β‐Amyloid Peptide Interacts Specifically with the Carboxyl‐Terminal Domain of Human Apolipoprotein E

β‐Amyloid Peptide Interacts Specifically with the Carboxyl‐Terminal Domain of Human... Abstract : 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 β‐amyloid peptide (Aβ) 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 Aβ‐binding activity of apoE and that this interaction involves pairs of apoE amphipathic α‐helices. We further demonstrate that Aβ is able to inhibit the association of the C‐terminal domain of apoE with lipids due to the formation of Aβ/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 Aβ. These data extend our understanding of human apoE‐dependent binding of Aβ by involving the C‐terminal domain of apoE in the efficient formation of apoE/Aβ complex. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Neurochemistry Wiley

β‐Amyloid Peptide Interacts Specifically with the Carboxyl‐Terminal Domain of Human Apolipoprotein E

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Publisher
Wiley Subscription Services, Inc., A Wiley Company
Copyright
© International Society for Neurochemistry
ISSN
0022-3042
eISSN
1471-4159
D.O.I.
10.1046/j.1471-4159.1999.0720230.x
Publisher site
See Article on Publisher Site

Abstract

Abstract : 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 β‐amyloid peptide (Aβ) 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 Aβ‐binding activity of apoE and that this interaction involves pairs of apoE amphipathic α‐helices. We further demonstrate that Aβ is able to inhibit the association of the C‐terminal domain of apoE with lipids due to the formation of Aβ/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 Aβ. These data extend our understanding of human apoE‐dependent binding of Aβ by involving the C‐terminal domain of apoE in the efficient formation of apoE/Aβ complex.

Journal

Journal of NeurochemistryWiley

Published: Jan 1, 1999

Keywords: ; ; ;

References

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