A flow cytometry–based in vitro assay reveals that formation of apolipoprotein E (ApoE)–amyloid beta complexes depends on ApoE isoform and cell type
Open accessAbstract
Apolipoprotein E (ApoE) is a secreted apolipoprotein with three isoforms, E2, E3, and E4, that binds to lipids and facilitates their transport in the extracellular environment of the brain and the periphery. The E4 allele is a major genetic risk factor for the sporadic form of Alzheimer's disease (AD), and studies of human brain and mouse models have revealed that E4 significantly exacerbates the deposition of amyloid beta (Aβ). It has been suggested that this deposition could be attributed to the formation of soluble ApoE isoform-specific ApoE-Aβ complexes. However, previous studies have reported conflicting results regarding the directionality and strength of those interactions. In this study, using a series of flow cytometry assays that maintain the physiological integrity of ApoE-Aβ complexes, we systematically assessed the association of Aβ with ApoE2, E3, or E4. We used ApoE secreted from HEK cells or astrocytes overexpressing ApoE fused with a GFP tag. As a source of soluble Aβ peptide, we used synthetic Aβ40 or Aβ42 or physiological Aβ secreted from CHO cell lines overexpressing WT or V717F variant amyloid precursor protein (APP). We observed significant interactions between the different ApoE isoforms and Aβ, with E4 interacting with Aβ more strongly than the E2 and E3 isoforms. We also found subtle differences depending on the Aβ type and the ApoE-producing cell type. In conclusion, these results indicate that the strength of the ApoE-Aβ association depends on the source of Aβ or ApoE.
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The single amino acid changes in the different APOE isoforms result in slightly different structures, which have a strikingly large effect on the binding affinities of APOE to lipids, Aβ and receptors.
“The single amino acid changes in the different APOE isoforms result in slightly different structures, which have a strikingly large effect on the binding affinities of APOE to lipids, Aβ and receptors99,111,116,140.”
From Multifaceted roles of APOE in Alzheimer disease (2024) · cites this paper as [116]
The Discussion (p. 13252) reports that ApoE4 has a more closed conformation and is more lipidated than ApoE2 and ApoE3, and the paper finds isoform-dependent ApoE–Aβ association. It does not establish that single amino acid changes cause these differences, or show a strikingly large effect on binding affinities to lipids and receptors; its proposed structural explanation for Aβ binding is explicitly tentative. (LLM, conf=0.88)
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- Authors
- Kara, E., Marks, J. D., Roe, A. D., Commins, C., Fan, Z., Calvo-Rodriguez, M., Wegmann, S., Hudry, E., & Hyman, B. T.
- Affiliations
- Harvard University (US)
- Corresponding author
- Hyman, Bradley T.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2018-08
- Volume
- 293
- Issue
- 34
- Pages
- 13247-13256
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC6109911
- OpenAlex
- W2811460956
- Cited by
- 20
- References
- 48
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 2 · 2023: 2 · 2022: 3 · 2021: 2 · 2020: 3 · 2019: 1
- FWCI
- 1.03
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- European Molecular Biology Organization (EMBO) (ATLF-815–2014)
- Marie Curie Actions of the European Commission (LTFCOFUND2013 GA-2013–609409)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- apolipoprotein E, amyloid-beta, APOE isoforms, APOE ε4, Alzheimer's disease, amyloid deposition, Aβ40, amyloid-beta 42, astrocytes, HEK cells, in vitro binding assay
- MeSH terms
- Animals, Astrocytes, Biological Assay, Flow Cytometry, Humans, Male, Mice, Transgenic, Neurons, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Cell Lineage, Protein Isoforms, Mice, Apolipoprotein E3, Apolipoprotein E4, Apolipoprotein E2, HEK293 Cells, In Vitro Techniques
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