Hepatocyte growth factor/scatter factor and its interaction with heparan sulphate and dermatan sulphate.

2.50
Hdl Handle:
http://hdl.handle.net/10541/82414
Title:
Hepatocyte growth factor/scatter factor and its interaction with heparan sulphate and dermatan sulphate.
Authors:
Catlow, Krista R; Deakin, Jon A; Delehedde, Maryse; Fernig, D G; Gallagher, John T; Pavão, M S G; Lyon, Malcolm
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.
Affiliation:
Cancer Research UK and University of Manchester Department of Medical Oncology, Christie Hospital NHS Trust, Manchester, U.K. KCatlow@PICR.man.ac.uk
Citation:
Hepatocyte growth factor/scatter factor and its interaction with heparan sulphate and dermatan sulphate. 2003, 31 (2):352-3 Biochem. Soc. Trans.
Journal:
Biochemical Society Transactions
Issue Date:
Apr-2003
URI:
http://hdl.handle.net/10541/82414
PubMed ID:
12653636
Type:
Article
Language:
en
ISSN:
0300-5127
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorCatlow, Krista R-
dc.contributor.authorDeakin, Jon A-
dc.contributor.authorDelehedde, Maryse-
dc.contributor.authorFernig, D G-
dc.contributor.authorGallagher, John T-
dc.contributor.authorPavão, M S G-
dc.contributor.authorLyon, Malcolm-
dc.date.accessioned2009-09-23T15:34:08Z-
dc.date.available2009-09-23T15:34:08Z-
dc.date.issued2003-04-
dc.identifier.citationHepatocyte growth factor/scatter factor and its interaction with heparan sulphate and dermatan sulphate. 2003, 31 (2):352-3 Biochem. Soc. Trans.en
dc.identifier.issn0300-5127-
dc.identifier.pmid12653636-
dc.identifier.urihttp://hdl.handle.net/10541/82414-
dc.description.abstractHepatocyte 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.en
dc.language.isoenen
dc.subject.meshAnimals-
dc.subject.meshDermatan Sulfate-
dc.subject.meshHeparitin Sulfate-
dc.subject.meshHepatocyte Growth Factor-
dc.subject.meshHumans-
dc.subject.meshKinetics-
dc.subject.meshProtein Binding-
dc.subject.meshSignal Transduction-
dc.titleHepatocyte growth factor/scatter factor and its interaction with heparan sulphate and dermatan sulphate.en
dc.typeArticleen
dc.contributor.departmentCancer Research UK and University of Manchester Department of Medical Oncology, Christie Hospital NHS Trust, Manchester, U.K. KCatlow@PICR.man.ac.uken
dc.identifier.journalBiochemical Society Transactionsen

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