Principles[ edit ] D-dimer formation. Shown are fibrinogen , with its one E domain and two D domains, acted upon in cascade, by the following enzymes : Thrombin , to create a mesh of fibrin protofibrils; Factor XIII to crosslink the fibrin mesh linking protofibril D domains , the scaffold for clot formation; Plasmin , whose action in fibrinolysis produces fibrin degradation products FDPs , the smallest of which are D-dimers, protein fragments with one E and two crosslinked D domains from an original fibrinogen. Both pathways lead to the generation of thrombin , an enzyme that turns the soluble blood protein fibrinogen into fibrin, which aggregates into proteofibrils. Another thrombin-generated enzyme, factor XIII , then crosslinks the fibrin proteofibrils at the D fragment site, leading to the formation of an insoluble gel which serves as a scaffold for blood clot formation. The resultant fragments, "high molecular weight polymers", are digested several times more by plasmin to lead to intermediate and then to small polymers fibrin degradation products or FDPs. The cross-link between two D fragments remains intact, however, and these are exposed on the surface when the fibrin fragments are sufficiently digested.

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