Urano T
Department of Physiology, Hamamatsu University School of Medicine, 3600, Handa-cho, Hamamatsu 431-3192, Japan.
Nihon Yakurigaku Zasshi. 2000 Nov;116(5):298-303. doi: 10.1254/fpj.116.298.
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.
凝血酶激活的纤维蛋白溶解抑制剂（TAFI）是一种60 kDa的血浆蛋白，已被证明与血浆羧肽酶B（CPB）和羧肽酶U（CPU）相同。TAFI被与血栓调节蛋白（TM）结合的凝血酶激活，并通过其CPB活性特异性地去除C末端的赖氨酸和精氨酸。其靶底物之一是纤溶酶消化的纤维蛋白α链中的C末端赖氨酸残基，这对于纤溶酶原与纤维蛋白的结合至关重要。因此，其去除似乎是TAFI抑制纤维蛋白溶解的主要机制。在本文中，描述了纤溶酶消化的纤维蛋白的C末端赖氨酸在纤维蛋白溶解中的相关性，然后讨论了TAFI和与TM结合的凝血酶在凝血和纤维蛋白溶解相互作用中的可能作用。
