Fibrinogen splice variation and cross-linking: Effects on fibrin structure/function and role of fibrinogen γ′ as thrombomobulin II

Abstract

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Global serum proteomic changes in water buffaloes infected with Fasciola gigantica

“…Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), FGG polymerizes to form an insoluble fibrin matrix [34], which is one of the primary components of blood clots [35]. Furthermore, FGG encoding protein functions during early stages of wound repair to stabilize the lesion and guide cell migration during re-epithelialization [36]. The downregulation of FGG can reduce the formation of blood clots and platelet aggregation in buffaloes infected with F. gigantica , which may make blood more accessible to the flukes.…”

Association of fibrinogen and plasmin inhibitor, but not coagulation factor XIII gene polymorphisms with coronary artery disease

“…Allele T favours the formation of alternatively spliced fibrinogen g'-chain instead of g-chain (17), and fibrin containing g'-variant binds thrombin more effectively, which may explain the reduced tendency to thrombosis among individuals with high levels of g'-variant. This is the current hypothesis though the mechanism by which the rs2066865 affects susceptibility to VTE is not fully elucidated (45). We can assume that the underlying mechanism in CAD patients is the same and that this explanation for 10034C > T FGG and VTE association is valid perhaps also for CAD.…”

Fibrinogen and Antifibrinolytic Proteins: Interactions and Future Therapeutics

“…During clot formation, α2AP becomes covalently cross-linked into the fibrin clot by activated factor XIII (FXIIIa) making the clot more resistant to degradation by plasmin [30]. The cross-linking mainly occurs between glutamine residue at position 14 of the α2AP molecule and lysine residue at position 303 of the α chain of fibrin [31], although additional cross-linking sites on fibrinogen have been proposed [32].…”