Common amino acid sequences deduced from coding exons of the porcine FGF4 gene in two breeds and production of the encoded protein in Escherichia coli

Biosci Biotechnol Biochem. 2013;77(1):173-7. doi: 10.1271/bbb.120698. Epub 2013 Jan 7.

Abstract

Fibroblast growth factor 4 (FGF4) is considered a crucial gene in the development of mammalian embryos. Here we identified common amino acid sequences predicted from coding exons of the FGF4 gene in five pigs of two breeds, and HispFGF4, a 6× histidine-tagged porcine FGF4, was produced in Escherichia coli. HispFGF4 was purified efficiently from the supernatant of cell lysate by heparin column chromatography. In a porcine embryonic fibroblast cell line, HispFGF4 showed significant mitogenic activities at concentrations as low as 0.001 nM (p<0.01). To the best of our knowledge, this is the first report describing the complete nucleotide sequence of coding exons for the porcine FGF4 protein in two breeds, together with the production of a recombinant, bioactive porcine FGF4 derivative.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Base Sequence
  • Breeding
  • Cloning, Molecular
  • Escherichia coli / genetics
  • Exons*
  • Fibroblast Growth Factor 4 / genetics*
  • Fibroblast Growth Factor 4 / metabolism
  • Fibroblast Growth Factor 4 / pharmacology
  • Fibroblasts / cytology
  • Fibroblasts / drug effects
  • Molecular Sequence Data
  • Open Reading Frames*
  • Recombinant Fusion Proteins / genetics*
  • Recombinant Fusion Proteins / metabolism
  • Recombinant Fusion Proteins / pharmacology
  • Sequence Alignment
  • Swine / embryology
  • Swine / genetics*

Substances

  • Fibroblast Growth Factor 4
  • Recombinant Fusion Proteins