Hepatocyte growth factor (HGF)/scatter factor (SF) is a unique growth factor, in that it binds both heparan sulphate (HS) and dermatan sulphate (DS). The sequences in HS and DS that specifically interact with and modulate HGF/SF activity have not yet been fully identified. Ascidian DS, which uniquely possesses O-sulphation at C-6 (and not C-4) of its N-acetylgalactosamine unit, was analysed for HGF/SF-binding activity in the biosensor. The kinetic analysis revealed a strong, biologically relevant interaction with an equilibrium dissociation constant (Kd) of approx. 1 nM. An Erk activation assay also demonstrated stimulation of the MAP kinase pathway downstream of the Met receptor following addition of both HGF/SF and ascidian DS to the glycosaminoglycan-deficient CHO-745 mutant cell line. Furthermore, the activation of Met and the MAP kinase pathway by HGF/SF and ascidian DS leads to a cellular response in the form of migration.
Hepatocyte growth factor/scatter factor and its interaction with heparan sulphate and dermatan sulphate
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K. Catlow, J.A. Deakin, M. Delehedde, D.G. Fernig, J.T. Gallagher, M.S.G. Pavão, M. Lyon; Hepatocyte growth factor/scatter factor and its interaction with heparan sulphate and dermatan sulphate. Biochem Soc Trans 1 April 2003; 31 (2): 352–353. doi: https://doi.org/10.1042/bst0310352
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