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Characterization of the inhibition of tissue factor in serum
GJ Broze and JP Miletich
Tissue factor (TF) is a lipoprotein cofactor that markedly enhances the
proteolytic activation of factors IX and X by factor VIIa. The functional
activity of TF is inhibited by serum in a time- and temperature-dependent
fashion. The inhibitory effect is also dependent on the presence of calcium
ions and can be reversed by calcium chelation (EDTA) and dilution, thus
excluding direct proteolytic destruction of TF as the mechanism for
inhibition. Using crude TF, serum immunodepleted of factor VII, and serum
depleted of the vitamin K- dependent coagulation factors by BaSO4
absorption, it is shown that TF factor inhibition requires the presence of
VII(a), X(a), and an additional moiety contained in barium-absorbed serum.
When each of the other required components were at saturating
concentrations, half- maximal inhibition of TF occurred in reaction
mixtures containing 2% (vol/vol) of TF at a factor VII(a) concentration of
4 ng/mL (80 pmol/L), a factor X concentration of 50 ng/mL (850 pmol/L), and
a concentration of barium-absorbed serum of 2.5% (vol/vol). Catalytically
active factor Xa appeared to be required for the generation of optimal TF
inhibition. The results are consistent with the conclusions of Hjort that
barium-absorbed serum contains a moiety that inhibits the VIIa- Ca2+-TF
complex. The role of factor X(a) in the generation of the inhibitory
phenomenon remains to be elucidated. The inhibitor present in serum
(plasma) may in part be produced by the liver in vivo since cultured human
hepatoma cells (HepG2) secrete this inhibitory activity in vitro.
Volume 69,
Issue 1,
pp. 150-155,
01/01/1987
Copyright © 1987 by The American Society of Hematology
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