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Fibrin formation, as well as other coagulation factors, is initiated by the binding of thrombin to its G-protein coupled receptor (GPCR), protease-activated receptor (PAR-1), in platelets, resulting in platelet shape change, ATP secretion, granule exocytosis, and aggregation. The peaks of thrombin production during thrombotic events are accompanied by large amounts of thrombin, which quickly clears fibrinogen from the circulation, but approximately 10% of this thrombin remains bound to fibrinogen to form clots. This ratio is largely dependent on the composition of the clot, e.g., fibrin polymerization, red blood cells, platelets, and white blood cells, however, fibrin is the dominant contributor to the clot strength. In the presence of a fibrin clot, the local thrombin concentrations in a blood vessel are in the 1 to 10nM range, while the local prothrombinase activity is in the 1-10 mM range [8][9][10][11][12][13][14][15][16][17][18]. These concentrations of thrombin and coagulation factors are able to lyse the fibrin clot and may generate soluble initiation factors that promote coagulation further into advanced fibrin formation. Even at this late stage, however, the fibrin clot remains unstable, and fibrin cleavage releases the soluble factors from the clot to perpetuate the cycle of thrombin generation, coagulation factor consumption, and clot dissolution.
An example of this is exhibited during a thrombotic event: the fibrin clot is first formed by the conversion of fibrinogen into fibrin in response to thrombin. By a converse reaction, thrombin is generated by the cleavage of prothrombin, which is a multi-chain, single-chain and single-chain, two-chain protein [19][20][21][22][23]. Released from the fibrin clot, the active fragments can sequester pro thrombin in complex with UH1 related-peptides to prevent reformation of new fibrin clots, which would inhibit the propagation of procoagulant fibrin strands. d2c66b5586