Invited Review: APOE at the interface of inflammation, neurodegeneration and pathological protein spread in Alzheimer's disease
Open accessAbstract
Despite more than a century of research, the aetiology of sporadic Alzheimer's disease ( AD ) remains unclear and finding disease modifying treatments for AD presents one of the biggest medical challenges of our time. AD pathology is characterized by deposits of aggregated amyloid beta (Aβ) in amyloid plaques and aggregated tau in neurofibrillary tangles. These aggregates begin in distinct brain regions and spread throughout the brain in stereotypical patterns. Neurodegeneration, comprising loss of synapses and neurons, occurs in brain regions with high tangle pathology, and an inflammatory response of glial cells appears in brain regions with pathological aggregates. Inheriting an apolipoprotein E ε4 ( APOE 4 ) allele strongly increases the risk of developing AD for reasons that are not yet entirely clear. Substantial amounts of evidence support a role for APOE in modulating the aggregation and clearance of Aβ, and data have been accumulating recently implicating APOE 4 in exacerbating neurodegeneration, tau pathology and inflammation. We hypothesize that APOE 4 influences all the pathological hallmarks of AD and may sit at the interface between neurodegeneration, inflammation and the spread of pathologies through the brain. Here, we conducted a systematic search of the literature and review evidence supporting a role for APOE 4 in neurodegeneration and inflammation. While there is no direct evidence yet for APOE 4 influencing the spread of pathology, we postulate that this may be found in future based on the literature reviewed here. In conclusion, this review highlights the importance of understanding the role of APOE in multiple important pathological mechanisms in AD .
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APOE isoforms modulate Tau phosphorylation and aggregation in an isoform-dependent manner, with APOE4 particularly associated with increased Tau pathology.
“APOE isoforms have been shown to modulate Tau phosphorylation and aggregation in an isoform-dependent manner, with APOE4 being particularly associated with increased Tau pathology [64].”
From Analysis of early effects of human APOE isoforms on Alzheimer’s disease and type III hyperlipoproteinemia pathways using knock-in rat models with humanized APP and APOE (2024) · cites this paper as [64]
The Results section (Mechanisms of APOE-related neurodegeneration; page unavailable) reports that APOE4 fragments exacerbate tau pathology and that APOE fragments increase tau phosphorylation. It does not establish that different APOE isoforms modulate tau aggregation in an isoform-dependent manner; its isoform comparison concerns tau-mediated neurodegeneration, not aggregation. (LLM, conf=0.86)
Experimental — accuracy not yet measuredThe interaction between APOE4 and Aβ has now been established as one of the mechanisms by which the APOEε4 allele increases Alzheimer disease risk.
“The link between APOE4 and Aβ has been studied extensively for the past three decades, and the interaction between the two proteins has now been established as one of the mechanisms by which the APOEε4 allele increases AD risk109.”
From Multifaceted roles of APOE in Alzheimer disease (2024) · cites this paper as [109]
The Introduction (page unavailable) says compelling studies show that APOE4 affects Aβ production, clearance and aggregation, supporting an Aβ-related contribution to Alzheimer disease risk. But it also says the exact mechanisms remain unresolved; the Mechanisms of APOE-related neurodegeneration section describes specific protein interactions as suggested rather than established. The claim overstates that certainty. (LLM, conf=0.84)
Experimental — accuracy not yet measuredAPOE4 is associated with increased Aβ deposition, and the mechanism behind this is multifaceted.
“APOE4 is associated with increased Aβ deposition, and the mechanism behind this is multifaceted.”
From Multifaceted roles of APOE in Alzheimer disease (2024) · cites this paper as [109]
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Alzheimer’s Disease: Key Insights from Two Decades of Clinical Trial Failures
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Multifaceted roles of APOE in Alzheimer disease
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“APOE isoforms have been shown to modulate Tau phosphorylation and aggregation in an isoform-dependent manner, with APOE4 being particularly associated with increased Tau pathology [64].”
Background
- Authors
- Tzioras, M., Davies, C., Newman, A., Jackson, R., & Spires‐Jones, T.
- Affiliations
- UK Dementia Research Institute (GB)
- Harvard University (US)
- Corresponding author
- Spires‐Jones, T.
- Venue
- Neuropathology and Applied Neurobiology
- Publisher
- Wiley
- Published
- 2018-11-28
- Volume
- 45
- Issue
- 4
- Pages
- 327-346
- ISSN
- 0305-1846 (ISSN-L)
- 1365-2990
- PMC
- PMC6563457
- OpenAlex
- W2900302187
- Cited by
- 147
- References
- 144
- Citations by year
- 2026: 16 · 2025: 19 · 2024: 13 · 2023: 22 · 2022: 22 · 2021: 21 · 2020: 20 · 2019: 13 · 2018: 1
- FWCI
- 1.81
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Neuropathology and Applied Neurobiology (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Discovery Research Portal (University of Dundee) (submittedVersion)
- Edinburgh Research Explorer (University of Edinburgh) (submittedVersion, other-oa)
- Funders
- Medical Research Council
- Alzheimer’s Research UK
- Wellcome Trust
- Alzheimer's Society
- Topics
- Health Sciences › Medicine › Physiology › 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, neuroinflammation, neurodegeneration, amyloid-beta, tau pathology, amyloid plaques, neurofibrillary tangles, glial cells, amyloid clearance
- MeSH terms
- Alzheimer Disease, Brain, Inflammation, Amyloid beta-Peptides, Neurofibrillary Tangles, Plaque, Amyloid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
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