Abstract
Schwannoma-derived growth factor (SDGF), an epidermal growth factor (EGF) family peptide recently discovered, has an EGF-like domain in the carboxyl terminal portion. In this study, we synthesized mSDGF(38-80) corresponding to the EGF-like domain of mouse SDGF by means of stepwise solid-phase method using Fmoc chemistry in order to evaluate the biological function of the EGF-like domain in SDGF. The linear peptide of mSDGF(38-80) was folded by direct oxidation with reduced and oxidized glutathione to form intramolecular disulfide bridges in synthetic peptide. On the biological activity, we examined mitogenic activity induced by mSDGF(38-80) in NIH/3T3 fibroblast cells and interaction with EGF receptor in A431 cells. In the results, mSDGF(38-80) was confirmed to form three disulfide linkages that were similar in pattern to EGF by amino acid and sequence analysis of fragments obtained after thermolytic digestion. However, mSDGF(38-80) possessed weak mitogenic activity in NIH/3T3 cells and weak binding affinity for the EGF receptor in A431 cells compared with those of human EGF. These results suggest that the EGF-like domain of SDGF may have little effect upon mitogenic activity and the EGF receptor binding of SDGF.
Published Version
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