Fibrinogen and Related Peptides Products
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Fibrinogen, also known as blood fibrinogen, is a protein that dissolves in water and is a protein synthesized by the liver that has a clotting function. It is an important substance in the process of coagulation and thrombosis. Fibrin is a monomer protein produced by thrombectomy of fibrin A and B in blood fibrin during blood coagulation. High fibrinogen is an important risk factor for various thrombotic diseases and is considered to be a marker of disease status in the clinic. Fibrinogen, a protein with coagulation function, is mainly synthesized by hepatocytes and is the highest coagulation factor in plasma. The molecular weight of fibrinogen is about 340kDa, which is composed of three pairs of polypeptide chains: α, β andγ. The two ends are D region and the middle is E region. The D region and E region are connected by three α helix peptide chains. Fibrinogen is an important substrate for thrombosis and is involved in the key steps of thrombosis. Fibrinogen forms fibrin monomer under the action of coagulation factors such as thrombin, blood fiber stabilizer factor (FXⅢa) and Ca2+, and covalently binds to form fibrin polymer. It’s α chain overlapped and covalently crosslinked to form a stable fibrin network, and finally reticulated erythrocyte (RBC), platelet (PLT), α 2-antiplasmin (α 2-AP) and other components to form a stable thrombus structure.
Mechanism of action
When platelets rupture, they release clotting-activated enzymes, which catalyze prothrombin to become thrombin under the action of calcium ions. Then thrombin solidifies water-soluble fibrinogen in plasma into water-insoluble fibrin. Fibrin kinks other blood cells into clumps and solidifies into clots. Fibrinogen (factor I) is a glycoprotein circulating in the blood of vertebrates. During tissue and vascular injury, it is converted to fibrin by thrombin and then to fibrin-based blood clots. Fibrinogen mainly acts as a blockage of blood vessels, therefore preventing excessive bleeding. However, fibrin, the product of fibrinogen, binds to and reduces the activity of thrombin. This activity, sometimes called antithrombin I, is used to limit blood clotting. This loss or decrease in antithrombin 1 activity caused by mutations in the fibrinogen gene or low fibrinogen conditions can lead to excessive blood coagulation and thrombosis. Fibrin also mediates platelet and endothelial cell diffusion, tissue fibroblasts proliferation, capillary formation and angiogenesis, thus promoting tissue revascularization, wound healing and tissue repair.
Function
Fibrinogen can promote platelet aggregation, promote the growth, proliferation and contraction of smooth muscle and endothelial cells, increase blood viscosity and peripheral resistance, cause endothelial cell injury, and promote the synthesis of collagen and deoxyribonucleic acid. In addition it can promote the chemotactic monocytes/macrophages migrate to the intima and promote erythrocyte adhesion and thrombosis. Therefore, it plays a very important role in the pathogenesis of cardiovascular disease.
References
- Franks, J. J., Kirsch, R. E., Kao, B., & Kloppel, T. M. (1984). Fibrinogen and fibrinogen-related peptides in cancer. In Pathophysiology of plasma protein metabolism (pp. 265-278). Palgrave, London.
- dema, C. M. (2015). Fibrinogen-related proteins (FREPs) in mollusks. In Pathogen-Host Interactions: Antigenic Variation v. Somatic Adaptations (pp. 111-129). Springer, Cham.
