HGF B Human

HGF is initially secreted as a single inactive polypeptide. This precursor is cleaved by serine proteases into two chains: a 69-kDa alpha-chain and a 34-kDa beta-chain. These chains are linked by a disulfide bond to form the active, heterodimeric molecule . The beta-chain, in particular, is essential for the biological activity of HGF, as it contains the receptor-binding site necessary for activating the c-Met receptor .

Recombinant human HGF (rh-HGF) is produced using DNA technology, where the gene encoding HGF is inserted into a host cell line, such as CHO (Chinese Hamster Ovary) cells, to produce the protein . The recombinant protein is then purified to achieve high levels of purity and activity. The recombinant form of HGF is used in various research and clinical applications due to its ability to stimulate hepatocyte proliferation and act as an anti-apoptotic factor .

HGF has shown potential as a therapeutic agent for treating fatal liver diseases, such as fulminant hepatitis (FH) and late-onset hepatic failure (LOHF). Clinical trials have been conducted to evaluate the safety, pharmacokinetics, and clinical efficacy of rh-HGF in patients with these conditions . Although some adverse effects, such as a decrease in blood pressure and renal toxicity, were observed in preclinical studies, these effects were manageable and did not require cessation of treatment .

The development of rh-HGF has been a significant milestone in the field of regenerative medicine. Researchers have successfully cloned the cDNA of human HGF, elucidated its primary structure, and identified it as a novel growth factor with unique structural characteristics . This has paved the way for further studies on the therapeutic potential of HGF in various diseases and conditions.