Thrombolytic properties of an inactive proenzyme form of human urokinase secreted from human kidney cells.

Abstract:

:The relative fibrin-binding, fibrinolytic and fibrinogenolytic properties of single-chain pro-urokinase, an inactive proenzyme form of human urokinase purified from cultured human kidney cells, and urokinase were compared. The affinity of single-chain pro-urokinase for fibrin was much higher than that of urokinase. In Vitro thrombolytic studies showed that single-chain pro-urokinase is approximately three times more potent in fibrinolysis than urokinase and that it does not degrade fibrinogen in the plasma at a concentration, at which complete plasma clot lysis takes place; whereas, urokinase extensively degrades the fibrinogen in the plasma. These specific, potent thrombolytic properties of single-chain pro-urokinase seem to be due to its high affinity for fibrin and to its conversion from the inactive single-chain form to the active two-chain form on the thrombus by the catalytic amount of plasmin generated during coagulation. This single-chain pro-urokinase obtained from human kidney cells by tissue culture should prove advantageous than urokinase in thrombolytic therapy.

journal_name

Cell Struct Funct

authors

Kasai S,Arimura H,Nishida M,Suyama T

doi

10.1247/csf.10.151

subject

Has Abstract

pub_date

1985-06-01 00:00:00

pages

151-9

issue

2

eissn

0386-7196

issn

1347-3700

journal_volume

10

pub_type

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