Factor XIII: Structure, Activation, and Interactions with Fibrinogen and Fibrin
- 1 June 2001
- journal article
- review article
- Published by Wiley in Annals of the New York Academy of Sciences
- Vol. 936 (1) , 291-311
- https://doi.org/10.1111/j.1749-6632.2001.tb03516.x
Abstract
Fibrin stabilizing factor (factor XIII or FXIII) plays a critical role in the generation of a viable hemostatic plug. Following exposure to thrombin and calcium, the zymogen is activated to FXIIIa that, in turn, catalyzes the formation of Nε(γ‐glutamyl)lysine protein‐to‐protein side chain bridges within the clot network. Introduction of these covalent crosslinks greatly augments the viscoelastic storage modulus of the structure and its resistance to fibrinolytic enzymes. Analysis of the individual reaction steps and regulatory control mechanisms involved in clot stabilization enabled us to reconstruct the entire physiological process. This also serves as a guide for the differential diagnosis of the variety of molecular defects of fibrin stabilization.Keywords
This publication has 74 references indexed in Scilit:
- Factor XIII Val 34 LeuStroke, 1998
- Plasma Factor XIII Binds Specifically to Fibrinogen Molecules Containing γ‘ ChainsBiochemistry, 1996
- Factor XIIIa-Catalyzed Cross-Linking of Recombinant αC Fragments of Human FibrinogenBiochemistry, 1996
- Biotinylated peptides containing a factor XIIIa or a tissue transglutaminase-reactive glutaminyl residue that block protein cross-linking phenomena by becoming incorporated into amine donor sitesBioconjugate Chemistry, 1992
- Factor XIII‐mediated cross‐linking of NH2‐terminal peptide of α2‐plasmin inhibitor to fibrinFEBS Letters, 1983
- Dissociation of the subunit structure of fibrin stabilizing factor during activation of the zymogenBiochemical and Biophysical Research Communications, 1974
- A New Haemorrhagic Disorder with Defective Fibrin Stabilization and CryofibrinogenaemiaBritish Journal of Haematology, 1974
- The transpeptidase system which crosslinks fibrin by γ-glutamyl-ε-lysine bondsBiochemical and Biophysical Research Communications, 1968
- The identification of isopeptide crosslinks in insoluble fibrinBiochemical and Biophysical Research Communications, 1968
- Accelerated Lysis of Blood ClotsNature, 1962