Cited by 398Parkinson's Disease Mechanisms and TreatmentsAlzheimer's disease research and treatmentsNuclear Receptors and Signaling

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β-Synuclein Inhibits α-Synuclein Aggregation

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Hashimoto, Makoto, Rockenstein, Edward, Mante, Michael, Mallory, Margaret, Masliah, Eliezer·2001·Neuron

DOI 10.1016/s0896-6273(01)00462-7

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Abstract

We characterized beta-synuclein, the non-amyloidogenic homolog of alpha-synuclein, as an inhibitor of aggregation of alpha-synuclein, a molecule implicated in Parkinson's disease. For this, doubly transgenic mice expressing human (h) alpha- and beta-synuclein were generated. In doubly transgenic mice, beta-synuclein ameliorated motor deficits, neurodegenerative alterations, and neuronal alpha-synuclein accumulation seen in halpha-synuclein transgenic mice. Similarly, cell lines transfected with beta-synuclein were resistant to alpha-synuclein accumulation. halpha-synuclein was coimmunoprecipitated with hbeta-synuclein in the brains of doubly transgenic mice and in the double-transfected cell lines. Our results raise the possibility that beta-synuclein might be a natural negative regulator of alpha-synuclein aggregation and that a similar class of endogenous factors might regulate the aggregation state of other molecules involved in neurodegeneration. Such an anti-amyloidogenic property of beta-synuclein might also provide a novel strategy for the treatment of neurodegenerative disorders.

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Spillantini, M. G., Schmidt, M. L., Lee, V. M.-Y., Trojanowski, J. Q., Jakes, R., & Goedert, M. (1997) · Nature · doi:10.1038/42166 · Cited by 8,382
Mutation in the α-Synuclein Gene Identified in Families with Parkinson's Disease
Polymeropoulos, M. H., Lavedan, C., Leroy, E., Ide, S. E., Dehejia, A., Dutra, A., Pike, B., Root, H., Rubenstein, J., Boyer, R., et al. (1997) · Science · doi:10.1126/science.276.5321.2045 · Cited by 8,240
AlaSOPro mutation in the gene encoding α-synuclein in Parkinson's disease
Krüger, R., Kuhn, W., Müller, T., Woitalla, D., Graeber, M., Kösel, S., Przuntek, H., Epplen, J. T., Schols, L., & Riess, O. (1998) · Nature Genetics · doi:10.1038/ng0298-106 · Cited by 3,836
A Drosophila model of Parkinson's disease
Feany, M. Β., & Bender, W. W. (2000) · Nature · doi:10.1038/35006074 · Cited by 2,156
High-Level Neuronal Expression of Aβ1–42in Wild-Type Human Amyloid Protein Precursor Transgenic Mice: Synaptotoxicity without Plaque Formation
Mucke, L., Masliah, E., Yu, G.-Q., Mallory, M., Rockenstein, E. M., Tatsuno, G., Hu, K., Kholodenko, D., Johnson-Wood, K., & McConlogue, L. (2000) · The Journal of Neuroscience · doi:10.1523/jneurosci.20-11-04050.2000 · Cited by 1,856
Self-citation
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Masliah, E., Rockenstein, E. M., Veinbergs, I., Mallory, M. E., Hashimoto, M., Takeda, A., Sagara, Y., Sisk, A., & Mucke, L. (2000) · Science · doi:10.1126/science.287.5456.1265 · Cited by 1,779
Self-citation
Stabilization of α-Synuclein Secondary Structure upon Binding to Synthetic Membranes
Davidson, W. S., Jonas, A., Clayton, D. F., & George, J. M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.16.9443 · Cited by 1,622
NACP, A Protein Implicated in Alzheimer's Disease and Learning, Is Natively Unfolded
Weinreb, P. H., Zhen, W., Poon, A. W., Conway, K. A., & Lansbury, P. T. (1996) · Biochemistry · doi:10.1021/bi961799n · Cited by 1,524
Accelerated in vitro fibril formation by a mutant α-synuclein linked to early-onset Parkinson disease
Conway, K. A., Harper, J. D., & Lansbury, P. T. (1998) · Nature Medicine · doi:10.1038/3311 · Cited by 1,520
Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease.
Uéda, K., Fukushima, H., Masliah, E., Xia, Y., Iwai, A., Yoshimoto, M., Otero, D. A., Kondo, J. D. M., Ihara, Y., & Saitoh, T. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.23.11282 · Cited by 1,502
Self-citation

Show all 60 references

Research works printed but not linked: 1

Masliah, 1998, The role of synaptic proteins in neurodegenerative disorders, Neurosci. News, 1, 14

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Authors: Hashimoto, M., Rockenstein, E., Mante, M., Mallory, M., & Masliah, E.
Affiliations: University of California San Diego (US)
Corresponding author: Masliah, Eliezer
ORCID: Hashimoto, Makoto
Rockenstein, Edward
Mante, Michael
Masliah, Eliezer
Venue: Neuron
Publisher: Elsevier BV
Published: 2001-10
Volume: 32
Issue: 2
Pages: 213-223
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/s0896-6273(01)00462-7
OpenAlex: W2064132534
Cited by: 398
References: 60
Citations by year: 2026: 5 · 2025: 6 · 2024: 11 · 2023: 7 · 2022: 10 · 2021: 11 · 2020: 14 · 2019: 7 · 2018: 17 · 2017: 10 · 2016: 11 · 2015: 16 · 2014: 17 · 2013: 18 · 2012: 20
FWCI: 19.66
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 4307 d)
Locations: Neuron (publishedVersion)
PubMed (publishedVersion)
Funders: National Institute on Aging (AG10689, R01AG010689, P50AG005131, AG-5131, AG 18440)
Topics: Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Receptors and Signaling
Keywords: beta-synuclein, alpha-synuclein, protein aggregation, Parkinson's disease, neurodegeneration, transgenic mice, motor impairment, protein-protein interaction, neurodegenerative disease treatment
MeSH terms: Animals, Antiparkinson Agents, Brain, Humans, Immunosorbent Techniques, Mice, Inbred C57BL, Mice, Inbred DBA, Mice, Transgenic, Motor Activity, Nerve Tissue Proteins, Recombinant Proteins, Transfection, Gene Expression, Dimerization, Neurodegenerative Diseases, Mice, Synucleins, alpha-Synuclein, beta-Synuclein

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β-Synuclein Inhibits α-Synuclein Aggregation

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