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Acta bioquímica clínica latinoamericana

Print version ISSN 0325-2957On-line version ISSN 1851-6114

Abstract

LAURICELLA, Ana María. Fibrin network variability. Acta bioquím. clín. latinoam. [online]. 2007, vol.41, n.1, pp.7-19. ISSN 0325-2957.

Fibrin is a protein network present in the clot. It can be characterized by its structure, fibers dimensions, ramification degree, porosity, viscoelasticity and deformability. All these properties depend on temperature, ions concentrations and on other plasmatic substances, mainly fibrinogen, thrombin and factor XIII. Greater fibrinogen or thrombin concentrations produce more dense, less porous and shorter fibered-fibrin networks. Fibrinogen alterations can generate abnormal fibrin, with different susceptibility to lysis, while calcium ions increase the fibrin networks' rigidity and porosity. Plasminogen activation and fibrinolysis rate are strongly dependent on the size and the fibrin network architecture. Tight networks are lysed more slowly while, within the same gel, thin fibers are lysed before thick ones. Otherwise, thicker fibers proved to be a better cofactor of plasminogen activation. Taking into account these factors helps understand the different fibrinolytic response, mainly when it is not explained by laboratory studies.

Keywords : fibrin; fibrin properties; fibrinogen; fibrin-formation.

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