ORBi: Pillot T. - beta-amyloid peptide interacts specifically with the carboxy-terminal domain of human apolipoprotein E: Relevance to Alzheimer's disease

Reference : beta-amyloid peptide interacts specifically with the carboxy-terminal domain of human ap...


	Document type :	Scientific journals : Article
	Discipline(s) :	Life sciences : Biochemistry, biophysics & molecular biology
	To cite this reference:	http://hdl.handle.net/2268/63678

Title :	beta-amyloid peptide interacts specifically with the carboxy-terminal domain of human apolipoprotein E: Relevance to Alzheimer's disease
Language :	English
Author, co-author :	Pillot, T. [> > > >]
	Goethals, M. [> > > >]
	Najib, J. [> > > >]
	Labeur, C. [> > > >]
	Lins, Laurence [Université de Liège > > Gembloux Agro-Bio Tech >]
	Chambaz, J. [> > > >]
	Brasseur, Robert [Université de Liège > > Gembloux Agro-Bio Tech >]
	Vandekerckhove, J. [> > > >]
	Rosseneu, M. [> > > >]
Publication date :	1999
Journal title :	Journal of Neurochemistry
Volume :	72
Issue/season :	1
Pages :	230-7
Peer reviewed :	Yes (verified by ORBi)
Audience :	International
ISSN :	0022-3042
Abstract :	[en] Growing evidence indicates the involvement of apolipoprotein E (apoE) in the development of late-onset and sporadic forms of Alzheimer's disease, although its exact role remains unclear. We previously demonstrated that beta-amyloid peptide (Abeta) displays membrane-destabilizing properties and that only apoE2 and E3 isoforms inhibit these properties. In this study, we clearly demonstrate that the carboxy-terminal lipid-binding domain of apoE (e.g., residues 200-299) is responsible for the Abeta-binding activity of apoE and that this interaction involves pairs of apoE amphipathic alpha-helices. We further demonstrate that Abeta is able to inhibit the association of the C-terminal domain of apoE with lipids due to the formation of Abeta/apoE complexes resistant to sodium dodecyl sulfate-polyacrylamide gel electrophoresis. On the contrary, the amino-terminal receptor-binding domain of apoE (e.g., residues 129-169) is not able to form stable complexes with Abeta. These data extend our understanding of human apoE-dependent binding of Abeta by involving the C-terminal domain of apoE in the efficient formation of apoE/Abeta complex.
Target :	Researchers ; Professionals
Permalink :	http://hdl.handle.net/2268/63678

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