Hepatocyte growth factor/scatter factor and its interaction with heparan sulphate and dermatan sulphate. (1st April 2003)

• Record Type: Journal Article
• Authors: Catlow, K.; Deakin, J.A.; Delehedde, M.; Fernig, D.G.; Gallagher, J.T.; Pavão, M.S.G.; Lyon, M.
• Is Part Of: Biochemical Society transactions. Volume 31:Number 2(2003)
• Page Start: 352
• Page End: 353
• Publication Date: 2003-04-01
• Subjects: cancer -- dermatan sulphate -- glycosaminoglycan -- heparan sulphate -- hepatocyte growth factor/scatter factor -- proteoglycan; Biochemistry -- Congresses; 572
• DOI: 10.1042/bst0310352
• Languages: English
• ISSNs: 0300-5127

Abstract

Abstract : 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 ( K d ) 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.