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β-Synuclein Inhibits α-Synuclein Aggregation
Open accessAbstract
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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“-Synuclein inhibits ␣-synuclein aggregation in mice, and mouse tau may retard human tau aggregation (Rochet et al., 2000;Hashimoto et al., 2001;Andorfer et al., 2003).”
From Aβ40 Inhibits Amyloid Deposition In Vivo (2007) · cites this paper as Hashimoto et al., 2001
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Cites
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
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-citationMasliah, 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-citationStabilization 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
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-citationIdentification of two distinct synucleins from human brain
Jakes, R., Spillantini, M. G., & Goedert, M. (1994) · FEBS Letters · doi:10.1016/0014-5793(94)00395-5 · Cited by 1,080
Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation
Serpell, L. C., Berriman, J. A., Jakes, R., Goedert, M., & Crowther, R. A. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.9.4897 · Cited by 755
α-Synuclein Promotes Mitochondrial Deficit and Oxidative Stress
Hsu, L. J., Sagara, Y., Arroyo, A., Rockenstein, E. M., Sisk, A., Mallory, M. E., Wong, J., Takenouchi, T., Hashimoto, M., & Masliah, E. (2000) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)64553-1 · Cited by 737
Self-citationα-Synuclein Fibrillogenesis Is Nucleation-dependent
Wood, S. J., Wypych, J., Steavenson, S., Louis, J., Citron, M., & Biere, A. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.28.19509 · Cited by 733
Both Familial Parkinson's Disease Mutations Accelerate α-Synuclein Aggregation
Narhi, L. O., Wood, S. J., Steavenson, S., Jiang, Y., Wu, G. M., Anafi, D., Kaufman, S. A., Martin, F. H., Sitney, K. C., Denis, P., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.14.9843 · Cited by 721
Amyloid diseases: Abnormal protein aggregation in neurodegeneration
Koo, E. H., Lansbury, P. T., & Kelly, J. W. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.9989 · Cited by 686
α-Synuclein Membrane Interactions and Lipid Specificity
Jo, E., McLaurin, J., Yip, C. M., George‐Hyslop, P. S., & Fraser, P. E. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004345200 · Cited by 610
Masliah, E., Rockenstein, E., Veinbergs, I., Sagara, Y., Mallory, M., Hashimoto, M., & Mucke, L. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.211412398 · Cited by 607
Self-citationDityrosine Cross-linking Promotes Formation of Stable α-Synuclein Polymers
Souza, J. M., Giasson, B. I., Chen, Q., Lee, V. M. ‐., & Ischiropoulos, H. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000206200 · Cited by 572
α-Synuclein Shares Physical and Functional Homology with 14-3-3 Proteins
Ostrerova, N., Petrucelli, L., Farrer, M. J., Mehta, N., Choi, P., Hardy, J., & Wolozin, B. L. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-14-05782.1999 · Cited by 560
The A53T α-Synuclein Mutation Increases Iron-Dependent Aggregation and Toxicity
Golts, N., Petrucelli, L., Hardy, J., Lee, J. M., Farer, M., & Wolozin, B. L. (2000) · Journal of Neuroscience · doi:10.1523/jneurosci.20-16-06048.2000 · Cited by 550
Interaction of Human α-Synuclein and Parkinson's Disease Variants with Phospholipids
Perrin, R. J., Woods, W. S., Clayton, D. F., & George, J. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004851200 · Cited by 444
Oxidative stress induces amyloid-like aggregate formation of NACP/α-synuclein in vitro
Hashimoto, M., Hsu, L. J., Xia, Y., Takeda, A., Sisk, A., Sundsmo, M., & Masliah, E. (1999) · NeuroReport · doi:10.1097/00001756-199903170-00011 · Cited by 429
Self-citationAbnormal accumulation of NACP/alpha-synuclein in neurodegenerative disorders.
