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Proteolytic activation of tissue plasminogen activator by plasma and tissue enzymes
Author(s) -
Ichinose Akitada,
Kisiel Walter,
Fujikawa Kazuo
Publication year - 1984
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 - 10.1016/0014-5793(84)80779-6
Subject(s) - plasmin , kallikrein , tissue factor , tissue plasminogen activator , chemistry , fibrinolysis , thrombin , factor ixa , activator (genetics) , plasminogen activator , biochemistry , enzyme , coagulation , microbiology and biotechnology , factor x , biology , endocrinology , medicine , platelet , immunology , receptor
Tissue kallikrein and factor Xa were found to activate tissue plasminogen activator (t‐PA) at a rate comparable with that of plasmin. During the activation reaction, the single‐chain molecule was converted into a two‐chain form. A slight t‐PA activating activity was also found in plasma kallikrein. Other activated coagulation factors, factor XIIa, factor XIa, factor IXa, factor VIIa, thrombin and activated protein C had no effect on t‐PA activation. t‐PA was also activated by a tissue kallikrein‐like enzyme that was isolated from the culture medium of melanoma cells. These results indicate that tissue kallikrein and factor Xa may participate in the extrinsic pathway of human fibrinolysis.