MYOSIN AS COFACTOR AND SUBSTRATE IN FIBRINOLYSIS

Citation
R. Machovich et al., MYOSIN AS COFACTOR AND SUBSTRATE IN FIBRINOLYSIS, FEBS letters, 407(1), 1997, pp. 93-96
Citations number
20
Categorie Soggetti
Biophysics,Biology
Journal title
ISSN journal
00145793
Volume
407
Issue
1
Year of publication
1997
Pages
93 - 96
Database
ISI
SICI code
0014-5793(1997)407:1<93:MACASI>2.0.ZU;2-T
Abstract
Myosin accelerates plasminogen activation by tissue-type plasminogen a ctivator (tPA), and is degraded extensively by plasmin, Myosin binds b oth tPA and plasminogen, and enhances activation of des(1-77)-plasmino gen by tPA but not by urokinase-type plasminogen activator (uPA), Myos in decreases K-M and increases k(cat) for des(1-77)-plasminogen activa tion by tPA, to yield catalytic efficiencies in excess of 8000 M-1 s(- 1), The effect of myosin is attributed to its C-terminal portion, the myosin rod. With a K-M of 3 mu M, myosin is a high-affinity substrate for plasmin, The findings indicate that myosin is a cofactor for plasm inogen activation and a substrate for plasmin. (C) 1997 Federation of European Biochemical Societies.