APOE Genotype Results in Differential Effects on the Peripheral Clearance of Amyloid-β42 in APOE Knock-in and Knock-out Mice
Open accessAbstract
The epsilon4 allele of apolipoprotein E (APOE) is currently the major genetic risk factor identified for Alzheimer's disease (AD). Previous in vivo data from our laboratory has demonstrated that amyloid-beta (Abeta) is rapidly removed from the plasma by the liver and kidney and that the rate of its clearance is affected by ApoE in C57BL/6J and APOE-/- mice. To expand upon these findings, we assessed the peripheral clearance of human synthetic Abeta42 in APOE epsilon2, epsilon3, and epsilon4 knock-in and APOE knock-out mice injected with lipidated recombinant apoE2, E3, and E4 protein. Our results show that APOE does influence the rate at which the mice are able to clear Abeta42 from their bloodstream. Both APOE epsilon4 mice and APOE knock-out mice treated with lipidated recombinant apoE4 demonstrated increased retention of plasma Abeta42 over time compared to APOE epsilon2/APOE knock-out rE2 and APOE epsilon3/APOE knock-out rE3 mice. These findings suggest that the peripheral clearance of Abeta42 is significantly altered by APOE genotype. Given that APOE epsilon4 is a risk factor for AD, then these novel findings provide some insight into the role of ApoE isoforms on the peripheral clearance of Abeta which may impact on clearance from the brain.
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APOE facilitates Aβ clearance and inhibits its aggregation through the formation of APOE-Aβ complexes, with APOE3-Aβ complexes being approximately 20 times more prevalent than APOE4-Aβ complexes.
“Moreover, APOE facilitates Aβ clearance and inhibits its aggregation through the formation of APOE-Aβ complexes, with APOE3-Aβ complexes being approximately 20 times more prevalent than APOE4-Aβ complexes [11, 12].”
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 [12]
The Discussion reports that ApoE supports peripheral Aβ clearance and that lipidated ApoE3 binds Aβ with 20-fold greater affinity than ApoE4. It says this binding may prevent conversion to neurotoxic species, but does not establish inhibition of aggregation or that ApoE3–Aβ complexes are 20 times more prevalent. (LLM, conf=0.88)
Experimental — accuracy not yet measuredAPOE modulates APP metabolism in an isoform-dependent manner through distinct mechanisms, including influencing APP processing via effects on lipid metabolism and modulating Aβ clearance and aggregation via the formation of APOE-Aβ complexes.
“APOE modulates APP metabolism in an isoform-dependent manner through distinct mechanisms: 1) influencing APP processing via effects on lipid metabolism [8–10], and 2) modulating Aβ clearance and aggregation via the formation of APOE-Aβ complexes [11, 12].”
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 [12]
The Introduction and Discussion (page unavailable) describe isoform-specific ApoE–Aβ binding and report reduced peripheral Aβ42 clearance with ApoE4 in mice. The Discussion suggests that stronger binding by ApoE2 and ApoE3 may prevent conversion of Aβ into neurotoxic species, but does not establish an effect on Aβ aggregation. The APP-processing clause is attached to other citations and is not judged here. (LLM, conf=0.83)
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- Authors
- Sharman, M. J., Morici, M., Hone, E., Berger, T., Taddei, K., Martins, I. J., Lim, W. L. F., Singh, S., Wenk, M. R., Ghiso, J., Buxbaum, J. D., Gandy, S., & Martins, R. N.
- Affiliations
- Edith Cowan University (AU)
- The University of Western Australia (AU)
- National University of Singapore (SG)
- New York University (US)
- Icahn School of Medicine at Mount Sinai (US)
- Corresponding author
- Martins, Ralph N.
- ORCID
- Venue
- Journal of Alzheimer's Disease
- Publisher
- SAGE Publications
- Published
- 2010-08-11
- Volume
- 21
- Issue
- 2
- Pages
- 403-409
- ISSN
- 1387-2877 (ISSN-L)
- 1875-8908
- PMC
- PMC3292909
- OpenAlex
- W1882000658
- Cited by
- 54
- References
- 19
- Citations by year
- 2025: 1 · 2024: 4 · 2023: 3 · 2022: 3 · 2021: 3 · 2020: 5 · 2019: 3 · 2018: 2 · 2017: 3 · 2016: 1 · 2015: 2 · 2014: 6 · 2013: 7 · 2012: 3
- FWCI
- 3.89
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Journal of Alzheimer s Disease (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- eCite Digital Repository (University of Tasmania) (submittedVersion)
- UWA Profiles and Research Repository (UWA) (submittedVersion)
- Research Online (Edith Cowan University) (submittedVersion)
- Figshare (submittedVersion)
- Funders
- National Institute on Aging (P01AG010491, AG10491)
- 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
- apolipoprotein E, APOE ε4
- MeSH terms
- Alzheimer Disease, Animals, Brain, Genotype, Humans, Mice, Inbred C57BL, Peptide Fragments, Recombinant Proteins, Tissue Distribution, Amyloid beta-Peptides, Mice, Knockout, Mice, Apolipoprotein E3, Apolipoprotein E4, Apolipoprotein E2, Gene Knock-In Techniques, Mice, 129 Strain
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