The DOI matches its Crossref record; 67 of the 69 references it cites were found in a registry or an index.
Human and Murine ApoE Markedly Alters Aβ Metabolism before and after Plaque Formation in a Mouse Model of Alzheimer's Disease
Open accessAbstract
The epsilon4 allele of apolipoprotein E (apoE) is a risk factor for Alzheimer's disease (AD), perhaps through effects on amyloid-beta (Abeta) metabolism. Detailed analyses of various Abeta parameters in aging APP(V717F+/-) transgenic mice expressing mouse apoE, no apoE, or human apoE2, apoE3, or apoE4 demonstrate that apoE facilitates, but is not required for, Abeta fibril formation in vivo. Human apoE isoforms markedly delayed Abeta deposition relative to mouse apoE, with apoE2 (and apoE3 to a lesser extent) having a prolonged ability to prevent Abeta from converting into fibrillar forms. Isoform-specific effects of human apoE on Abeta levels and neuritic plaque formation mimicked that observed in AD (E4 > E3 > E2). Importantly, observation of an apoE-dependent decrease in percent soluble Abeta and enrichment of Abeta in membrane microdomains prior to Abeta deposition indicates that apoE influences Abeta metabolism early in the amyloidogenic process and provides a possible novel mechanism by which apoE affects AD pathogenesis.
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In the citing paper
“we and others have reported human apoE isoform-dependent differences in amyloid plaque deposition in APP-transgenic mice (E4 > E3 > E2) (10-14).”
From Human ApoE isoforms differentially regulate brain amyloid-β peptide clearance (2011) · cites this paper as [11]
In the citing paper
“However, mAPOE has been shown to have different effects on Aβ plaque metabolism and formation compared to human APOE [104, 105].”
From APOE Christchurch enhances a disease-associated microglial response to plaque but suppresses response to tau pathology (2025) · cites this paper as [104]
In the citing paper
“The loss in binding is thought to contribute to a decrease in the clearance of Aβ and thus is part of the mechanism for the increased risk of apoE ɛ4 allele carriers to develop AD [13–15].”
From Discovery of a Missense Mutation (Q222K) of the APOE Gene from the Australian Imaging, Biomarker and Lifestyle Study (2023) · cites this paper as [13]
In the citing paper
“In several different Aβ plaque-depositing mice that are genetically engineered to express the human APOE isoforms instead of mouse APOE (Box 3), APOE4 induces greater Aβ fibrillization and deposition in compact plaques relative to APOE3, whereas APOE2 markedly delays the onset and decreases the extent of Aβ plaque deposition117–120.”
From Multifaceted roles of APOE in Alzheimer disease (2024) · cites this paper as [117]
In the citing paper
“Apoe knockout plaque-depositing mice highlight the complexity of the APOE–Aβ interaction, as these mice still exhibit deposition of Aβ plaques, but the plaques are less compact and do not cause the synaptic and cognitive deficits typical of plaque-depositing mice with Apoe intact117,119,122.”
From Multifaceted roles of APOE in Alzheimer disease (2024) · cites this paper as [117]
In the citing paper
“This process is likely to explain why both Apoe knockout and Trem2 knockout plaque-depositing mice exhibit reduced microglial reactivity against Aβ plaques and their plaques are less compact117,119,122,155.”
From Multifaceted roles of APOE in Alzheimer disease (2024) · cites this paper as [117]
In the citing paper
“APOE4-targeted replacement mice, expressing the human APOE4 allele instead of the mouse Apoe, crossed with different AD mouse models such as PDAPP, APP/ PS1ΔE9 and 5xFAD, accelerated plaque formation compared to APOE3-targeted replacement mice (Bales et al, 2009; Castellano et al, 2011; Fagan et al, 2002; Holtzman et al, 2000a; Rodriguez et al, 2014; Youmans et al, 2012).”
From APOE from astrocytes restores Alzheimer’s Aβ-pathology and DAM-like responses in APOE deficient microglia (2024) · cites this paper as Fagan et al, 2002
In the citing paper
“In general, experiments suggest the order of APOE4 > APOE3 > APOE2 for effects on amyloid deposition (Fagan et al, 2002; Castellano et al, 2011; Hudry et al, 2013; Zhao et al, 2016)”
From APOE from astrocytes restores Alzheimer’s Aβ-pathology and DAM-like responses in APOE deficient microglia (2024) · cites this paper as Fagan et al, 2002
In the citing paper
“Interestingly, the human apoE transgenic mice display an isoform-specific pattern of Aβ deposition in the hippocampus, with apoE4 mice having increased levels of Aβ deposits and more thioflavine-S positive plaques than apoE3 mice (Fagan et al., 2002; Holtzman et al., 2000).”
From The role of apolipoprotein E in Alzheimer's disease (2009) · cites this paper as Fagan et al., 2002
In the citing paper
“The expression of human apoE isoform transgenes in PDAPP mice resulted in a marked delay in the deposition of Aβ and formation of neuritic plaques, compared to PDAPP mice expressing murine apoE or no apoE (Fagan et al., 2002; Holtzman et al., 2000; Holtzman et al., 1999).”
