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Plasmin is an important enzyme (EC 3.4.21.7) present in blood that degrades many blood plasma proteins, most notable, fibrin clots. The degradation of fibrin is termed fibrinolysis.
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Functions
It is a serine protease that is released as plasminogen from the liver into the circulation and activated by tissue plasminogen activator (tPA), urokinase plasminogen activator (uPA), thrombin, fibrin, and factor XII (Hageman factor). It is inactivated by alpha 2-antiplasmin, a serine protease inhibitor (serpin).
Apart from fibrinolysis, plasmin proteolyses proteins in various other systems: It activates collagenases, some mediators of the complement system and weakens the wall of the Graafian follicle (leading to ovulation). It cleaves fibrin, fibronectin, thrombospondin, laminin, and von Willebrand factor.
Pathology
Deficiency in plasmin may lead to thrombosis, as clots are not degraded adequately.
Further reading
- Anglés-Cano E, Rojas G (2003). "Apolipoprotein(a): structure-function relationship at the lysine-binding site and plasminogen activator cleavage site". Biol. Chem. 383 (1): 93–9. PMID 11928826.
- Ranson M, Andronicos NM (2004). "Plasminogen binding and cancer: promises and pitfalls". Front. Biosci. 8: s294–304. PMID 12700073.
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Wikipedia content modification information:
- This page was last modified on 8 July 2008, at 00:45.
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