Apolipoprotein E associated with reconstituted high-density lipoprotein-like particles is protected from aggregation.

Abstract:

:Apolipoprotein E (APOE) genotype determines Alzheimer's disease (AD) susceptibility, with the APOE ε4 allele being an established risk factor for late-onset AD. The ApoE lipidation status has been reported to impact amyloid-beta (Aβ) peptide metabolism. The details of how lipidation affects ApoE behavior remain to be elucidated. In this study, we prepared lipid-free and lipid-bound ApoE particles, mimicking the high-density lipoprotein particles found in vivo, for all three isoforms (ApoE2, ApoE3, and ApoE4) and biophysically characterized them. We find that lipid-free ApoE in solution has the tendency to aggregate in vitro in an isoform-dependent manner under near-physiological conditions and that aggregation is impeded by lipidation of ApoE.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Hubin E,Verghese PB,van Nuland N,Broersen K

doi

10.1002/1873-3468.13428

subject

Has Abstract

pub_date

2019-06-01 00:00:00

pages

1144-1153

issue

11

eissn

0014-5793

issn

1873-3468

journal_volume

593

pub_type

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