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Molecular Regulation of Fibrinolysis

  • H. Roger Lijnen
Part of the Developments in Cardiovascular Medicine book series (DICM, volume 193)

Abstract

Mammalian blood contains a fibrinolytic system comprised of a proenzyme, plasminogen, that can be converted to the active enzyme, plasmin, by several types of plasminogen activators. Plasmin, in turn, degrades fibrin into soluble fibrin degradation products [1]. Two physiological plasminogen activators have been identified that are immunologically distinct, the tissue-type (t-PA) and the urokinase-type plasminogen activator (u-PA). t-PA-mediated plasminogen activation is mainly involved in the dissolution of fibrin in the circulation [1]. u-PA binds to a specific cellular receptor (u-PAR) and activates cell-bound plasminogen; its main role appears to be in the induction of pericellular proteolysis via the degradation of matrix components or via activation of latent proteases or growth factors. Thus, u-PA may play a role in events such as tissue remodeling and repair, macrophage function, ovulation, embryo implantation, and tumor invasion [2,3]. The recent observation that mice deficient in u-PAR display a virtually normal phenotype has, however, somewhat challenged an important role of the u-PA/u-PAR system in these phenomena [4].

Keywords

Plasminogen Activator Plasminogen Activation Human Plasminogen Plasmin Inhibitor Lysine Binding Site 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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© Kluwer Academic Publishers 1997

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  • H. Roger Lijnen

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