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The cleavage and inactivation of plasminogen activator inhibitor type 1 by
neutrophil elastase: the evaluation of its physiologic relevance in
fibrinolysis
K Wu, T Urano, H Ihara, Y Takada, M Fujie, M Shikimori, K Hashimoto and A Takada
Department of Physiology, Hamamatsu University, School of Medicine,
Shizuoka, Japan.
The effect of the proteolytic cleavage of plasminogen activator inhibitor
type 1 (PAI-1) by human neutrophil elastase (HNE) on fibrinolysis was
investigated. HNE cleaved active PAI-1 and produced low molecular weight
forms of inactive PAI-1, as previously reported. Latent PAI-1 was resistant
to HNE treatment. Vitronectin (VN) partially protected the cleavage.
NH2-terminal sequence analysis indicated that the cleavage site was
Val355-Ser356 (P4-P3). The effects of PAI-1 cleavage by HNE on clot lysis
was studied in a purified system. Clot lysis time without PAI-1 was 20.0
+/- 5.0 minutes and was prolonged to 86.7 +/- 2.9 minutes by 68 nmol/L of
PAI-1. It was shortened when HNE (from 0.6 nmol/L to 80 nmol/L) was added
and returned to the value obtained without PAI-1 by 80 nmol/L of HNE (20.0
+/- 5.8 minutes). However, in the absence of PAI-1, elastase did not
enhance clot lysis at all. Euglobulin clot lysis time was also shortened
after HNE treatment. The cleavage and inactivation of PAI-1 by HNE was
shown to be a novel pathway to enhance fibrinolysis.
Volume 86,
Issue 3,
pp. 1056-1061,
08/01/1995
Copyright © 1995 by The American Society of Hematology
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