Oxidative Modification of Fibrinogen Inhibits Its Transformation into Fibrin under the Effect of Thrombin

Abstract

Changes in the capacity of fibrinogen subjected to oxidative modification to transform into fibrin under the effect of thrombin and to form a fibrin clot were studied. The effects of oxidized fibrinogen preparations on the clot formation by citrate-treated donor plasma were evaluated by the thrombin time test. Oxidation impaired the capacity of isolated fibrinogen to form a fibrin clot under the effect of thrombin. Addition of oxidized fibrinogen solutions to donor plasma led to prolongation of the plasma clotting time. Maximum addition (33% volume) of oxidized fibrinogen led to a 10-26% prolongation of clotting time in comparison with addition of the same volume of the same solution without fibrinogen.

ROS-driven structural and functional fibrinogen modifications are reverted by interleukin-6 inhibition in Giant Cell Arteritis

“…In addition, the antioxidant (Trolox) treatment reverted this effect, confirming the role of oxidation on fibrinogen function [19]. This is in line with other reports showing that oxidation impairs the clotting ability of fibrinogen when incubated with thrombin [38,39]. In agreement, oxidized fibrinogen showed a reduced susceptibility to plasmin-induced lysis, which significantly correlated with leukocyte ROS production, dityrosine content, intrinsic fluorescence, and polymerization parameters.…”

The many faces of the octahedral ferritin protein

“…Therefore, ferritin binds to the substrate of clot formation, fibrinogen and to a-2-macroglobulin, the inhibitor of proteases that cause the formation and break down of clots. Oxidation of fibrinogen causes dysregulation of coagulation (Azizova et al 2009a). In addition, oxidized fibrinogen stimulates aggregation of platelets and activates leukocytes triggering an inflammatory response (Shcheglovitova et al 2006).…”

Oxidized tyrosinase: A possible antigenic stimulus for non-segmental vitiligo autoantibodies

“…These novel findings on tyrosinase have also been well supported by number of studies. As for examples, modification of structural protein can lead to loss of function, as fibrinogen on exposure to ROS loses its ability to form a solid clot [51]. Oxidation of synovial fluid/serum immunoglobulin' causes aggregation, which contribute to the etiology of rheumatic disorders [52,53].…”