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Expression of a biologically active analogue of somatomedin-C/insulin-like growth factor I.

Peters MA, Lau EP, Snitman DL, Van Wyk JJ, Underwood LE, Russell WE, Svoboda ME
Gene. 1985 35 (1-2): 83-9

PMID: 3896937 · DOI:10.1016/0378-1119(85)90160-x

A synthetic gene coding for an analogue of somatomedin-C/insulin-like growth factor I (Sm-C/IGF-I) was synthesized by solid support phosphoramidite chemistry and subsequently cloned and expressed in Escherichia coli as a fusion protein. The gene, designed with a threonine codon substituted for a methionine codon at position 59 was expressed fused to an eight-amino acid leader peptide under the direction of the E. coli tryptophan promoter. The fusion protein, termed L0-[Thr59]-Sm-C/IGF-I was purified extensively (greater than 97%) and found to be 60% as active as native Sm-C/IGF-I in a radioimmunoassay and 50% as potent as native Sm-C/IGF-I in a radioreceptor assay. Like native Sm-C/IGF-I it was also mitogenic for Balb/c 3T3 cells. After removal of the eight amino acid leader peptide by cyanogen bromide treatment, the resulting threonine analogue, termed [Thr59]-Sm-C/IGF-I was 80% as potent as native Sm-C/IGF-I in both the RIA and the radioreceptor assays. It was also mitogenic in Balb/c 3T3 cells. These two analogues, therefore, display biological activities similar to human-derived Sm-C/IGF-I.

MeSH Terms (15)

Animals Cell Division Cloning, Molecular DNA, Recombinant Escherichia coli Humans Insulin Insulin-Like Growth Factor I Mice Mitogens Operon Peptide Biosynthesis Peptides Plasmids Somatomedins

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