The Fibrinogen Gamma Chain (FGG) is a crucial component of fibrinogen, a blood-borne glycoprotein involved in blood clotting. Fibrinogen is composed of three pairs of nonidentical polypeptide chains: alpha, beta, and gamma. The gamma chain plays a significant role in the formation of fibrin, the primary protein involved in blood clot formation following vascular injury .
The gamma chain of fibrinogen is encoded by the FGG gene, located on chromosome 4 in humans . The protein encoded by this gene is essential for the conversion of fibrinogen to fibrin by thrombin, which is a critical step in the blood coagulation process . The gamma chain also has various cleavage products that regulate cell adhesion, spreading, vasoconstriction, chemotactic activities, and act as mitogens for several cell types .
Recombinant human fibrinogen gamma chain is produced using DNA sequences encoding the human FGG gene. This recombinant protein is often expressed in yeast and is used in various research and clinical applications . The recombinant protein typically consists of 285 amino acids and has a predicted molecular mass of 32.2 kDa . It is usually lyophilized from sterile PBS and can be stored under sterile conditions at -20°C to -80°C .
Mutations in the FGG gene can lead to several disorders, including dysfibrinogenemia, hypofibrinogenemia, and thrombophilia . These conditions affect the blood’s ability to clot properly, leading to either excessive bleeding or clotting. Elevated levels of fibrinogen gamma chain have been associated with various diseases, including coronary artery disease and deep vein thrombosis . Additionally, abnormal expression of FGG mRNA has been observed in hepatocellular carcinoma (HCC) patients, suggesting its potential role as a predictor of clinical progression in these patients .