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Factor IX is activated in vivo by the tissue factor mechanism
KA Bauer, BL Kass, H ten Cate, JJ Hawiger and RD Rosenberg
Charles A. Dana Research Institute, Boston, MA.
Despite significant progress in elucidating the biochemistry of the
hemostatic mechanism, the process of blood coagulation in vivo remains
poorly understood. Factor IX is a vitamin K-dependent glycoprotein that can
be activated by factor XIa or the factor VII-tissue factor complex in
vitro. To investigate the role of these two pathways in factor IX
activation in humans, we have developed a sensitive procedure for
quantifying the peptide that is liberated with the generation of factor
IXa. The antibody population used for the immunoassay was raised in rabbits
and chromatographed on a factor IX-agarose immunoadsorbent to obtain
antibody populations with minimal intrinsic reactivity toward factor IX. We
determined that the mean level of the factor IX activation peptide (FIXP)
in normal individuals under the age of 40 years was 203 pmol/L and that
levels increased significantly with advancing age. The mean concentration
of FIXP was markedly reduced to 22.7 pmol/L in nine patients with
hereditary factor VII deficiency (factor VII coagulant activity less than
7%) but was not significantly different from normal controls in nine
subjects with factor XI deficiency (factor XI coagulant activity less than
8%). These data indicate that factor IXa generation in vivo results mainly
from the activity of the tissue factor mechanism rather than the contact
system (factor XII, prekallikrein, high molecular-weight kininogen, factor
XI). Our results may also help to explain the absence of a bleeding
diathesis in many patients with deficiencies of the contact factors of
coagulation.
Volume 76,
Issue 4,
pp. 731-736,
08/15/1990
Copyright © 1990 by The American Society of Hematology
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