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Tumor necrosis factor-alpha induces activation of coagulation and
fibrinolysis in baboons through an exclusive effect on the p55 receptor
T van der Poll, PM Jansen, KJ Van Zee, MB Welborn , I de Jong, CE Hack, H Loetscher, W Lesslauer, SF Lowry and LL Moldawer
Cornell University Medical College, Laboratory of Surgical Metabolism, New
York, NY 10021, USA.
Tumor necrosis factor-alpha (TNF-alpha) can bind to two distinct
transmembrane receptors, the p55 and p75 TNF receptors. We compared the
capability of two mutant TNF proteins with exclusive affinity for the p55
or p75 TNF receptor with that of wild type TNF, to activate the hemostatic
mechanism in baboons. Both activation of the coagulation system, monitored
by the plasma levels of thrombin-antithrombin III complexes, and activation
of the fibrinolytic system (plasma levels of tissue-type plasminogen
activator, and plasminogen activator inhibitor type I), were of similar
magnitude after intravenous injection of wild type TNF or the TNF mutant
with affinity only for the p55 receptor. Likewise, wild type TNF and the
TNF p55 specific mutant were equally potent in inducing neutrophil
degranulation (plasma levels of elastase- alpha 1-antitrypsin complexes).
Wild type TNF tended to be a more potent inducer of secretory phospholipase
A2 release than the p55 specific TNF mutant. Administration of the TNF
mutant binding only to the p75 receptor did not induce any of these
responses. We conclude that TNF-Induced stimulation of coagulation,
fibrinolysis, neutrophil degranulation, and release of secretory
phospholipase A2 are predominantly mediated by the p55 TNF receptor.
Volume 88,
Issue 3,
pp. 922-927,
08/01/1996
Copyright © 1996 by The American Society of Hematology
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