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Impaired Balance of Mitochondrial Fission and Fusion in Alzheimer's Disease
Open accessAbstract
Mitochondrial dysfunction is a prominent feature of Alzheimer's disease (AD) neurons. In this study, we explored the involvement of an abnormal mitochondrial dynamics by investigating the changes in the expression of mitochondrial fission and fusion proteins in AD brain and the potential cause and consequence of these changes in neuronal cells. We found that mitochondria were redistributed away from axons in the pyramidal neurons of AD brain. Immunoblot analysis revealed that levels of DLP1 (also referred to as Drp1), OPA1, Mfn1, and Mfn2 were significantly reduced whereas levels of Fis1 were significantly increased in AD. Despite their differential effects on mitochondrial morphology, manipulations of these mitochondrial fission and fusion proteins in neuronal cells to mimic their expressional changes in AD caused a similar abnormal mitochondrial distribution pattern, such that mitochondrial density was reduced in the cell periphery of M17 cells or neuronal process of primary neurons and correlated with reduced spine density in the neurite. Interestingly, oligomeric amyloid-beta-derived diffusible ligands (ADDLs) caused mitochondrial fragmentation and reduced mitochondrial density in neuronal processes. More importantly, ADDL-induced synaptic change (i.e., loss of dendritic spine and postsynaptic density protein 95 puncta) correlated with abnormal mitochondrial distribution. DLP1 overexpression, likely through repopulation of neuronal processes with mitochondria, prevented ADDL-induced synaptic loss, suggesting that abnormal mitochondrial dynamics plays an important role in ADDL-induced synaptic abnormalities. Based on these findings, we suggest that an altered balance in mitochondrial fission and fusion is likely an important mechanism leading to mitochondrial and neuronal dysfunction in AD brain.
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“Increased accumulation of APP and its processed peptides in the mitochondria of AD neurons and their effects on mitochondrial dynamics and mitophagy have been documented (21–24).”
From Alzheimer's Disease–Associated Amyloid-β Precursor Protein Prevents Aging Stress–Induced Mitophagy and Fumarate Depletion to Improve Antitumor Immunity (2025) · cites this paper as [24]
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In the citing paper
“Mitochondrial fission-fusion dynamics through alterations of Drp1, Parkin, and Pink1 functions (23,24), which play essential roles in mitophagy induction and mitochondrial quality control during healthy brain aging, are disrupted in various neurodegenerative diseases, including Parkinson’s disease (PD) and AD (25).”
From Alzheimer's Disease–Associated Amyloid-β Precursor Protein Prevents Aging Stress–Induced Mitophagy and Fumarate Depletion to Improve Antitumor Immunity (2025) · cites this paper as [24]
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“Aβ accumulates in mitochondria in AD brain, which is accompanied by altered mitochondrial structure, decreased mitochondrial respiratory function and ATP production, impaired mitochondrial dynamics, and elevated mitochondria-associated oxidative stress.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [97]
In the citing paper
“Mitochondrial Aβ levels correlate with abnormalities in mitochondrial structure and function.”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [97]
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“Aβ peptides can induce ROS production from mitochondria, leading to release of cytochrome c and apoptosis-inducing factor, thereby driving mitochondrial dysfunction, cell apoptosis and neuronal loss [97, 100].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [97]
In the citing paper
“Soluble Aβ oligomers disrupted the balance between mitochondrial fission and fusion, leading to significant mitochondrial dysfunction.197,198”
From Amyloid β-based therapy for Alzheimer’s disease: Challenges, successes and future (2023) · cites this paper as [197]
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Metadata
- Authors
- Wang, X., Su, B., Lee, H.-G., Li, X., Perry, G., Smith, M. A., & Zhu, X.
- Affiliations
- Case Western Reserve University (US)
- The University of Texas at San Antonio (US)
- Venue
- Journal of Neuroscience
- Publisher
- Society for Neuroscience
- Published
- 2009-07-15
- Volume
- 29
- Issue
- 28
- Pages
- 9090-9103
- ISSN
- 0270-6474 (ISSN-L)
- 1529-2401
- PMC
- PMC2735241
- OpenAlex
- W2089141103
- Cited by
- 1,224
- References
- 50
- Citations by year
- 2026: 49 · 2025: 82 · 2024: 71 · 2023: 92 · 2022: 77 · 2021: 102 · 2020: 83 · 2019: 71 · 2018: 60 · 2017: 75 · 2016: 67 · 2015: 59 · 2014: 57 · 2013: 58 · 2012: 84
- FWCI
- 29.56
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Neuroscience (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Alzheimer's Association (AG031852, IIRG-07-60196)
- National Institutes of Health (IIRG-07-60196)
- National Institute on Aging (AG 031852, R01AG031852)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- Alzheimer's disease, mitochondrial dynamics, mitochondrial fission, mitochondrial fusion, Drp1, OPA1, Mfn1, mitofusin 2, Fis1, mitochondrial distribution, axons, pyramidal neurons, synaptic loss, dendritic spines, PSD-95, mitochondrial dysfunction
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Animals, Antibodies, Monoclonal, Biotin, Cells, Cultured, Embryo, Mammalian, Gene Expression Regulation, Hippocampus, Humans, Membrane Proteins, Microtubule-Associated Proteins, Middle Aged, Mitochondria, Mutation, Neuroblastoma, Neurons, Postmortem Changes, Time Factors, Transfection, Amyloid beta-Peptides, Microscopy, Immunoelectron, Reactive Oxygen Species, GTP Phosphohydrolases, Mitochondrial Proteins, Membrane Transport Proteins, Mitochondrial Membrane Transport Proteins, Dynamins, Green Fluorescent Proteins, Rats, Cyclooxygenase 1
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