Thrombin-Activatable Fibrinolysis Inhibitor

Author(s): Pauline F. Marx

Journal Name: Current Medicinal Chemistry

Volume 11 , Issue 17 , 2004

Become EABM
Become Reviewer

Abstract:

The coagulation system is a potent mechanism that prevents blood loss after vascular injury. It consists of a number of linked enzymatic reactions resulting in thrombin generation. Thrombin converts soluble fibrinogen into a fibrin clot. The clot is subsequently removed by the fibrinolytic system upon wound healing. Thrombin-activatable fibrinolysis inhibitor (TAFI), which is identical to the previously identified proteins procarboxypeptidase B, R, and U, forms a link between blood coagulation and fibrinolysis. TAFI circulates as an inactive proenzyme in the bloodstream, and becomes activated during blood clotting. The active form, TAFIa, inhibits fibrinolysis by cleaving off C-terminal lysine residues from partially degraded fibrin that stimulates the tissue-type plasminogen activator-mediated conversion of plasminogen to plasmin. Consequently, removal of these lysines leads to less plasmin formation and subsequently to protection of the fibrin clot from break down. Moreover, TAFI may also play a role in other processes such as, inflammation and tissue repair. In this review, recent developments in TAFI research are discussed.

Keywords: tafi, cpu, cpr, cpb, carboxypeptidase, coagulation, fibrinolysis

Rights & PermissionsPrintExport Cite as

Article Details

VOLUME: 11
ISSUE: 17
Year: 2004
Page: [2335 - 2348]
Pages: 14
DOI: 10.2174/0929867043364586
Price: $65

Article Metrics

PDF: 3