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Mechanism of antithrombin III inhibition of factor VIIa/tissue factor
activity on cell surfaces. Comparison with tissue factor pathway
inhibitor/factor Xa-induced inhibition of factor VIIa/tissue factor
activity
LV Rao, O Nordfang, AD Hoang and UR Pendurthi
Department of Biochemistry, University of Texas Health Center at Tyler
75710.
Recent studies have shown that antithrombin III (AT III)/heparin is capable
of inhibiting the catalytic activity of factor VIIa bound either to
relipidated tissue factor (TF) in suspension or to TF expressed on cell
surfaces. We report studies of the mechanism of which by AT III inhibits
factor VIIa bound to cell surface TF and compare this inhibitory mechanism
with that of tissue factor pathway inhibitor (TFPI)-induced inhibition of
factor VIIa/TF. AT III alone and AT III/heparin to a greater extent reduced
factor VIIa bound to cell surface TF. Our data show that the decrease in
the amount of factor VIIa associated with cell surface TF in the presence
of AT III was the result of (1) accelerated dissociation of factor VIIa
from cell surface TF after the binding of AT III to factor VIIa/TF
complexes and (2) the inability of the resultant free factor VIIa-AT III
complexes to bind effectively to a new cell surface TF site. Binding of
TFPI/factor Xa to cell surface factor VIIa/TF complexes markedly decreased
the dissociation of factor VIIa from the resultant quaternary complex of
factor VIIa/TF/TFPI/factor Xa. Addition of high concentrations of factor
VIIa could reverse the AT III-induced inhibition of cell surface factor
VIIa/TF activity but not TFPI/factor Xa-induced inhibition of factor
VIIa/TF activity.
Volume 85,
Issue 1,
pp. 121-129,
01/01/1995
Copyright © 1995 by The American Society of Hematology
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