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Inhibition of endotoxin-induced activation of the coagulation and
fibrinolytic pathways using a recombinant endotoxin-binding protein
(rBPI23)
MA von der Mohlen, SJ van Deventer, M Levi, B van den Ende, NI Wedel, BJ Nelson, N Friedmann and JW ten Cate
Center of Thrombosis, Hemostasis, Atherosclerosis and Inflammation
Research, Academic Medical Center, Amsterdam, The Netherlands.
A recombinant endotoxin-neutralizing protein, rBPI23, was shown to
partially prevent endotoxin-induced activation of the fibrinolytic and
coagulation systems in experimental endotoxemia in humans. In a placebo-
controlled, blinded crossover study, eight volunteers were challenged twice
with an intravenous bolus injection of endotoxin (40 EU/kg of body weight)
and concurrently received either rBPI23 (1 mg/kg) or placebo (human serum
albumin, 0.2 mg/kg). rBPI23 treatment significantly lowered the
endotoxin-induced fibrinolytic response, ie, reduced the release of
tissue-type plasminogen activator, urokinase- type plasminogen activator,
plasminogen activator inhibitor antigen, and complex formation of plasmin
alpha 2-antiplasmin (P = .0078 for each). Plasminogen activator inhibitor
activity was also reduced, but not significantly according to the Hochberg
method (P = .0304). The endotoxin-induced activation of the procoagulant
state as reflected by increase in F1 + 2 fragments and TAT complexes was
blunted by rBPI23 infusion (P = .0391 [not significant according to the
Hochberg method] and .0078, respectively). These results indicate that
rBPI23 is capable of reducing both the activation of the fibrinolytic and
the coagulation systems after low-dose endotoxin infusion in humans.
Volume 85,
Issue 12,
pp. 3437-3443,
06/15/1995
Copyright © 1995 by The American Society of Hematology
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