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New insights into the molecular mechanisms of the fibrinolytic system
Author(s) -
RIJKEN D. C.,
LIJNEN H. R.
Publication year - 2009
Publication title -
journal of thrombosis and haemostasis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.947
H-Index - 178
eISSN - 1538-7836
pISSN - 1538-7933
DOI - 10.1111/j.1538-7836.2008.03220.x
Subject(s) - plasmin , fibrinolysis , fibrin , plasminogen activator , chemistry , urokinase receptor , thrombin , microbiology and biotechnology , urokinase , tissue plasminogen activator , activator (genetics) , receptor , biophysics , biochemistry , biology , platelet , immunology , enzyme , medicine , endocrinology , genetics
Summary. 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.