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Interactions of putative heparin-binding domains of basic fibroblast growth factor and its receptor, FGFR-1, with heparin using synthetic peptides.
- Source :
-
Glycoconjugate journal [Glycoconj J] 1998 Apr; Vol. 15 (4), pp. 419-22. - Publication Year :
- 1998
-
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.
- Subjects :
- Animals
Binding Sites
Binding, Competitive
Biosensing Techniques
Cell Line
DNA biosynthesis
Humans
In Vitro Techniques
Kinetics
Mice
Peptide Fragments chemical synthesis
Peptide Fragments chemistry
Rats
Receptor, Fibroblast Growth Factor, Type 1
Receptors, Fibroblast Growth Factor chemistry
Fibroblast Growth Factor 2 chemistry
Fibroblast Growth Factor 2 metabolism
Heparin metabolism
Peptide Fragments metabolism
Receptor Protein-Tyrosine Kinases
Receptors, Fibroblast Growth Factor metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0282-0080
- Volume :
- 15
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Glycoconjugate journal
- Publication Type :
- Academic Journal
- Accession number :
- 9613830
- Full Text :
- https://doi.org/10.1023/a:1006986104865