Reaction of a Tumour-associated Trypsin Inhibitor with Serine Proteinases Associated with Coagulation and Tumour Invasion

Overview

Journal Biochem J

Specialty Biochemistry

Date 1988 Sep 15

PMID 2461702

Citations 10

Authors

U Turpeinen

E Koivunen

U H Stenman

Affiliations

Soon will be listed here.

Abstract

The inhibition of six serine proteinases by a tumour-associated trypsin inhibitor (TATI) was studied using synthetic peptide substrates. Physiological concentrations of TATI inhibited the amidolytic activities of trypsin, plasmin, urokinase and tissue plasminogen activator (tPA). Chymotrypsin, kallikrein and thrombin were also inhibited, but by much higher concentrations of TATI. The ability of TATI to inhibit trypsin, plasmin, urokinase and tPA suggests that it has a role in proteolytic processes in vivo involving these enzymes.

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