Effects of introducing fibrinogen Aalpha character into the factor XIII activation peptide segment.

ABSTRACT: The formation of a blood clot involves the interplay of thrombin, fibrinogen, and Factor XIII. Thrombin cleaves fibrinopeptides A and B from the N-termini of the fibrinogen Aalpha and Bbeta chains. Fibrin monomers are generated that then polymerize into a noncovalently associated network. By hydrolyzing the Factor XIII activation peptide segment at the R37-G38 peptide bond, thrombin assists in activating the transglutaminase FXIIIa that incorporates cross-links into the fibrin clot. In this work, the kinetic effects of introducing fibrinogen Aalpha character into the FXIII AP segment were examined. Approximately 25% of fibrinogen Aalpha is phosphorylated at Ser3, producing a segment with improved binding to thrombin. FXIII AP ((22)AEDDL(26)) has sequence properties in common with Fbg Aalph

SUBMITTER: Jadhav MA 

PROVIDER: S-EPMC2966857 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature