![]() 1Ī couple of polymorphisms have been identified in the genes encoding the mature fibrinogen protein. Factor XIIIa-dependent cross-linking of adjacent γ and α chains of polymerized fibrin gives rise to γ-chain dimers and α-chain multimers and is essential for the structural integrity of a fibrin clot. Fibrinogen is a 340-kDa dimeric glycoprotein consisting of 6 chains (Aα, Bβ, γ) 2. Abnormalities in this system can cause bleeding or thrombosis. The conversion of fibrinogen to fibrin and subsequent stabilization of the growing fibrin clot by factor XIII (FXIII) are the ultimate events in the activated coagulation cascade, leading to an effective seal on vascular injury. These findings may provide a mechanism by which Ala312 fibrinogen could predispose to clot embolization. The number of branch points per square micrometer was similar between genotypes.Ĭonclusions- Our study shows that Ala312 influences clot structure and properties by increased factor XIII cross-linking and formation of thicker fibrin fibers. ![]() On electron microscopy analysis, we found larger fiber diameters in the Ala312 clots and observed a lower number of fibers per square micrometer. Methods and Results- We studied the properties of clots formed from purified Ala312 and Thr312 fibrinogen and found that Ala312 fibrinogen produces stiffer clots, associated with increased α chain cross-linking, as demonstrated by SDS-Page. We have previously shown an association of Ala312 fibrinogen with poststroke mortality in subjects with atrial fibrillation and with pulmonary embolism in subjects with venous thrombosis.
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