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
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Binding Sites
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Binding, Competitive
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Biosensing Techniques
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Cell Line
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DNA / biosynthesis
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Fibroblast Growth Factor 2 / chemistry*
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Fibroblast Growth Factor 2 / metabolism*
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Heparin / metabolism*
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Humans
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In Vitro Techniques
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Kinetics
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Mice
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Peptide Fragments / chemical synthesis
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Peptide Fragments / chemistry
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Peptide Fragments / metabolism*
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Rats
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Receptor Protein-Tyrosine Kinases*
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Receptor, Fibroblast Growth Factor, Type 1
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Receptors, Fibroblast Growth Factor / chemistry
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Receptors, Fibroblast Growth Factor / metabolism*
Substances
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Peptide Fragments
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Receptors, Fibroblast Growth Factor
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Fibroblast Growth Factor 2
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Heparin
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DNA
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FGFR1 protein, human
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Fgfr1 protein, mouse
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Fgfr1 protein, rat
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Receptor Protein-Tyrosine Kinases
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Receptor, Fibroblast Growth Factor, Type 1