title: Thrombin activatable fibrinolysis inhibitor: not just an inhibitor of fibrinolysis.
abstract: OBJECTIVE
  To review the activation of thrombin activatable fibrinolysis inhibitor (TAFI) and activity of activated TAFI (TAFIa) as it relates to the regulation of both fibrinolytic and proinflammatory substances.
  
  
  METHODS
  Published articles and reviews (from PubMed, published between 1962 and 2003) on experimental studies of coagulation, fibrinolysis, and inflammation.
  
  
  CONCLUSIONS
  The principal physiologic role of TAFI is still a matter of debate. Although TAFI activation can result from proteolysis by a number of proteases, the most likely physiologic activators are thrombin (in complex with the cofactor thrombomodulin) and plasmin (in complex with polysaccharide cofactors). The activated enzyme, TAFIa, displays carboxypeptidase B-like activity and probably regulates both fibrinolysis and inflammation in response to injury and infection. At present, there is limited understanding of the role that TAFI plays in the interrelationships between coagulation, fibrinolysis, and inflammation. Although the potential therapeutic value of TAFIa inhibition/TAFI activation awaits further investigation, the data gathered to date suggest that, like activated protein C, TAFIa may play a pivotal role in regulating the crosstalk between coagulation, fibrinolysis, and inflammation.
authors.affiliation: McMaster University, Hamilton, Ontario, Canada.
authors.forename: Laszlo
authors.initials: L
authors.lastname: Bajzar
authors.forename: Nidhi
authors.initials: N
authors.lastname: Jain
authors.forename: Ping
authors.initials: P
authors.lastname: Wang
authors.forename: John B
authors.initials: JB
authors.lastname: Walker
mesh_terms: D025901:Carboxypeptidase B2 / Q000502:physiology*; D005342:Fibrinolysis / Q000502:physiology*; D006801:Humans; D001121:Lysine Carboxypeptidase / Q000502:physiology
chemical_list: D025901:Carboxypeptidase B2; D001121:Lysine Carboxypeptidase