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PMID: 11116046 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Thrombin activatable fibrinolysis inhibitor and an antifibrinolytic pathway.

Arteriosclerosis, thrombosis, and vascular biology ·Vol. 20 ·No. 12 ·2000-12-00 ·Pages 2511-8

Bajzar L

Abstract

Coagulation and fibrinolysis are processes that form and dissolve fibrin, respectively. These processes are exquisitely regulated and protect the organism from excessive blood loss or excessive fibrin deposition. Regulation of these cascades is accomplished by a variety of mechanisms involving cellular responses, flow, and protein-protein interactions. With respect to regulation mediated by protein-protein interaction, the coagulation cascade appears to be more complex than the fibrinolytic cascade because it has more components. Yet each cascade is regulated by initiators, cofactors, feedback reactions, and inhibitors. Coagulation is also controlled by an anticoagulant pathway composed of (minimally) thrombin, thrombomodulin, and protein C.(1) Protein C is converted by the thrombin/thrombomodulin complex to activated protein C (APC), which catalyzes the proteolytic inactivation of the essential cofactors required for thrombin formation, factors Va and VIIIa. An analogous antifibrinolytic pathway has been identified recently. This pathway provides an apparent symmetry between coagulation and fibrinolysis and is also composed of thrombin, thrombomodulin, and a zymogen that is activated to an enzyme. The enzyme proteolytically inactivates a cofactor to attenuate fibrinolysis. However, unlike APC, which is a serine protease, the antifibrinolytic enzyme is a metalloprotease that exhibits carboxypeptidase B-like activity. Within a few years of each other, 5 groups independently described a molecule that accounts for this antifibrinolytic activity. We refer to this molecule as thrombin activatable fibrinolysis inhibitor (TAFI), a name that is based on functional properties by which it was identified, assayed, and purified. (Because of the preferences of some journals "activatable" is occasionally referred to as "activable.") This review will encompass a historical account of efforts to isolate TAFI and characterize it with respect to its activation, activity, regulation, and potential function in vivo.

MeSH Terms
Antifibrinolytic Agents/isolation & purification,metabolism,pharmacology Binding Sites Carboxypeptidase B2 Carboxypeptidases/genetics,isolation & purification,metabolism,pharmacology Cell-Free System Chromatography, Affinity Electrophoresis, Polyacrylamide Gel Enzyme Activation/drug effects Enzyme Stability Fibrinolysis Humans Isoenzymes/isolation & purification Kinetics Protein C/metabolism Substrate Specificity Terminology as Topic Thrombin/physiology Thrombomodulin/metabolism
Chemicals
Antifibrinolytic Agents Isoenzymes Protein C Thrombomodulin Carboxypeptidases Carboxypeptidase B2 Thrombin
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Bajzar L
Hamilton Civic Hospitals Research Centre and McMaster University, Hamilton, Ontario, Canada. lbajzar@thrombosis.hhscr.org
Article Info
Journal
Arteriosclerosis, thrombosis, and vascular biology
Abbr.
Arterioscler Thromb Vasc Biol
ISSN
1524-4636
Published
2000-12-00
Pages
2511-8
Language
English
Region
United States
NLM ID
9505803
Subset
IM
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