Hepatocyte Growth Factor/Scatter Factor Binds with High Affinity to Dermatan Sulfate*

@article{Lyon1998HepatocyteGF,
  title={Hepatocyte Growth Factor/Scatter Factor Binds with High Affinity to Dermatan Sulfate*},
  author={Malcolm Lyon and Jon A. Deakin and Hassan Rahmoune and David G. Fernig and Takuji Nakamura and John T. Gallagher},
  journal={The Journal of Biological Chemistry},
  year={1998},
  volume={273},
  pages={271 - 278}
}
We have demonstrated by affinity chromatography that hepatocyte growth factor/scatter factor (HGF/SF) binds strongly to dermatan sulfate (DS), with a similar ionic strength dependence to that previously seen with heparan sulfate (HS). Analysis of binding kinetics on a biosensor yields an equilibrium dissociation constant,K D , of 19.7 nm. This corresponds to a 10–100-fold weaker interaction than that with HS, primarily due to a faster dissociation rate of the complex. The smallest DS… Expand
The Mode of Action of Heparan and Dermatan Sulfates in the Regulation of Hepatocyte Growth Factor/Scatter Factor*
TLDR
The role of these glycosaminoglycan may be primarily to effect a conformational change in hepatocyte growth factor/scatter factor, rather than to induce a necessary growth factor dimerization, or to stabilize a ternary complex by additionally interacting with Met. Expand
Hepatocyte Growth Factor/Scatter Factor Binds to Small Heparin-derived Oligosaccharides and Stimulates the Proliferation of Human HaCaT Keratinocytes*
TLDR
The results suggest that HGF/SF binds to a tetrasaccharide and that although this is sufficient to enable the stimulation of DNA synthesis, longer oligosaccharides are more efficient, perhaps by virtue of their ability to bind more easily other molecules. Expand
Interactions of Hepatocyte Growth Factor/Scatter Factor with Various Glycosaminoglycans Reveal an Important Interplay between the Presence of Iduronate and Sulfate Density*
TLDR
GAG recognition of HGF/SF appears to be primarily driven by electrostatic interactions and exhibits an interesting interplay between requirements for iduronate and sulfate density that may reflect in part a preference for particular sugar chain conformations. Expand
The Binding Properties of Minimal Oligosaccharides Reveal a Common Heparan Sulfate/Dermatan Sulfate-binding Site in Hepatocyte Growth Factor/Scatter Factor That Can Accommodate a Wide Variety of Sulfation Patterns*
TLDR
An unexpected degree of flexibility in the GAG-HGF/SF interface is revealed, allowing a single binding site in the protein to accommodate iduronate-containing sequences of variable sulfation pattern and/or density from different GAGs. Expand
The Interactions of Hepatocyte Growth Factor/Scatter Factor and Its NK1 and NK2 Variants with Glycosaminoglycans Using a Modified Gel Mobility Shift Assay
TLDR
It is shown that all three hepatocyte growth factor/scatter factor variants share identical heparan/dermatan sulfate binding properties and that both glycosaminoglycans occupy the same binding site. Expand
Heparin and heparan sulfate bind interleukin-10 and modulate its activity.
TLDR
The hypothesis that soluble and cell-surface GAG and, in particular, their sulfate groups are important in binding and modulation of hIL-10 activity is supported. Expand
Molecular recognition and modulation of hepatocyte growth factor activity by heparan and dermatan sulfates
Introduction  Hepatocyte growth factor/scatter factor (HGF/SF) is an unusual growth factor in that it binds both heparan sulfate (HS) ( Lyon et al. 1994 ) and dermatan sulfate (DS) ( Lyon et al. 1998Expand
Differential binding of platelet-derived growth factor isoforms to glycosaminoglycans
TLDR
It is shown that certain PDGF isoforms bind in a specific manner to glycosaminoglycans (GAGs), and PDGF activity at the cell surface may depend on the expression of various cellular GAG species. Expand
Glycosaminoglycan affinity of the complete fibroblast growth factor family.
TLDR
The interactions between FGFs and GAGs thus appear to be more diverse than previously understood, as the differential interactions of these growth factors with G AGs may be key determinants of their specific biological activities. Expand
Interaction of chondroitin sulfate and dermatan sulfate from various biological sources with heparin-binding growth factors and cytokines
TLDR
Analysis of the binding of CS and DS with a number of heparin-binding neurotrophic factors/cytokines using surface plasmon resonance (SPR) and structurally characterized the chains suggest that even low sulfated CS and/or DS chains may contain binding domains, which include fine sugar sequences with specific sulfation patterns, and that sugar sequences, conformations and electrostatic potential are more important than the simple degree of sulfation represented by disaccharide composition. Expand
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