Interactions of putative heparin-binding domains of basic fibroblast growth factor and its receptor, FGFR-1, with heparin using synthetic peptides.
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.
Kinsella
L
L
Cancer Laboratory, School of Biological Sciences, Liverpool, UK.
Chen
H L
HL
Smith
J A
JA
Rudland
P S
PS
Fernig
D G
DG
D000818:Animals; D001665:Binding Sites; D001667:Binding, Competitive; D015374:Biosensing Techniques; D002460:Cell Line; D004247:DNA / Q000096:biosynthesis; D016222:Fibroblast Growth Factor 2 / Q000737:chemistry* / Q000378:metabolism*; D006493:Heparin / Q000378:metabolism*; D006801:Humans; D066298:In Vitro Techniques; D007700:Kinetics; D051379:Mice; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism*; D051381:Rats; D020794:Receptor Protein-Tyrosine Kinases; D051496:Receptor, Fibroblast Growth Factor, Type 1; D017468:Receptors, Fibroblast Growth Factor / Q000737:chemistry / Q000378:metabolism*
D010446:Peptide Fragments; D017468:Receptors, Fibroblast Growth Factor; D016222:Fibroblast Growth Factor 2; D006493:Heparin; D004247:DNA; C496348:FGFR1 protein, human; C496349:Fgfr1 protein, mouse; C496350:Fgfr1 protein, rat; D020794:Receptor Protein-Tyrosine Kinases; D051496:Receptor, Fibroblast Growth Factor, Type 1