Cited by 268Alzheimer's disease research and treatmentsDementia and Cognitive Impairment ResearchNeuroinflammation and Neurodegeneration Mechanisms

The DOI matches its Crossref record; 95 of the 95 references it cites were found in a registry or an index; 28 of the 38 sources its claims cite were checked for support.

APOE4-specific Changes in Aβ Accumulation in a New Transgenic Mouse Model of Alzheimer Disease

Open access

Abstract

APOE4 is the greatest risk factor for Alzheimer disease (AD) and synergistic effects with amyloid-β peptide (Aβ) suggest interactions among apoE isoforms and different forms of Aβ accumulation. However, it remains unclear how the APOE genotype affects plaque morphology, intraneuronal Aβ, soluble Aβ42, and oligomeric Aβ (oAβ), particularly in vivo. As the introduction of human APOE significantly delays amyloid deposition in transgenic mice expressing familial AD (FAD) mutations (FAD-Tg), 5xFAD-Tg mice, which exhibit amyloid deposition by age 2 months, were crossed with apoE-targeted replacement mice to produce the new EFAD-Tg mice. Compared with 5xFAD mice, Aβ deposition was delayed by ∼4 months in the EFAD mice, allowing detection of early changes in Aβ accumulation from 2-6 months. Although plaque deposition is generally greater in E4FAD mice, E2/E3FAD mice have significantly more diffuse and E4FAD more compact plaques. As a first report in FAD-Tg mice, the APOE genotypes had no effect on intraneuronal Aβ accumulation in EFAD mice. In E4FAD mice, total apoE levels were lower and total Aβ levels higher than in E2FAD and E3FAD mice. Profiles from sequential three-step extractions (TBS, detergent, and formic acid) demonstrated that the lower level of total apoE4 is reflected only in the detergent-soluble fraction, indicating that less apoE4 is lipoprotein-associated, and perhaps less lipidated, compared with apoE2 and apoE3. Soluble Aβ42 and oAβ levels were highest in E4FAD mice, although soluble apoE2, apoE3, and apoE4 levels were comparable, suggesting that the differences in soluble Aβ42 and oAβ result from functional differences among the apoE isoforms. Thus, APOE differentially regulates multiple aspects of Aβ accumulation.

Overview

AI snapshot

Written from the paper’s full text.

TL;DR

A new EFAD mouse model (5xFAD crossed with human APOE-targeted replacement mice) delays Aβ deposition by ~4 months versus 5xFAD, creating a 2–6-month window to compare APOE genotypes. APOE4 uniquely increases compact plaques, total/soluble Aβ42, and oligomeric Aβ, while total apoE4 is lower and less lipoprotein-associated, but intraneuronal Aβ is comparable across APOE genotypes.

Key findings

  • Aβ deposition was delayed ~4 months in EFAD versus 5xFAD mice; plaque deposition was generally greatest in E4FAD, significant at 4 months in frontal cortex and subiculum and at 6 months in frontal cortex. At 6 months in subiculum, E2FAD and E4FAD plaque levels were both significantly higher than E3FAD.
  • Plaque morphology differed by APOE genotype: E2FAD and E3FAD had mostly diffuse plaques (>50%), whereas diffuse plaques were significantly lower in E4FAD (~30% at 6 months); compact plaques were ~20% in E2FAD/E3FAD but 40–50% in E4FAD.
  • Intraneuronal Aβ increased with age and varied by brain region but showed no significant APOE genotype-specific differences in frontal cortex, subiculum, or CA3.
  • Total apoE4 was lower than apoE2/apoE3, reflected only in the TBSX detergent-soluble fraction, suggesting less apoE4 is lipoprotein-associated. Total Aβ42 was higher in E4FAD; soluble Aβ42 was 2-fold higher in cortex and 3-fold higher in hippocampus, and oligomeric Aβ was ~2-fold higher in cortex and 3-fold higher in hippocampus in E4FAD versus E2FAD/E3FAD. At 6 months, TBS-soluble and FA-extracted Aβ42 in E4FAD were at least 4-fold higher than in E2FAD or E3FAD.

Methods

  • EFAD mice were generated by crossing 5xFAD mice carrying five FAD mutations with homozygous human APOE2-, APOE3-, or APOE4-targeted replacement mice; male mice were used at 2, 4, and 6 months.
  • Brains were analyzed by immunohistochemistry with MOAB-2 and NeuN, Thioflavin S plaque staining and morphology quantification, unbiased stereology for intraneuronal Aβ, three-step sequential extraction (TBS, TBSX, formic acid), and ELISAs for apoE, Aβ42, and oligomeric Aβ; APP levels were checked by Western blot.
  • Data were analyzed by one-way or two-way ANOVA with Tukey’s or Bonferroni’s post hoc tests; p < 0.05 was considered significant.

Limitations

  • The paper states that female mice were excluded from this initial study for consistency because apoE isoform-specific interactions with Aβ are known to be influenced by gender.
  • The paper notes that the 2–6-month window is still early in the overall process of Aβ accumulation and that drug intervention trials have not yet been performed in EFAD mice.
  • Evident from the text: the study is limited to male mice, does not report cognitive/behavioral outcomes, and focuses on correlative biochemical and histological changes rather than establishing causal mechanisms.

