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Mechanisms of Hybrid Oligomer Formation in the Pathogenesis of Combined Alzheimer's and Parkinson's Diseases
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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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Deramecourt, V., Bombois, S., Maurage, C., Ghestem, A., Drobecq, H., Vanmechelen, E., Lebert, F., Pasquier, F., & Delacourte, A. (2006) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/01.jnen.0000205145.54457.ea · Cited by 109
Hashimoto, M., Rockenstein, E. M., Mante, M., Crews, L. A., Bar‐On, P., Gage, F. H., Marr, R. A., & Masliah, E. (2004) · Gene Therapy · doi:10.1038/sj.gt.3302349 · Cited by 86
Self-citationBiological Markers of Alzheimer’s Disease
Klunk, W. E. (1998) · Neurobiology of Aging · doi:10.1016/s0197-4580(98)00013-x · Cited by 81
Effects of the cholesterol‐lowering compound methyl‐β‐cyclodextrin in models of α‐synucleinopathy
Bar‐On, P., Rockenstein, E. M., Adame, A., Ho, G. J., Hashimoto, M., & Masliah, E. (2006) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2006.04017.x · Cited by 78
Self-citationADDLs & protofibrils —the missing links?
Klein, W. L. (2002) · Neurobiology of Aging · doi:10.1016/s0197-4580(01)00312-8 · Cited by 77
Early Stages for Parkinson’s Development: α-Synuclein Misfolding and Aggregation
Yu, J., & Lyubchenko, Y. L. (2008) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-008-9115-5 · Cited by 71
Smith, D. P., Tew, D. J., Hill, A. F., Bottomley, S., Masters, C. L., Barnham, K. J., & Cappai, R. (2008) · Biochemistry · doi:10.1021/bi701522m · Cited by 66
Molecular Insights into Alzheimer's Disease
Pettegrew, J. W. (1989) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1989.tb12486.x · Cited by 63
Cortical Lewy body disease and Parkinson's disease dementia
Burn, D. J. (2006) · Current Opinion in Neurology · doi:10.1097/01.wco.0000247607.34697.a2 · Cited by 60
Yang, F., Uéda, K., Chen, P.-P., Ashe, K. H., & Cole, G. M. (2000) · Brain Research · doi:10.1016/s0006-8993(99)02207-6 · Cited by 54
Effects of Cerebrolysin on amyloid-beta deposition in a transgenic model of Alzheimer's disease.
Rockenstein, E. M., Mallory, M. E., Mante, M., Alford, M. F., Windisch, M., Moessler, H., & Masliah, E. (2002) · PubMed · Cited by 48
Self-citationDimeric structures of α-synuclein bind preferentially to lipid membranes
Giannakis, E., Pacífico, J., Smith, D. P., Hung, L. W., Masters, C. L., Cappai, R., Wade, J. D., & Barnham, K. J. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2008.01.012 · Cited by 45
Effects of Cerebrolysin™ on amyloid-β deposition in a transgenic model of Alzheimer’s disease
Rockenstein, E. M., Mallory, M. E., Mante, M., Alford, M. F., Windisch, M., Moessler, H., & Masliah, E. (2002) · Journal of neural transmission. Supplementum · doi:10.1007/978-3-7091-6139-5_31 · Cited by 40
Self-citationAggregation and fibrillization of prions in lipid membranes.
Kazlauskaite, J., & Pinheiro, T. J. T. (2005) · Biochemical Society Symposia · doi:10.1042/bss0720211 · Cited by 30
Lippa, S. M., Lippa, C. F., & Mori, H. (2005) · American Journal of Alzheimer s Disease & Other Dementias® · doi:10.1177/153331750502000506 · Cited by 29
Kurata, T., Kawarabayashi, T., Murakami, T., Miyazaki, K., Morimoto, N., Ohta, Y., Takehisa, Y., Nagai, M., Ikeda, M., Matsubara, E., et al. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21352 · Cited by 26
MAPAS: a tool for predicting membrane-contacting protein surfaces
Sharikov, Y., Walker, R. C., Greenberg, J. P., Kouznetsova, V. L., Nigám, S. K., Miller, M. A., Masliah, E., & Tsigelny, I. F. (2008) · Nature Methods · doi:10.1038/nmeth0208-119 · Cited by 22
Self-citation
Flagged first, then by citations
1 of the 115 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- IG McKeith, 1996, Consensus guidelines for the clinical and pathologic diagnosis of dementia with Lewy bodies (DLB): report of the consortium on DLB international workshop., Neurology, 47, 1113, 10.1212/WNL.47.5.1113 · DOI · Paper page
Cited by
Sorted by citations
Neuropathological alterations in Alzheimer disease
Serrano-Pozo, A., Frosch, M. P., Masliah, E., & Hyman, B. T. (2011) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a006189 · Cited by 3,345
Self-citationThe many faces of α-synuclein: from structure and toxicity to therapeutic target
Lashuel, H. A., Overk, C., Oueslati, A., & Masliah, E. (2012) · Nature reviews. Neuroscience · doi:10.1038/nrn3406 · Cited by 1,684
Self-citationIn vivo demonstration that α-synuclein oligomers are toxic
Winner, B., Jappelli, R., Maji, S. K., Desplats, P. A., Boyer, L., Aigner, S., Hetzer, C., Loher, T., Vilar, M., Campioni, S., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1100976108 · Cited by 1,463
Self-citationNguyen, P. H., Ramamoorthy, A., Sahoo, B. R., Zheng, J., Faller, P., Straub, J. E., Domínguez, L., Shea, J., Dokholyan, N. V., Simone, A. D., et al. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01122 · Cited by 680
Amyloid oligomers: formation and toxicity of Aβ oligomers
Sakono, M., & Zako, T. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07568.x · Cited by 633
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
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