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Functions & Recent Research Progress
F2, also known as prothrombin or coagulation factor II, is an important component of the coagulation cascade in which it converts fibrinogen to fibrin, activates coagulation factors V, VII, VIII, XIII and forms complexes with protein C and thrombomodulin. It also activates platelets and regulates the behavior of additional cells through protease-activated receptors (PARs).As a plasma serine protease, thrombin is synthesized as a 622 amino acid precursor with a 24 amino acid signal peptide and a 19 residue pro peptide. The mature chain can be further processed into several forms including those designated as alpha-, beta- and gamma-thrombin.
Figure 1.Activation system (Yahui Chen,2015)
Most studies suggest that patients with mild hepatitis and chronic hepatitis have normal or mild decline in coagulation factor II activity; patients with moderate, severe, and cirrhosis of chronic hepatitis have significantly decreased levels of coagulation factor II activity, indicating a reduction in hepatocytes. The degree of damage is closely related.
F2, or prothrombin, is a vitamin K-dependent proenzyme that functions in the blood coagulation cascade. Inherited factor II deficiency is an extremely rare autosomal recessive disorder affecting both genders: clinical bleeding can vary widely in homozygous individuals, and heterozygotes often remain clinically asymptomatic.
Additionally, the innate immune system is the first line of defence against infection and is responsible for the recognition of pathogen-associated molecular patterns, which are important for the activation of acquired immune responses. F2 is an important factor in the coagulation system and is involved in recognition and interaction with various bacterial and extracellular proteins. In this study, scientists analyzed the expression of F2 in various tissues after pathogen challenge. The full-length F2 cDNA contains a 1854 bp open reading frame encoding 617 amino acids. Alignment analysis revealed that the gamma-carboxyglutamate-rich domain of the deduced protein, the two tricyclic domains and the trypsin-like serine protease domain are very conserved. F2 is ubiquitously expressed in all examined tissues, but is primarily detected in the liver and skin. Interestingly, F2 has agglutinating activity against E. coli and E. coli, but no agglutination effect on Vibrio ordalii and S.iniae. These findings indicate that F2 exerts immune function in immune responses and may be involved in innate immunity and blood clotting.