From The role of apolipoprotein E in Alzheimer's disease (2009) · cites this paper as Fagan et al., 2002
In the citing paper
“Interestingly, it has been shown that in young PDAPP mice prior to the onset of Aβ deposition, that the lack of apoE may actually increases soluble Aβ levels, a finding that is consistent with cell culture data (Dodart et al., 2002; Fagan et al., 2002).”
From The role of apolipoprotein E in Alzheimer's disease (2009) · cites this paper as Fagan et al., 2002
In the citing paper
“Furthermore, in the PDAPP mouse model, the anatomical pattern of Aβ deposition was markedly different (Fagan et al., 2002; Irizarry et al., 2000).”
From The role of apolipoprotein E in Alzheimer's disease (2009) · cites this paper as Fagan et al., 2002
In the citing paper
“Importantly, m-apoE and h-APP combine in FAD-Tg mice to produce severe Aβ pathology, pathology that is reduced by knocking-out (KO) the m-APOE, further reduced by knocking-in (KI) h-APOE4, and again reduced with h-APOE3-KI (review [79–87]).”
From Inhibition of ACAT as a Therapeutic Target for Alzheimer's Disease Is Independent of ApoE4 Lipidation (2023) · cites this paper as [85]
In the citing paper
“M-apoE and h-apoE differ in both structure [119] and functions ranging from lipid binding and transport, to effects on AD pathology [22, 84, 85, 119, 120].”
From Inhibition of ACAT as a Therapeutic Target for Alzheimer's Disease Is Independent of ApoE4 Lipidation (2023) · cites this paper as [85]
In the citing paper
“Clearly, human apoE isoforms affect A metabolism and deposition differently than murine apoE, but whether this is due to altered clearance and/or structure of A in vivo remains to be determined.”
In the citing paper
“Moreover, a second mechanism by which impaired ApoE4-containing vesicle recycling would be predicted to contribute to accelerated amyloid accumulation and plaque deposition (Fagan et al., 2002) involves the reduced turnover rate of Aβ in the brains of ApoE4 targeted replacement mice (Castellano et al., 2011) and humans (Wildsmith et al., 2012).”
From Reversal of ApoE4-induced recycling block as a novel prevention approach for Alzheimer’s disease (2018) · cites this paper as Fagan et al., 2002
In the citing paper
“Our data are consistent with previous findings by the Holtzman group (Fagan et al., 2002) that showed that mouse ApoE promotes plaque deposition more potently than human ApoE4.”
From NHE6 depletion corrects ApoE4-mediated synaptic impairments and reduces amyloid plaque load (2021) · cites this paper as Fagan et al., 2002
In the citing paper
“To date, substantial evidence has demonstrated ApoE affects amyloid-β deposition in a dosage and isoform-specific fashion (ApoE4>ApoE3>ApoE2)96–100”
From Interplay between innate immunity and Alzheimer disease: APOE and TREM2 in the spotlight (2018) · cites this paper as [99]
In the citing paper
“Compared with other ApoE isoforms, ApoE4 exacerbates the deposition of amyloid plaques in the brain98–100.”
From Interplay between innate immunity and Alzheimer disease: APOE and TREM2 in the spotlight (2018) · cites this paper as [99]
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Metadata
- Authors
- Fagan, A. M., Watson, M., Parsadanian, M., Bales, K. R., Paul, S. M., & Holtzman, D. M.
- Affiliations
- Washington University in St. Louis (US)
- Eli Lilly (United States) (US)
- Venue
- Neurobiology of Disease
- Publisher
- Elsevier BV
- Published
- 2002-04
- Volume
- 9
- Issue
- 3
- Pages
- 305-318
- ISSN
- 0969-9961 (ISSN-L)
- OpenAlex
- W1991607389
- Cited by
- 290
- References
- 69
- Citations by year
- 2026: 4 · 2025: 15 · 2024: 22 · 2023: 4 · 2022: 15 · 2021: 7 · 2020: 15 · 2019: 14 · 2018: 6 · 2017: 8 · 2016: 8 · 2015: 9 · 2014: 8 · 2013: 6 · 2012: 13
- FWCI
- 10.81
- Type
- journal article
- Language
- en
- Open access
- green
- doaj.org
- Licence
- Locations
- Neurobiology of Disease (publishedVersion)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institute on Aging (AG11355, AG00861-01, AG05681-16, P50AG005681, AG13956, P01AG011355)
- 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
- apolipoprotein E, Alzheimer's disease, amyloid-beta metabolism, APOE ε4, APOE isoforms, APP transgenic mice, neuritic plaques, soluble amyloid-beta, lipid rafts, APOE2, APOE3
- MeSH terms
- Alzheimer Disease, Animals, Apolipoproteins E, Disease Models, Animal, Hippocampus, Humans, Mice, Transgenic, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Protein Isoforms, Mice, Plaque, Amyloid
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