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Detection of factor X activation in humans
KA Bauer, BL Kass, H ten Cate, MA Bednarek, JJ Hawiger and RD Rosenberg
Charles A. Dana Research Institute, Beth Israel Hospital, Boston, MA 02215.
A sensitive radioimmunoassay (RIA) for the fragment that is liberated from
factor X when this zymogen is activated by factor VII/VIIa-tissue factor or
factor IXa was developed. Antisera were raised in rabbits to a synthetic 15
amino acid peptide containing the COOH-terminal sequence of the activation
fragment coupled to bovine serum albumin with glutaraldehyde. The
reactivity of the antibody population obtained toward the factor X zymogen
was negligible (less than 1/36,000 that of the activation peptide on a
molar basis). However, because other plasma constituents contributed to a
nonspecific basal signal in the RIA, a procedure by which the peptide could
be reproducibly extracted from plasma was developed. The mean level of this
species in normal individuals younger than the age of 40 was 66.4 pmol/L,
and elevations up to 550 pmol/L were observed in patients with evidence of
disseminated intravascular coagulation. The validity of these measurements
of factor X activation is supported by the fact that the RIA signal
migrates on reverse-phase high pressure liquid chromatography in a manner
identical to that of the native peptide and can be quantitatively
recovered. The mean concentration of the activation fragment was markedly
decreased to 25.7 pmol/L in patients with hereditary factor VII deficiency
(P = .0001 v normal controls), whereas the mean level in subjects with
factor VIII deficiency was 61.1 pmol/L (P greater than .1 v normal
controls). These data indicate that the basal (ie, in the absence of
thrombosis or provocative stimuli) levels of FXP under in vivo conditions
result mainly from the activity of the extrinsic pathway.
Volume 74,
Issue 6,
pp. 2007-2015,
11/01/1989
Copyright © 1989 by The American Society of Hematology
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