Rijken D C, Lijnen H R
Department of Hematology, Erasmus University Medical Center Rotterdam, Rotterdam, The Netherlands.
J Thromb Haemost. 2009 Jan;7(1):4-13. doi: 10.1111/j.1538-7836.2008.03220.x. Epub 2008 Nov 8.
Fibrinolysis is regulated by specific molecular interactions between its main components. Activation of plasminogen by tissue-type plasminogen activator (t-PA) is enhanced in the presence of fibrin or at the endothelial cell surface. Urokinase-type plasminogen activator (u-PA) binds to a specific cellular u-PA receptor (u-PAR), resulting in enhanced activation of cell-bound plasminogen. Inhibition of fibrinolysis occurs at the level of plasminogen activation or at the level of plasmin. Assembly of fibrinolytic components at the surface of fibrin results in fibrin degradation. Assembly at the surface of cells provides a mechanism for generation of localized cell-associated proteolytic activity. This review includes novel proteins such a thrombin-activatable fibrinolysis inhibitor (TAFI) and discusses new insights into molecular mechanisms obtained from the rapidly growing knowledge of crystal structures of proteins.
纤维蛋白溶解由其主要成分之间的特定分子相互作用调节。在纤维蛋白存在的情况下或在内皮细胞表面，组织型纤溶酶原激活物（t-PA）对纤溶酶原的激活作用增强。尿激酶型纤溶酶原激活物（u-PA）与特定的细胞u-PA受体（u-PAR）结合，导致细胞结合型纤溶酶原的激活增强。纤维蛋白溶解的抑制发生在纤溶酶原激活水平或纤溶酶水平。纤维蛋白溶解成分在纤维蛋白表面的组装导致纤维蛋白降解。在细胞表面的组装提供了一种产生局部细胞相关蛋白水解活性的机制。本综述包括诸如凝血酶激活的纤维蛋白溶解抑制剂（TAFI）等新型蛋白质，并讨论了从蛋白质晶体结构快速增长的知识中获得的关于分子机制的新见解。
