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Cited by 36Alzheimer's disease research and treatmentsCholesterol and Lipid MetabolismLipoproteins and Cardiovascular Health

Self-Assembly of HEK Cell-Secreted ApoE Particles Resembles ApoE Enrichment of Lipoproteins as a Ligand for the LDL Receptor-Related Protein

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LaDu, Mary Jo, Stine,, W. Blaine, Narita, Masaaki, Getz, Godfrey S., Reardon, Catherine A., Bu, Guojun·2006·Biochemistry
DOI 10.1021/bi051765sPMC PMC2564845
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Abstract

Recent studies have shown that the lipidation and assembly state of apolipoprotein E (apoE) determine receptor recognition and amyloid-beta peptide (Abeta) binding. We previously demonstrated that apoE secreted by HEK cells stably expressing apoE3 or apoE4 (HEK-apoE) binds Abeta and inhibits Abeta-induced neurotoxicity by an isoform-specific process that requires apoE receptors. Here we characterized the structure of HEK-apoE assemblies and determined their receptor binding specificity. By chromatography, HEK-apoE elutes in high molecular mass fractions and is the size of plasma HDL, consistent with a multiprotein assembly. No lipid was associated with these apoE assemblies. Several methods for analyzing receptor binding indicate that HEK-apoE is a ligand for low-density lipoprotein (LDL) receptor-related protein (LRP) but not the LDL receptor. This suggests that self-assembly of apoE may induce a functional conformation necessary for binding to LRP. Our results indicate that, in addition to lipid content, the assembly state of apoE influences Abeta binding and receptor recognition.

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  • The HEK293 expression system does not fully recapitulate the lipidation state or post-translational modifications of ApoE in primary astrocytes or neurons.

    “Third, the HEK293 expression system does not fully recapitulate the lipidation state or post-translational modifications of ApoE in primary astrocytes or neurons”

    From APOE Isoform-Dependent Self-Association Measured by a Split-Luciferase Complementation Assay: Differential Effects of Disease-Risk and Protective Variants (2026) · cites this paper as [13]

    The lipid-analysis passage (page not provided) reports no detectable lipid in HEK-secreted ApoE, unlike astrocyte-secreted lipoproteins, which contain phospholipid and cholesterol. This supports the lipidation comparison, but the paper does not establish a corresponding difference in post-translational modifications or compare HEK-secreted ApoE with neuron-secreted ApoE on either measure. (LLM, conf=0.88)

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Cited by

Sorted by citations

Authors
LaDu, M. J., Stine, Narita, M., Getz, G. S., Reardon, C. A., & Bu, G.
Affiliations
Washington University in St. Louis (US)
ORCID
Venue
Biochemistry
Publisher
American Chemical Society (ACS)
Published
2005-12-17
Volume
45
Issue
2
Pages
381-390
ISSN
  • 0006-2960 (ISSN-L)
  • 1520-4995
DOI
10.1021/bi051765s
PMC
PMC2564845
OpenAlex
W2140205792
Cited by
36
References
8
Citations by year
2026: 2 · 2025: 2 · 2023: 3 · 2021: 1 · 2020: 1 · 2019: 1 · 2018: 2 · 2017: 3 · 2016: 1 · 2015: 1 · 2014: 1 · 2013: 2 · 2012: 2
FWCI
1.51
Type
journal article
Language
en
Open access
Locations
  • Biochemistry (publishedVersion)
  • PubMed (publishedVersion)
  • PubMed Central (acceptedVersion)
  • Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
Funders
  • Gladstone Institutes
  • National Institute on Aging (R01AG027924, R01AG019121, AG 19121)
  • National Institute of Diabetes and Digestive and Kidney Diseases (R01DK061761)
  • National Institute of Neurological Disorders and Stroke (NS520138, NS 37525, R01NS037525)
Topics
  • Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
  • Health Sciences › Medicine › Surgery › Cholesterol and Lipid Metabolism
  • Health Sciences › Medicine › Surgery › Lipoproteins and Cardiovascular Health
Keywords
apolipoprotein E, APOE3, APOE ε4, amyloid-beta binding, LDL receptor-related protein, LDL receptor, APOE isoforms, amyloid-beta toxicity
MeSH terms
Animals, Apolipoproteins E, Cell Line, Chromatography, Gel, Fibroblasts, Humans, Iodine Radioisotopes, Ligands, Protein Binding, Receptors, LDL, Ultracentrifugation, Low Density Lipoprotein Receptor-Related Protein-1, Mice, Apolipoprotein E3, Apolipoprotein E4

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