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Myosin as cofactor and substrate in fibrinolysis
Author(s) -
Machovich Raymund,
Ajtai Katalin,
Kolev Krasimir,
Owen Whyte G.
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)00303-7
Subject(s) - plasmin , myosin , plasminogen activator , chemistry , biochemistry , urokinase , fibrinolysis , activator (genetics) , biophysics , substrate (aquarium) , tissue plasminogen activator , enzyme , biology , medicine , endocrinology , receptor , ecology , genetics
Myosin accelerates plasminogen activation by tissue‐type plasminogen activator (tPA), and is degraded extensively by plasmin. Myosin binds both tPA and plasminogen, and enhances activation of des 1‐77 ‐plasminogen by tPA but not by urokinase‐type plasminogen activator (uPA). Myosin decreases K M and increases k cat for des 1‐77 ‐plasminogen activation 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 μM, myosin is a high‐affinity substrate for plasmin. The findings indicate that myosin is a cofactor for plasminogen activation and a substrate for plasmin.