Cited by 275Parkinson's Disease Mechanisms and TreatmentsAlzheimer's disease research and treatmentsNuclear Receptors and Signaling

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Reversible Inhibition of α-Synuclein Fibrillization by Dopaminochrome-mediated Conformational Alterations

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Norris, Erin H., Giasson, Benoit I., Hodara, Roberto, Xu, Shaohua, Trojanowski, John Q., Ischiropoulos, Harry, Lee, Virginia M.-Y.·2005·Journal of Biological Chemistry

DOI 10.1074/jbc.m412621200

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Abstract

Previous studies demonstrated that alpha-synuclein (alpha-syn) fibrillization is inhibited by dopamine, and studies to understand the molecular basis of this process were conducted (Conway, K. A., Rochet, J. C., Bieganski, R. M., and Lansbury, P. T., Jr. (2001) Science 294, 1346-1349). Dopamine inhibition of alpha-syn fibrillization generated exclusively spherical oligomers that depended on dopamine autoxidation but not alpha-syn oxidation, because mutagenesis of Met, His, and Tyr residues in alpha-syn did not abrogate this inhibition. However, truncation of alpha-syn at residue 125 restored the ability of alpha-syn to fibrillize in the presence of dopamine. Mutagenesis and competition studies with specific synthetic peptides identified alpha-syn residues 125-129 (i.e. YEMPS) as an important region in the dopamine-induced inhibition of alpha-syn fibrillization. Significantly, the dopamine oxidation product dopaminochrome was identified as a specific inhibitor of alpha-syn fibrillization. Dopaminochrome promotes the formation of spherical oligomers by inducing conformational changes, as these oligomers regained the ability to fibrillize by simple denaturation/renaturation. Taken together, these data indicate that dopamine inhibits alpha-syn fibrillization by inducing structural changes in alpha-syn that can occur through the interaction of dopaminochrome with the 125YEMPS129 motif of alpha-syn. These results suggest that the dopamine autoxidation can prevent alpha-syn fibrillization in dopaminergic neurons through a novel mechanism. Thus, decreased dopamine levels in substantia nigra neurons might promote alpha-syn aggregation in Parkinson's disease.

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α-Synuclein in Lewy bodies
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
Self-citation
α-synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with lewy bodies
Spillantini, M. G., Crowther, R. A., Jakes, R., Hasegawa, M., & Goedert, M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.11.6469 · Cited by 2,868
Parkinson's Disease
Lang, A. E., & Lozano, A. M. (1998) · New England Journal of Medicine · doi:10.1056/nejm199810083391506 · Cited by 2,072
The substantia nigra of the human brain
Damier, P., Hirsch, É. C., Agid, Y., & Graybiel, A. M. (1999) · Brain · doi:10.1093/brain/122.8.1437 · Cited by 1,827
Mice Lacking α-Synuclein Display Functional Deficits in the Nigrostriatal Dopamine System
Abeliovich, A., Schmitz, Y., Fariñas, I., Choi-Lundberg, D., Ho, W.-H., Castillo, P. E., Shinsky, N., Verdugo, J. M. G., Armanini, M., Ryan, A., et al. (2000) · Neuron · doi:10.1016/s0896-6273(00)80886-7 · Cited by 1,722
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
Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies.
(1998) · Europe PMC (PubMed Central) · Cited by 1,594
Self-citation
Oxidative Damage Linked to Neurodegeneration by Selective α-Synuclein Nitration in Synucleinopathy Lesions
Giasson, B. I., Duda, J. E., Murray, I. V. J., Chen, Q., Souza, J. M., Hurtig, H. I., Ischiropoulos, H., Trojanowski, J. Q., & Lee, V. M. ‐. (2000) · Science · doi:10.1126/science.290.5493.985 · Cited by 1,567
Self-citation
Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
Conway, K. A., Lee, S., Rochet, J., Ding, T. T., Williamson, R. E., & Lansbury, P. T. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.571 · Cited by 1,559
Neuropathology of Parkinson's Disease
Forno, L. (1996) · Journal of Neuropathology and Experimental Neurology · doi:10.1097/00005072-199603000-00001 · Cited by 1,556

Show all 51 references

Research works printed but not linked: 4

Louis, 1996, Adv. Neurol., 69, 311
Baba, 1998, Am. J. Pathol., 152, 879
Takeda, 1998, Am. J. Pathol., 152, 367
Lee, 2001, FASEB J., 15, 916

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Authors: Norris, E. H., Giasson, B. I., Hodara, R., Xu, S., Trojanowski, J. Q., Ischiropoulos, H., & Lee, V. M.-Y.
Affiliations: Institute on Aging (US)
Children's Hospital of Philadelphia (US)
Corresponding author: Lee, Virginia M.-Y.
ORCID: Norris, Erin H.
Giasson, Benoit I.
Hodara, Roberto
Xu, Shaohua
Trojanowski, John Q.
Ischiropoulos, Harry
Lee, Virginia M.-Y.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2005-06
Volume: 280
Issue: 22
Pages: 21212-21219
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m412621200
OpenAlex: W1975188689
Cited by: 273
References: 51
Citations by year: 2026: 5 · 2025: 4 · 2024: 5 · 2023: 12 · 2022: 8 · 2021: 14 · 2020: 9 · 2019: 21 · 2018: 14 · 2017: 8 · 2016: 5 · 2015: 17 · 2014: 17 · 2013: 15 · 2012: 13
FWCI: 11.25
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 5600 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Institutes of Health (NS044233, AG-09215)
National Institute on Aging (AG09215, P01AG009215)
National Institute of Neurological Disorders and Stroke (P01NS044233, NS-044233)
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: alpha-synuclein, fibrillization, dopamine autoxidation, conformational change, Parkinson's disease, dopaminergic neurons, substantia nigra, protein aggregation
MeSH terms: Circular Dichroism, Dopamine, Histidine, Humans, Methionine, Microscopy, Electron, Mutation, Nerve Tissue Proteins, Oxygen, Parkinson Disease, Peptides, Protein Conformation, Recombinant Proteins, Time Factors, Tyrosine, Mutagenesis, Protein Structure, Secondary, Spectroscopy, Fourier Transform Infrared, DNA, Complementary, Oxidative Stress, Microscopy, Atomic Force, Amino Acid Motifs, Indolequinones, Synucleins, alpha-Synuclein

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Reversible Inhibition of α-Synuclein Fibrillization by Dopaminochrome-mediated Conformational Alterations

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