Reference : beta-amyloid peptide interacts specifically with the carboxy-terminal domain of human...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
beta-amyloid peptide interacts specifically with the carboxy-terminal domain of human apolipoprotein E: Relevance to Alzheimer's disease
Pillot, T. [> > > >]
Goethals, M. [> > > >]
Najib, J. [> > > >]
Labeur, C. [> > > >]
Lins, Laurence mailto [Université de Liège - ULg > > Gembloux Agro-Bio Tech >]
Chambaz, J. [> > > >]
Brasseur, Robert mailto [Université de Liège - ULg > > Gembloux Agro-Bio Tech >]
Vandekerckhove, J. [> > > >]
Rosseneu, M. [> > > >]
Journal of Neurochemistry
Yes (verified by ORBi)
[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.
Researchers ; Professionals

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