Dissolution of Fibrin Clot

Stable Identifier
Homo sapiens
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The crosslinked fibrin multimers in a clot are broken down to soluble polypeptides by plasmin, a serine protease. Plasmin can be generated from its inactive precursor plasminogen and recruited to the site of a fibrin clot in two ways, by interaction with tissue plasminogen activator at the surface of a fibrin clot, and by interaction with urokinase plasminogen activator at a cell surface. The first mechanism appears to be the major one responsible for the dissolution of clots within blood vessels. The second, although capable of mediating clot dissolution, may normally play a major role in tissue remodeling, cell migration, and inflammation (Chapman 1997; Lijnen 2001).
Clot dissolution is regulated in two ways. First, efficient plasmin activation and fibrinolysis occur only in complexes formed at the clot surface or on a cell membrane - proteins free in the blood are inefficient catalysts and are rapidly inactivated. Second, both plasminogen activators and plasmin itself are inactivated by specific serpins, proteins that bind to serine proteases to form stable, enzymatically inactive complexes (Kohler and Grant 2000).
These events are outlined in the drawing: black arrows connect the substrates (inputs) and products (outputs) of individual reactions, and blue lines connect output activated enzymes to the other reactions that they catalyze.

Literature References
PubMed ID Title Journal Year
11460480 Elements of the fibrinolytic system

Lijnen, HR

Ann N Y Acad Sci 2001
10853003 Plasminogen-activator inhibitor type 1 and coronary artery disease

Kohler, HP, Grant, PJ

N Engl J Med 2000
9330876 Plasminogen activators, integrins, and the coordinated regulation of cell adhesion and migration

Chapman, HA

Curr Opin Cell Biol 1997
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