Takeda, A., Mallory, M. E., Sundsmo, M. P., Honer, W. G., Hansen, L. A., & Masliah, E. (1998) · Europe PMC (PubMed Central) · Cited by 403
Self-citationInfluence of mutation type and X chromosome inactivation on Rett syndrome phenotypes
Amir, R. E., den Veyver, I. B. V., Schultz, R., Malicki, D. M., Tran, C. Q., Dahle, E. J., Philippi, A., Tímár, L., Percy, A. K., Motil, K. J., et al. (2000) · Annals of Neurology · doi:10.1002/1531-8249(200005)47:5 · Cited by 351
Copper(II)-induced self-oligomerization of α-synuclein
Paik, S. R., Shin, H.-J., Lee, J., Chang, C., & Kim, J. (1999) · Biochemical Journal · doi:10.1042/bj3400821 · Cited by 340
NACP, a presynaptic protein, immunoreactivity in Lewy bodies in Parkinson's disease
Wakabayashi, K., Matsumoto, K., Takayama, K., Yoshimoto, M., & Takahashi, H. (1997) · Neuroscience Letters · doi:10.1016/s0304-3940(97)00891-4 · Cited by 331
Trojanowski, J. Q., Goedert, M., Iwatsubo, T., & Lee, V. M. ‐. (1998) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400432 · Cited by 297
Han, H., Weinreb, P. H., & Lansbury, P. T. (1995) · Chemistry & Biology · doi:10.1016/1074-5521(95)90071-3 · Cited by 287
Hashimoto, M., Hsu, L. J., Sisk, A., Xia, Y., Takeda, A., Sundsmo, M. P., & Masliah, E. (1998) · Brain Research · doi:10.1016/s0006-8993(98)00514-9 · Cited by 266
Self-citationRockenstein, E. M., McConlogue, L., Tan, H. T., Power, M., Masliah, E., & Mucke, L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.47.28257 · Cited by 255
Self-citationAlpha‐synuclein in Lewy Body Disease and Alzheimer's Disease
Hashimoto, M., & Masliah, E. (1999) · Brain Pathology · doi:10.1111/j.1750-3639.1999.tb00552.x · Cited by 254
Self-citationRamassamy, C., Averill‐Bates, D. A., Beffert, U., Bastianetto, S., Théroux, L., Lussier‐Cacan, S., Cohn, J. S., Christen, Y., Davignon, J., Quirion, R., et al. (1999) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(99)00102-1 · Cited by 244
Role of Cytochrome c as a Stimulator of α-Synuclein Aggregation in Lewy Body Disease
Hashimoto, M., Takeda, A., Hsu, L. J., Takenouchi, T., & Masliah, E. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.41.28849 · Cited by 239
Self-citationNon-A.beta. Component of Alzheimer's Disease Amyloid (NAC) is Amyloidogenic
Iwai, A., Yoshimoto, M., Masliah, E., & Saitoh, T. (1995) · Biochemistry · doi:10.1021/bi00032a006 · Cited by 237
Self-citationRochet, J., Conway, K. A., & Lansbury, P. T. (2000) · Biochemistry · doi:10.1021/bi001315u · Cited by 221
da Costa, C. A., Ancolio, K., & Checler, F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m002413200 · Cited by 216
Zhou, W., Hurlbert, M. S., Schaack, J. B., Prasad, K. N., & Freed, C. R. (2000) · Brain Research · doi:10.1016/s0006-8993(00)02215-0 · Cited by 207
Yoshimoto, M., Iwai, A., Kang, D. E., Otero, D. A., Xia, Y., & Saitoh, T. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.20.9141 · Cited by 203
Interaction between Aβ(1−42) and Aβ(1−40) in Alzheimer's β-Amyloid Fibril Formation in Vitro
Hasegawa, K., Yamaguchi, I., Omata, S., Gejyo, F., & Naiki, H. (1999) · Biochemistry · doi:10.1021/bi991161m · Cited by 198
Expression of mutant alpha-synuclein causes increased susceptibility to dopamine toxicity
Tabrizi, S. J. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.18.2683 · Cited by 196
Enhanced vulnerability to oxidative stress by α-synuclein mutations and C-terminal truncation
Kanda, S., Bishop, J. F., Eglitis, M. A., Yang, Y., & Mouradian, M. M. (2000) · Neuroscience · doi:10.1016/s0306-4522(00)00077-4 · Cited by 193
Biere, A. L., Wood, S. J., Wypych, J., Steavenson, S., Jiang, Y., Anafi, D., Jacobsen, F. W., Jarosinski, M. A., Wu, G., Louis, J., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m005514200 · Cited by 181
Stimulation of breast cancer invasion and metastasis by synuclein gamma.
