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Media type:
E-Article
Title:
Factor XIII: Structure, Activation, and Interactions with Fibrinogen and Fibrin
Contributor:
LORAND, LASZLO
imprint:
Wiley, 2001
Published in:Annals of the New York Academy of Sciences
Language:
English
DOI:
10.1111/j.1749-6632.2001.tb03516.x
ISSN:
0077-8923;
1749-6632
Origination:
Footnote:
Description:
<jats:p><jats:bold>A<jats:sc>bstract</jats:sc>: </jats:bold> 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 N<jats:sup>ε</jats:sup>(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.</jats:p>