Structure‐function relationships in thrombin‐activatable fibrinolysis inhibitor. (30th March 2016)

• Record Type: Journal Article
• Authors: Plug, T.; Meijers, J. C. M.
• Is Part Of: Journal of thrombosis and haemostasis. Volume 14:Number 4(2016:Apr.)
• Page Start: 633
• Page End: 644
• Publication Date: 2016-03-30
• Subjects: carboxypeptidase B2 -- carboxypeptidase R -- carboxypeptidase U -- fibrinolysis -- thrombin‐activatable fibrinolysis inhibitor (TAFI); Thrombosis -- Periodicals; Hemostasis -- Periodicals; Blood coagulation disorders -- Periodicals; 616.1
• DOI: 10.1111/jth.13261
• Languages: English
• ISSNs: 1538-7933

Abstract

Summary: Thrombin‐activatable fibrinolysis inhibitor (TAFI) is an important regulator in the balance of coagulation and fibrinolysis. TAFI is a metallocarboxypeptidase that circulates in plasma as zymogen. Activated TAFI (TAFIa) cleaves C‐terminal lysine or arginine residues from peptide substrates. The removal of C‐terminal lysine residues from partially degraded fibrin leads to reduced plasmin formation and thus attenuation of fibrinolysis. TAFI also plays a role in inflammatory processes via the removal of C‐terminal arginine or lysine residues from bradykinin, thrombin‐cleaved osteopontin, C3a, C5a and chemerin. TAFI has been studied extensively over the past three decades and recent publications provide a wealth of information, including crystal structures, mutants and structural data obtained with antibodies and peptides. In this review, we combined and compared available data on structure/function relationships of TAFI.