Reaction of a tumour-associated trypsin inhibitor with serine proteinases associated with coagulation and tumour invasion

U Turpeinen; E Koivunen; U H Stenman

doi:10.1042/bj2540911

Reaction of a tumour-associated trypsin inhibitor with serine proteinases associated with coagulation and tumour invasion

Biochem J. 1988 Sep 15;254(3):911-4. doi: 10.1042/bj2540911.

Authors

U Turpeinen¹, E Koivunen, U H Stenman

Affiliation

¹ Department I of Obstetrics and Gynaecology, Helsinki University Central Hospital, Finland.

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.

MeSH terms

Aprotinin / pharmacology
Chymotrypsin / antagonists & inhibitors
Fibrinolysin / antagonists & inhibitors
Humans
Kallikreins / antagonists & inhibitors
Macromolecular Substances
Neoplasm Invasiveness
Serine Proteinase Inhibitors*
Thrombin / antagonists & inhibitors
Tissue Plasminogen Activator / antagonists & inhibitors
Trypsin Inhibitor, Kazal Pancreatic / pharmacology*
Trypsin Inhibitor, Kunitz Soybean / pharmacology
Trypsin Inhibitors / pharmacology*
Urokinase-Type Plasminogen Activator / antagonists & inhibitors

Substances

Macromolecular Substances
Serine Proteinase Inhibitors
Trypsin Inhibitors
Trypsin Inhibitor, Kazal Pancreatic
Aprotinin
Trypsin Inhibitor, Kunitz Soybean
Kallikreins
Chymotrypsin
Thrombin
Tissue Plasminogen Activator
Fibrinolysin
Urokinase-Type Plasminogen Activator