Diversity Does Make a Difference: Fibroblast Growth Factor-Heparin Interactions
Abstract
Fibroblast growth factors (FGFs) are members of a protein family with a broad range of biological activities. The best characterized FGFs interact with two distinct extracellular receptors — a transmembrane tyrosine kinase FGF receptor (FGFR) and a heparan sulfate-related proteoglycan of the extracellular matrix. These components form a FGF—FGFR—proteoglycan complex that activates the FGF-mediated signal transduction process through FGFR dimerization. Recent crystal structure determinations of FGF—heparin complexes have provided insights into both the interactions between these components and the role of heparin-like proteoglycans in FGF function. Future advances in this field will benefit enormously from an ability to specifically prepare homogenous heparin-based oligosaccharides of defined sequence for use in biochemical and structural studies of FGF and many other systems.
Additional Information
© 1998 Current Biology Ltd. We thank T Arakawa, JR Fromm, GM Fox, RE Hileman and D Bar-Shalom for discussions of FGF and hepatic-related research conducted in the authors' laboratories, and A DiGabriele and WA Hendrickson for providing a preprint of their work on the FGF-l-heparin structure. SF was supported by the Alexander Hollaender Distinguished Postdoctoral Fellowship Program, sponsored by the DOE-OHER. Support for RJL was from National Institutes of Health grants GM38060 and HL52622.Additional details
- Eprint ID
- 53426
- DOI
- 10.1016/S0959-440X(98)80147-4
- Resolver ID
- CaltechAUTHORS:20150108-160400458
- GM38060
- NIH
- HL52622
- NIH
- Alexander Hollaender Distinguished Postdoctoral Fellowship
- Created
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2015-01-13Created from EPrint's datestamp field
- Updated
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2021-11-10Created from EPrint's last_modified field