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Mechanisms of Hybrid Oligomer Formation in the Pathogenesis of Combined Alzheimer's and Parkinson's Diseases
Open accessAbstract
BACKGROUND: Misfolding and pathological aggregation of neuronal proteins has been proposed to play a critical role in the pathogenesis of neurodegenerative disorders. Alzheimer's disease (AD) and Parkinson's disease (PD) are frequent neurodegenerative diseases of the aging population. While progressive accumulation of amyloid beta protein (Abeta) oligomers has been identified as one of the central toxic events in AD, accumulation of alpha-synuclein (alpha-syn) resulting in the formation of oligomers and protofibrils has been linked to PD and Lewy body Disease (LBD). We have recently shown that Abeta promotes alpha-syn aggregation and toxic conversion in vivo, suggesting that abnormal interactions between misfolded proteins might contribute to disease pathogenesis. However the molecular characteristics and consequences of these interactions are not completely clear. METHODOLOGY/PRINCIPAL FINDINGS: In order to understand the molecular mechanisms involved in potential Abeta/alpha-syn interactions, immunoblot, molecular modeling, and in vitro studies with alpha-syn and Abeta were performed. We showed in vivo in the brains of patients with AD/PD and in transgenic mice, Abeta and alpha-synuclein co-immunoprecipitate and form complexes. Molecular modeling and simulations showed that Abeta binds alpha-syn monomers, homodimers, and trimers, forming hybrid ring-like pentamers. Interactions occurred between the N-terminus of Abeta and the N-terminus and C-terminus of alpha-syn. Interacting alpha-syn and Abeta dimers that dock on the membrane incorporated additional alpha-syn molecules, leading to the formation of more stable pentamers and hexamers that adopt a ring-like structure. Consistent with the simulations, under in vitro cell-free conditions, Abeta interacted with alpha-syn, forming hybrid pore-like oligomers. Moreover, cells expressing alpha-syn and treated with Abeta displayed increased current amplitudes and calcium influx consistent with the formation of cation channels. CONCLUSION/SIGNIFICANCE: These results support the contention that Abeta directly interacts with alpha-syn and stabilized the formation of hybrid nanopores that alter neuronal activity and might contribute to the mechanisms of neurodegeneration in AD and PD. The broader implications of such hybrid interactions might be important to the pathogenesis of other disorders of protein misfolding.
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“Co-immunoprecipitation experiments have shown that αSyn monomers, dimers, trimers and pentamers bind to monomeric Aβ in post-mortem samples from AD and DLB brains [67].”
From α-synuclein in the pathophysiology of Alzheimer’s disease (2019) · cites this paper as [67]
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Self-citation
Metadata
- Authors
- Tsigelny, I. F., Crews, L., Desplats, P., Shaked, G. M., Sharikov, Y., Mizuno, H., Spencer, B., Rockenstein, E., Trejo, M., Platoshyn, O., Yuan, J. X.-J., & Masliah, E.
- Affiliations
- San Diego Supercomputer Center (US)
- University of California San Diego (US)
- Corresponding author
- Masliah, Eliezer
- ORCID
- Venue
- PLoS ONE
- Publisher
- Public Library of Science (PLoS)
- Published
- 2008-09-04
- Volume
- 3
- Issue
- 9
- Pages
- e3135
- ISSN
- 1932-6203 (ISSN-L)
- PMC
- PMC2519786
- OpenAlex
- W2065878937
- Cited by
- 281
- References
- 115
- Citations by year
- 2026: 3 · 2025: 12 · 2024: 14 · 2023: 14 · 2022: 13 · 2021: 18 · 2020: 25 · 2019: 20 · 2018: 18 · 2017: 22 · 2016: 16 · 2015: 18 · 2014: 14 · 2013: 9 · 2012: 21
- FWCI
- 9.93
- Type
- journal article
- Language
- en
- Status
- Retracted
- Update notices
- retraction (2025-03-18)
- Open access
- gold
- doi.org
- Licence
- Locations
- PLoS ONE (publishedVersion, public-domain)
- PubMed Central (publishedVersion, public-domain)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Figshare (submittedVersion, cc-by)
- Funders
- U.S. Department of Energy
- National Institutes of Health (AG‐18440)
- National Institute on Aging (R37AG018440, R01AG018440, AG 18440)
- National Heart, Lung, and Blood Institute (R01HL066012, HL066012)
- Argonne National Laboratory
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Alzheimer's disease, Parkinson's disease, amyloid-beta, alpha-synuclein, protein-protein interaction, protein misfolding, Lewy body disease, nanopores, cation channels, calcium influx, protein aggregation, transgenic mice
- MeSH terms
- Alzheimer Disease, Animals, Brain, Calcium, Computer Simulation, Electrophysiology, Humans, Mice, Transgenic, Parkinson Disease, Protein Denaturation, Protein Structure, Tertiary, Protein Folding, Lewy Body Disease, Mice, alpha-Synuclein
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