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Title: [Regulatory mechanism of fibrinolysis system by thrombin activatable fibrinolysis inhibitor (TAFI)]. Author: Urano T. Journal: Nihon Yakurigaku Zasshi; 2000 Nov; 116(5):298-303. PubMed ID: 11215380. Abstract: Thrombin-activatable fibrinolysis inhibitor (TAFI) is a 60-kDa plasma protein that has been shown to be identical to plasma carboxypeptidase B (CPB) and carboxypeptidase U (CPU). TAFI is activated by thrombomodulin (TM)-bound thrombin and specifically removes the C-terminal Lys and Arg by its CPB activity. One of its target substrates is the C-terminal Lys residue in the alpha-chain of plasmin-digested fibrin, which is critical for plasminogen binding to fibrin. Thus, its removal seems to be the main mechanism through which TAFI inhibits fibrinolysis. In this article, relevance of C-terminal Lys of plasmin-digested fibrin in fibrinolysis is described, and then possible roles of TAFI and TM-bound thrombin in a cross-talk between coagulation and fibrinolysis are discussed.[Abstract] [Full Text] [Related] [New Search]