Model-written summary. Check it against the paper before relying on it.

Integrity signals

Registry

Crossref · 10.1074/jbc.m112.407957

Cites

95 of 95 references verified0 citation errors · 0 not checkable

Statistics

Nothing to recompute.

Verification

Claims the paper makes

28 of 38 cited sources checked · 19 supported · 0 flagged · accuracy not yet measured

  • It may state two separate claims as one. 34
  • Probably not a substantial claim. 18
49 of 49
  • The paper relies on this without support.

    Human apoE in apoE-TR mice is expressed primarily by glia at physiologically regulated levels.

    “ApoE-TR mice are perhaps the most biologically relevant transgenic mouse model for apoE, as human apoE is expressed primarily by glia at physiologically regulated levels.”
  • The paper relies on this without support.

    APOE4 is the greatest risk factor for Alzheimer disease.

    “APOE4 is the greatest risk factor for Alzheimer disease (AD)”
  • The paper relies on this without support.

    It is unclear how the APOE genotype affects plaque morphology, intraneuronal Aβ, soluble Aβ42, and oligomeric Aβ (oAβ), particularly in vivo.

    “However, it remains unclear how the APOE genotype affects plaque morphology, intraneuronal A␤, soluble A␤42, and oligomeric A␤ (oA␤), particularly in vivo.”
  • The paper relies on this without support.

    No studies have yet reported the effect of APOE genotype on intraneuronal Aβ accumulation in an apoE/FAD-Tg mouse.

    “To our knowledge, no studies have yet reported the effect of APOE genotype on intraneuronal A␤ accumulation in an apoE/ FAD-Tg mouse.”
  • The paper relies on this without support.

    Introduction of human APOE significantly delays amyloid deposition in transgenic mice expressing familial AD (FAD) mutations.

    “As the introduction of human APOE significantly delays amyloid deposition in transgenic mice expressing familial AD (FAD) mutations (FAD-Tg)”
  • The paper relies on this without support.

    Intraneuronal Aβ has been correlated with cognitive deficits in FAD-Tg mice.

    “Indeed, intraneuronal A␤ has been correlated with cognitive deficits in FAD-Tg mice.”
6 of 6

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Cited works that were retracted

Works this paper cites that were later retracted, from the retraction notices publishers deposit. Major when the notice came out before this paper was published.

  • Cites a retracted work: 10.1523/jneurosci.6637-10.2011

    Info

    The cited work was retracted on 2015-02-25 (notice 10.1523/jneurosci.5236-14.2015), not before this paper was published (2012-12).

    Cited work 10.1523/jneurosci.6637-10.2011 · retracted 2015-02-25 · notice 10.1523/jneurosci.5236-14.2015 · this paper published 2012-12

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Metadata

Authors
Youmans, K. L., Tai, L. M., Nwabuisi-Heath, E., Jungbauer, L., Kanekiyo, T., Gan, M., Kim, J., Eimer, W. A., Estus, S., Rebeck, G. W., Weeber, E. J., Bu, G., Yu, C., & LaDu, M. J.
Affiliations
  • University of Illinois Chicago (US)
  • Mayo Clinic in Florida (US)
  • Washington University in St. Louis (US)
  • Northwestern University (US)
  • University of Kentucky (US)
  • Georgetown University (US)
  • University of South Florida (US)
Corresponding author
LaDu, Mary Jo
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
2012-12
Volume
287
Issue
50
Pages
41774-41786
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2168481427
Cited by
268
References
93
Citations by year
2026: 7 · 2025: 18 · 2024: 28 · 2023: 21 · 2022: 25 · 2021: 23 · 2020: 25 · 2019: 23 · 2018: 16 · 2017: 18 · 2016: 19 · 2015: 18 · 2014: 15 · 2013: 12
FWCI
4.86
Type
journal article
Language
en
Open access
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
  • Figshare (submittedVersion)
  • Rare & Special e-Zone (The Hong Kong University of Science and Technology) (submittedVersion)
Funders
  • Alzheimer's Association (P01AG030128-03S1, ZEN-08-899000, UL1RR029879)
  • National Institutes of Health
  • University of Illinois at Urbana-Champaign
  • National Institute on Aging (P01AG030128, R01AG027924, R01AG035379, R01AG035355, T32AG036697)
  • National Institute of Neurological Disorders and Stroke (P01NS074969)
  • National Center for Research Resources (UL1RR029879)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
  • Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
  • Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
Keywords
APOE ε4, Alzheimer's disease, amyloid-beta deposition, APOE isoforms, 5xFAD mice, amyloid plaques, intraneuronal amyloid-beta, amyloid-beta oligomers, familial Alzheimer's disease
MeSH terms
Alzheimer Disease, Animals, Disease Models, Animal, Genotype, Humans, Mice, Transgenic, Mutation, Amyloid beta-Peptides, Protein Isoforms, Mice, Apolipoprotein E4

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