Identification of binding domains for basic fibroblast growth factor in proteoglycan macrophage colony-stimulating factor

Biochem Biophys Res Commun. 1997 Jan 13;230(2):392-7. doi: 10.1006/bbrc.1996.5968.

Abstract

We recently demonstrated that proteoglycan macrophage colony-stimulating factor (PG-M-CSF) binds basic fibroblast growth factor (bFGF) and neutralizes the biological activity of bFGF. In this study, we identified the binding sites of PG-M-CSF for bFGF. We examined the binding of bFGF to overlapping 12-mer peptides with the sequence of the putative binding region. High affinity binding was detected at two peaks; one consisted of the three adjacent peptides, 212-223, 213-224 and 214-225 and the other, of the three adjacent peptides, 246-257, 247-258 and 248-259. The synthetic peptide (212VDPGSAKQRPPRST225) did not inhibit bFGF binding to another peptide (246PQPRPSVGAFNPGM259), and vice versa. However, both peptides inhibited the bFGF-induced but not platelet-derived growth factor-induced stimulation of DNA synthesis in murine Balb/c 3T3 cells.

MeSH terms

  • 3T3 Cells
  • Amino Acid Sequence
  • Animals
  • Binding Sites
  • CHO Cells
  • Cell Division / drug effects
  • Cricetinae
  • DNA / biosynthesis
  • Fibroblast Growth Factor 2 / chemistry*
  • Fibroblast Growth Factor 2 / metabolism*
  • Humans
  • Kinetics
  • Macrophage Colony-Stimulating Factor / chemistry*
  • Macrophage Colony-Stimulating Factor / metabolism*
  • Mice
  • Molecular Sequence Data
  • Peptide Fragments / chemical synthesis
  • Peptide Fragments / chemistry
  • Peptide Fragments / pharmacology*
  • Proteoglycans / chemistry*
  • Proteoglycans / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism
  • Transfection

Substances

  • Peptide Fragments
  • Proteoglycans
  • Recombinant Proteins
  • Fibroblast Growth Factor 2
  • Macrophage Colony-Stimulating Factor
  • DNA