Jia, T., Liu, Y. E., Liu, J., & Shi, Y. E. (1999) · PubMed · Cited by 171
A new brain‐specific 14‐kDa protein is a phosphoprotein
Nakajo, S., TSUKADA, K., Omata, K., Nakamura, Y., & Nakaya, K. (1993) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1993.tb18337.x · Cited by 170
Masliah, E., Iwai, A., Mallory, M. E., Uéda, K., & Saitoh, T. (1996) · Europe PMC (PubMed Central) · Cited by 168
Self-citationAltered expression of the synuclein family mRNA in Lewy body and Alzheimer’s disease
Rockenstein, E. M., Hansen, L. A., Mallory, M. E., Trojanowski, J. Q., Galasko, D. R., & Masliah, E. (2001) · Brain Research · doi:10.1016/s0006-8993(01)02772-x · Cited by 162
Self-citationJensen, P. H., Højrup, P., Hager, H., Nielsen, M. S., JACOBSEN, L., Olesen, O. F., Gliemann, J., & Jakes, R. (1997) · Biochemical Journal · doi:10.1042/bj3230539 · Cited by 143
Oxidative stress in Parkinson's disease and other neurodegenerative disorders.
Jenner, P. G. (1996) · PubMed · Cited by 106
alpha-Synuclein forms a complex with transcription factor Elk-1
Iwata, A., Miura, S., Kanazawa, I., Sawada, M., & Nukina, N. (2001) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2001.t01-1-00232.x · Cited by 98
Jensen, P. H., Sørensen, E. S., Petersen, T. E., Gliemann, J., & Rasmussen, L. K. (1995) · Biochemical Journal · doi:10.1042/bj3100091 · Cited by 97
Synoretin—A New Protein Belonging to the Synuclein Family
Surguchov, A. P., Surgucheva, I. G., Solessio, E. C., & Baehr, W. (1999) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.1999.0735 · Cited by 96
El‐Agnaf, O. M. A., & Irvine, G. B. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4262 · Cited by 91
Properties of NACP/α-synuclein and its role in Alzheimer’s disease
Iwai, A. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00036-3 · Cited by 78
Reduced Neuritic Outgrowth and Cell Adhesion in Neuronal Cells Transfected with Human α-Synuclein
Takenouchi, T., Hashimoto, M., Hsu, L. J., Mackowski, B., Rockenstein, E. M., Mallory, M. E., & Masliah, E. (2001) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.2000.0923 · Cited by 77
Self-citationPaik, S. R., Lee, J., Kim, D.-H., Chang, C., & Kim, Y. (1998) · FEBS Letters · doi:10.1016/s0014-5793(97)01537-8 · Cited by 69
Masliah, E. (2001) · Journal of Alzheimer s Disease · doi:10.3233/jad-2001-3117 · Cited by 67
Self-citationFerrigno, P. K., & Silver, P. A. (2000) · Neuron · doi:10.1016/s0896-6273(00)81132-0 · Cited by 65
Noguchi, C. T., Rodgers, G. P., & Schechter, A. N. (1989) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1989.tb24152.x · Cited by 41
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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Metadata
- Authors
- Hashimoto, M., Rockenstein, E., Mante, M., Mallory, M., & Masliah, E.
- Affiliations
- University of California San Diego (US)
- Corresponding author
- Masliah, Eliezer
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2001-10
- Volume
- 32
- Issue
- 2
- Pages
- 213-223
- ISSN
- 0896-6273 (ISSN-L)
- 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
- 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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