Human Fibrinogen

Abstract

The structure and physical properties of human fibrinogen and fibrin are reviewed along with methods for the detection of products of their metabolism. Interactions of human fibrinogen with thrombin, factor XIII, plasminogen, glycoprotein IIb/IIIa, and other proteins are related to their relevance to thrombosis and hemostasis. To the extent information is available, the structural determinants of these interactions are delineated, and kinetic and thermodynamic parameters associated with the interactions are listed. Individual steps in the reaction pathway for the conversion of fibrinogen to cross-linked fibrin are characterized. The altered hemostatic properties of mutational variants of fibrinogen are related to their altered structure. The structures of the genes coding for the polypeptide chains of fibrinogen are discussed along with the current state of knowledge of the control and regulation of fibrinogen synthesis. Fibrinogen catabolism and fibrinolysis are also reviewed.

Immobilization of a nonsteroidal antiinflammatory drug onto commercial segmented polyurethane surface to improve haemocompatibility properties

“…Albumin is the preponderant protein in blood, its abundance outweighing all the rest of plasma proteins [56]. Adsorption of this protein has a profound influence on the succeeding events of the blood coagulation cascade and a reduced platelet adhesion has been reported for polymers which adsorb relative amounts of albumin [57][58][59]. Fibrinogen plays a central role in hemostasis participating not only in the coagulation cascade, but it also promotes adhesion of platelets and activates then when adsorbed onto certain solid surfaces [60,61].…”