Neutrophil proteases in plasminogen activation.

R. Machovich, A. Himer, W. G. Owen

Research output: Contribution to journalArticle

13 Citations (Scopus)

Abstract

Leukocyte elastase and leukocyte cathepsin G degrade porcine plasminogen primarily by hydrolysis of the A447-I448 bond between kringle4 and kringle5. The rate of formation of des-kringle1-4-plasminogen is faster with elastase (k"obs greater than 10(5) mol-1 s-1) than with cathepsin G (kobs less than 300 mol-1 s-1). In contrast to elastase, leukocyte cathepsin G does not inactivate alpha 2-antiplasmin. Consequently, plasminogen activation by urokinase in the presence of alpha 2-antiplasmin is elastase-dependent, but cathepsin G does not overcome the action of alpha 2-antiplasmin. The rate-enhancing effect of fibrin(ogen) fragments in plasminogen activation by tissue-type plasminogen activator is also disabled efficiently by these proteases. It is concluded that enhancement of plasmin expression by neutrophil proteases is accounted for primarily by the action of elastase.

Original languageEnglish
Pages (from-to)273-277
Number of pages5
JournalBlood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis
Volume1
Issue number3
Publication statusPublished - Aug 1990

ASJC Scopus subject areas

  • Hematology

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