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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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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