Lack of Critical Domains in the β-Chain of Hepatocyte Growth Factor

• Published in: Biochemical and biophysical research communications 1995-05, Vol.210 (3), p.1017-1024
• Main Authors: Lee, H.S., Huang, G.T., Sheu, J.C., Chiou, L.L., Horng, M.C., Lai, M.Y., Chen, D.S., Lee, S.C.
• Format: Article
• Language: English
• Subjects: Animals; Carcinoma, Hepatocellular; Cell Division - drug effects; Cell Line; Dogs; Hepatocyte Growth Factor - biosynthesis; Hepatocyte Growth Factor - chemistry; Hepatocyte Growth Factor - pharmacology; Humans; Liver - cytology; Liver - drug effects; Liver Neoplasms; Macromolecular Substances; Mice; Mutagenesis; Phosphotyrosine; Polymerase Chain Reaction; Proto-Oncogene Proteins c-met; Receptor Protein-Tyrosine Kinases - metabolism; Recombinant Proteins - biosynthesis; Recombinant Proteins - chemistry; Recombinant Proteins - pharmacology; Sequence Deletion; Spodoptera; Transfection; Tumor Cells, Cultured; Tyrosine - analogs & derivatives; Tyrosine - analysis; Tyrosine - metabolism
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1995.1758

Hepatocyte growth factor (HGF) is a cytokine with pleiotropic effects on many different cell types. Its biological activities depend on the disulfide-linked α β heterodimeric molecule. To study the functions of the β-chain of HGF, insect cell-expressed HGFs prepared from nested deletions from C-terminus of β-chain were studied for their biological activities and ligand-binding functions. The results demonstrated that the functions of HGF are dependent on the intactness of its β-chain. The loss of HGF activities is correlated with the progressive deletion of β-chain. There is not a single critical domain in the β-chain that is essential for the functions of HGF. We propose that β-chain may act to stabilize the ligand-receptor binding or contribute to the proper conformation of HGF to interact with its receptor.