulich-Henn and G Muller-Berghaus
Clinical Research Unit for Blood Coagulation and Thrombosis, Max-Planck-
Gesellschaft, Giessen, FRG.
The interaction of the multifunctional S protein (vitronectin) with
cultured human endothelial cells of macrovascular and microvascular origin
was investigated. Purified S protein, coated on polystyrene Petri dishes,
induced dose-dependent and time-dependent attachment and spreading of human
umbilical vein endothelial cells (HUVECs) as well as human omental tissue
microvascular endothelial cells (HOTMECs) at 37 degrees C. Not only
isolated S protein, but also the ternary S protein- thrombin-antithrombin
III (STAT) complex promoted attachment of approximately 90% of the cells
within 2 hours at an S protein concentration of 0.13 mumol/L. Inhibition of
attachment in these experiments was achieved by the addition of the
cell-attachment pentapeptide Gly-Arg-Gly-Asp-Ser and by monospecific
antibodies against S protein, whereas nonrelated peptides or antibodies
against fibronectin, fibrinogen, or von Willebrand factor (vWF) were
ineffective. Direct binding of S protein to HUVECs and HOTMECs was studied
with cells in suspension at a density of 1 x 10(6) cells/mL and was maximal
after 120 minutes. S protein bound to both cell types in a dose-dependent
fashion with an estimated dissociation constant Kd = 0.2 mumol/L. At a
200-fold to 500-fold molar excess of unlabeled S protein, greater than 80%
of bound radiolabeled S protein was displaceable, whereas binding was
reduced to 30% to 50% by addition of the pentapeptide, the STAT complex, or
by physiologic concentrations of fibrinogen or vWF as well as Fab fragments
of anti(human S protein)IgG, but not by Fab rabbit IgG. These findings
present evidence for the specific association of S protein with endothelial
cells ultimately leading to attachment and spreading of cells. Moreover, a
novel function for the ternary STAT complex, which induced endothelial cell
attachment and spreading virtually identical to free S protein, is
described. These data further suggest a possible role for S protein during
coagulation as major vessel wall-related adhesive protein at sites of
vascular injury.
Volume 71,
Issue 6,
pp. 1581-1589,
06/01/1988
Copyright © 1988 by The American Society of Hematology
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