ApoE4 and Aβ Oligomers Reduce BDNF Expression via HDAC Nuclear Translocation
Open accessAbstract
Apolipoprotein E4 (ApoE4) is a major genetic risk factor for several neurodegenerative disorders, including Alzheimer's disease (AD). Epigenetic dysregulation, including aberrations in histone acetylation, is also associated with AD. We show here for the first time that ApoE4 increases nuclear translocation of histone deacetylases (HDACs) in human neurons, thereby reducing BDNF expression, whereas ApoE3 increases histone 3 acetylation and upregulates BDNF expression. Amyloid-β (Aβ) oligomers, which have been implicated in AD, caused effects similar to ApoE4. Blocking low-density lipoprotein receptor-related protein 1 (LRP-1) receptor with receptor-associated protein (RAP) or LRP-1 siRNA abolished the ApoE effects. ApoE3 also induced expression of protein kinase C ε (PKCε) and PKCε retained HDACs in the cytosol. PKCε activation and ApoE3 supplementation prevented ApoE4-mediated BDNF downregulation. PKCε activation also reversed Aβ oligomer- and ApoE4-induced nuclear import of HDACs, preventing the loss in BDNF. ApoE4 induced HDAC6-BDNF promoter IV binding, which reduced BDNF exon IV expression. Nuclear HDAC4 and HDAC6 were more abundant in the hippocampus of ApoE4 transgenic mice than in ApoE3 transgenic mice or wild-type controls. Nuclear translocation of HDA6 was also elevated in the hippocampus of AD patients compared with age-matched controls. These results provide new insight into the cause of synaptic loss that is the most important pathologic correlate of cognitive deficits in AD.
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ApoE4 increased the nuclear translocation of HDACs in human neuroblastomas, thereby reducing brain derived neurotrophic factor expression.
“In another study, ApoE4 increased the nuclear translocation of histone deacetylases (HDACs) in human neuroblastomas, thereby reducing brain derived neurotrophic factor expression [54].”
From Apolipoprotein E metabolism and functions in brain and its role in Alzheimer's disease (2017) · cites this paper as [54]
The Materials section identifies SH-SY5Y cells as human neuroblastoma cells, and the HDAC nuclear-import results report increased nuclear HDAC4 and HDAC6 with ApoE4 plus cholesterol. Figure 7 reports reduced BDNF expression under that treatment. The claim omits a decisive condition: the nuclear-import results state that ApoE4 alone did not change HDAC translocation. Page numbers are not available in our copy. (LLM, conf=0.90)
Experimental — accuracy not yet measuredApoE3 retains HDACs in the cytosol via elevating the expression of protein kinase C ε.
“In contrast, ApoE3 retains HDACs in the cytosol via elevating the expression of protein kinase C ε.”
From Apolipoprotein E metabolism and functions in brain and its role in Alzheimer's disease (2017) · cites this paper as [54]
In “ApoE-mediated HDAC nucleo-cytoplasmic shuttling is regulated by PKCε” (page unavailable), ApoE3 plus cholesterol increased PKCε mRNA, and PKCε knockdown abolished ApoE3-mediated nuclear export of HDAC4 and HDAC6. The claim omits the cholesterol condition: the “ApoE4 induces nuclear import of class II HDACs” section reports no change in HDAC4 or HDAC6 translocation with ApoE3 alone. The finding also concerns HDAC4 and HDAC6, not HDACs generally. (LLM, conf=0.86)
Experimental — accuracy not yet measuredsApoE has been found to influence the transcriptome by modulating histone acetylation.
“Of note, sApoE has been found to influence the transcriptome by modulating histone acetylation (68, 69).”
From Secreted Apoe rewires melanoma cell state vulnerability to ferroptosis (2024) · cites this paper as [69]
The histone H3 acetylation and BDNF-expression sections (page not provided) show that ApoE3 and ApoE4, when administered with cholesterol, alter histone acetylation and BDNF gene expression. The paper does not demonstrate an effect on the transcriptome as a whole; its Discussion attributes a whole-transcriptome observation to previous work. (LLM, conf=0.86)
Experimental — accuracy not yet measuredIn the brains of Alzheimer's disease patients, nuclear translocation of HDA6 was increased compared with controls.
“In the brains of Alzheimer's disease patients, nuclear translocation of HDA6 was increased as compared with controls.”
From Apolipoprotein E metabolism and functions in brain and its role in Alzheimer's disease (2017) · cites this paper as [54]
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- Authors
- Sen, A., Nelson, T. J., & Alkon, D. L.
- Affiliations
- Blanchette Rockefeller Neurosciences Institute (US)
- Venue
- The Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2015-05-13
- Volume
- 35
- Issue
- 19
- Pages
- 7538-7551
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC6705431
- OpenAlex
- W1493503901
- Cited by
- 133
- References
- 76
- Citations by year
- 2026: 10 · 2025: 11 · 2024: 10 · 2023: 7 · 2022: 12 · 2021: 17 · 2020: 11 · 2019: 10 · 2018: 17 · 2017: 11 · 2016: 13 · 2015: 4
- FWCI
- 11.05
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Neuroscience (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Keywords
- APOE ε4, amyloid-beta oligomers, BDNF expression, histone deacetylase, histone H3 acetylation, LRP1, receptor-associated protein, protein kinase C epsilon, HDAC6, HDAC4, hippocampus, synaptic loss, Alzheimer's disease, epigenetic regulation, APOE3
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Animals, Apolipoproteins E, Brain, Cell Nucleolus, Cells, Cultured, Cholesterol, Female, Gene Expression Regulation, Histone Deacetylases, Humans, Male, Mice, Transgenic, Middle Aged, Neuroblastoma, Neurons, Protein Kinase C, Case-Control Studies, Amyloid beta-Peptides, Brain-Derived Neurotrophic Factor, Protein Transport, Low Density Lipoprotein Receptor-Related Protein-1, RNA Interference, Cell Line, Tumor, Mice
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