Interactions of putative heparin-binding domains of basic fibroblast growth factor and its receptor, FGFR-1, with heparin using synthetic peptides

Glycoconj J. 1998 Apr;15(4):419-22. doi: 10.1023/a:1006986104865.

Abstract

We have examined structure-function relationships that have been proposed to account for the heparin-binding properties of basic fibroblast growth factor and its receptor, FGFR-1, using synthetic peptides, DNA synthesis assays and binding assays in a resonant mirror biosensor. The results suggest that the interaction of FGFR-1 with heparin may not be physiologically relevant and that the site of interaction of the polysaccharide on bFGF is more complex than has been anticipated.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Binding, Competitive
  • Biosensing Techniques
  • Cell Line
  • DNA / biosynthesis
  • Fibroblast Growth Factor 2 / chemistry*
  • Fibroblast Growth Factor 2 / metabolism*
  • Heparin / metabolism*
  • Humans
  • In Vitro Techniques
  • Kinetics
  • Mice
  • Peptide Fragments / chemical synthesis
  • Peptide Fragments / chemistry
  • Peptide Fragments / metabolism*
  • Rats
  • Receptor Protein-Tyrosine Kinases*
  • Receptor, Fibroblast Growth Factor, Type 1
  • Receptors, Fibroblast Growth Factor / chemistry
  • Receptors, Fibroblast Growth Factor / metabolism*

Substances

  • Peptide Fragments
  • Receptors, Fibroblast Growth Factor
  • Fibroblast Growth Factor 2
  • Heparin
  • DNA
  • FGFR1 protein, human
  • Fgfr1 protein, mouse
  • Fgfr1 protein, rat
  • Receptor Protein-Tyrosine Kinases
  • Receptor, Fibroblast Growth Factor, Type 1