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 Lettjournal_title
FEBS lettersauthors
Hubin E,Verghese PB,van Nuland N,Broersen Kdoi
10.1002/1873-3468.13428subject
Has Abstractpub_date
2019-06-01 00:00:00pages
1144-1153issue
11eissn
0014-5793issn
1873-3468journal_volume
593pub_type
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