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Neutralization of heparin activity by neutrophil lactoferrin
HF Wu, RL Lundblad and FC Church
Department of Pathology, University of North Carolina at Chapel Hill School
of Medicine 27599-7035.
Lactoferrin is a prominent component of neutrophil secondary granules, and
its blood concentration is increased in certain inflammatory diseases. In
contrast to the well-described biochemical characterization of lactoferrin
as an iron-binding protein, its physiologic role in the regulation of
inflammation and other host defense mechanisms is unclear. In this report,
we provide evidence that lactoferrin has a potent heparin-neutralizing
activity during thrombin inhibition by the serine proteinase inhibitors
(serpins) antithrombin and heparin co-factor II. Activated neutrophil
supernatant, which contains lactoferrin and other heparin-binding proteins,
could neutralize the heparin-dependent antithrombin-thrombin inhibition
reaction. The addition of lactoferrin to plasma corrected the heparin-
induced prolongation of blood plasma coagulation as measured by the
activated partial thromboplastin time (aPTT). Treatment of whole blood with
specific inflammatory mediators, fMLP, lipopolysaccharide (LPS), and tumor
necrosis factor-alpha (TNF-alpha) increased the concentration of both
plasma lactoferrin and platelet factor 4 while inhibiting the blood
anticoagulant activity of heparin as measured by the aPTT. These results
suggest that the prothrombotic sequelae of some inflammatory processes may
be partly due to various agonists that release neutrophil lactoferrin,
which can then neutralize glycosaminoglycan-dependent serpin-thrombin
inhibition reactions.
Volume 85,
Issue 2,
pp. 421-428,
01/15/1995
Copyright © 1995 by The American Society of Hematology
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