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Plasmin breaks down fibrin into soluble parts called fibrin degradation products (FDPs). FDPs compete with thrombin, and thus slow down clot formation by preventing the conversion of fibrinogen to fibrin. This effect can be seen in the thrombin clotting time (TCT) test, which is prolonged in a person that has active fibrinolysis.
Moreover, plasmin which is formed in excess in hyperfibrinolysis can proteolytically activate or inactivate many plasmatic or cellular proteins involved in hemostasis. Especially the degradation of fibrinogen, an essential protein for platelet aggregation and clot stability, may be a major cause for clinical bleeding.
Once in the body, tPA has can cause the desired thrombolytic activity (see figure), or be inactivated and removed. In the bloodstream tPA has a half-life of 4 to 6 minutes. [39] tPA can be bound by a plasminogen activator inhibitor, resulting in inactivation of its activity. The protein is then removed from the bloodstream by the liver.
Fibrin (also called Factor Ia) is a fibrous, non-globular protein involved in the clotting of blood. It is formed by the action of the protease thrombin on fibrinogen , which causes it to polymerize .
Without this inhibitory protein, plasmin activity goes largely unchecked, resulting in an accelerated and excessive breakdown of fibrin clots. [7] This means that even as the body forms necessary blood clots in response to injury or during normal hemostasis, these clots are rapidly and precipitously dissolved. [8]
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Under homeostatic conditions, the body is maintained in a finely tuned balance of coagulation and fibrinolysis. The activation of the coagulation cascade yields thrombin that converts fibrinogen to fibrin; the stable fibrin clot being the final product of hemostasis. The fibrinolytic system then functions to break down fibrinogen and fibrin.
Fibrinogen is made and secreted into the blood primarily by liver hepatocyte cells. Endothelium cells are also reported to make small amounts of fibrinogen, but this fibrinogen has not been fully characterized; blood platelets and their precursors, bone marrow megakaryocytes, while once thought to make fibrinogen, are now known to take up and store but not make the glycoprotein.