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Manganese Superoxide Dismutase Overexpression Attenuates MPTP Toxicity
Open accessAbstract
There is substantial evidence implicating mitochondrial dysfunction and free radical generation in the neurotoxicity of MPTP. Manganese superoxide dismutase (MnSOD) is the primary antioxidant enzyme protecting against superoxide radicals produced within mitochondria. Overexpression of human MnSOD in transgenic mice resulted in increased MnSOD localized to mitochondria in neurons and a 50% increase in total MnSOD activity in brain homogenates. We found that MPTP toxicity was significantly attenuated in the MnSOD transgenic mice which overexpress the human manganese superoxide dismutase gene, with these mice showing threefold greater dopamine levels than controls following MPTP. There were no alterations in MPP+ levels, suggesting that the effects were not due to altered metabolism of MPTP. A significant increase in 3-nitrotyrosine levels was seen in littermate controls but not in transgenic mice overexpressing human MnSOD. These results provide further evidence implicating mitochondrial dysfunction and oxidative damage in the pathogenesis of MPTP neurotoxicity.
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“the neurotoxicity of MPTP was significantly reduced in SOD2-overexpressing mice compared to wild-type mice [81]”
From Healthy Human Fecal Microbiota Transplantation into Mice Attenuates MPTP-Induced Neurotoxicity via AMPK/SOD2 Pathway (2023) · cites this paper as [81]
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Cites
Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
Beauchamp, C., & Fridovich, I. (1971) · Analytical Biochemistry · doi:10.1016/0003-2697(71)90370-8 · Cited by 12,892
Boveris, A., & Chance, B. (1973) · Biochemical Journal · doi:10.1042/bj1340707 · Cited by 2,626
Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese superoxide dismutase
Li, Y., Huang, T.-T., Carlson, E. J., Melov, S., Ursell, P. C., Olson, J. L., Noble, L. J., Yoshimura, M. P., Berger, C., Chan, P. H., et al. (1995) · Nature Genetics · doi:10.1038/ng1295-376 · Cited by 1,789
Peroxynitrite-mediated tyrosine nitration catalyzed by superoxide dismutase
Ischiropoulos, H., Zhu, L., Chen, J., Tsai, M., Martin, J. C., Smith, C. D. L., & Beckman, J. S. (1992) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(92)90431-u · Cited by 1,499
Lebovitz, R. M., Zhang, H., Vogel, H., Cartwright, J., Dionne, L., Lu, N., Huang, S., & Matzuk, M. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.18.9782 · Cited by 1,023
Mitochondrial Superoxide Dismutase
Weisiger, R. A., & Fridovich, I. (1973) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)43735-6 · Cited by 960
Keller, J. N., Kindy, M. S., Holtsberg, F. W., St. Clair, D. K., Yen, H.-C., Germeyer, A., Steiner, S. M., Bruce-Keller, A. J., Hutchins, J. B., & Mattson, M. P. (1998) · The Journal of Neuroscience · doi:10.1523/jneurosci.18-02-00687.1998 · Cited by 863
Self-citationAn assay for superoxide dismutase activity in mammalian tissue homogenates
Spitz, D. R., & Oberley, L. W. (1989) · Analytical Biochemistry · doi:10.1016/0003-2697(89)90192-9 · Cited by 751
Human copper-containing superoxide dismutase of high molecular weight.
Marklund, S. L. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.24.7634 · Cited by 749
Pathological implications of nitric oxide, superoxide and peroxynitrite formation
Beckman, J. S., & Crow, J. P. (1993) · Biochemical Society Transactions · doi:10.1042/bst0210330 · Cited by 674
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Browne, S. E., & Beal, M. F. (2002) · International review of neurobiology · doi:10.1016/s0074-7742(02)53010-5 · Cited by 17
Self-citationAge-dependent redox status in the brain stem of NO-deficient hypertensive rats
Majzúnová, M., Pakanová, Z., Kvasnicka, P., Bališ, P., Čačányiová, S., & Dovinová, I. (2017) · Journal of Biomedical Science · doi:10.1186/s12929-017-0366-4 · Cited by 15
Chiueh, C., Andoh, T., & Chock, P. (2005) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2005.03.020 · Cited by 15
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Han, X., Zhang, B., Gong, Q., Liu, T., Wang, C., Sun, Y., Jia, H., pu, Y., Hou, Q., & Yang, X. (2024) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2024.10.281 · Cited by 12
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Age-related alterations of oxidative stress markers in the mouse hippocampal CA1 sector
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Szweda, L. I., Szweda, P. A., & Holian, A. (2000) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(00)19053-6 · Cited by 12
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Jackson-Lewis, V. R., & Smeyne, R. J. (2005) · Elsevier eBooks · doi:10.1016/b978-012088382-0/50012-8 · Cited by 5
Jackson-Lewis, V., Lester, D. B., Kozina, E. A., Przedborski, S., & Smeyne, R. J. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405195-9.00017-2 · Cited by 5
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Lee, T.-K., Lee, J., Kim, D., Lee, J., Kim, S., Kim, H. I., Shin, M. C., Cho, J., Won, M., & Choi, S. Y. (2022) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2022.11572 · Cited by 4
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Saif, S. (2004) · Digital WPI · Cited by 3
Gu, L., Miller, K. E., & Dryhurst, G. (2000) · Neurotoxicity Research · doi:10.1007/bf03033344 · Cited by 2
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Kiningham, K. K. (2014) · Royal Society of Chemistry eBooks · doi:10.1039/9781782622383-00077 · Cited by 2
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Holley, A. K., & Clair, D. K. S. (2016) · Oxidative stress in applied basic research and clinical practice · doi:10.1007/978-3-319-30705-3_3 · Cited by 2
Manganese Superoxide Dismutase Transgenic Mice: Characteristics and Implications
Chow, C. K., Yen, H., Ibrahim, W. H., & Clair, D. K. S. (2002) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(02)53064-0 · Cited by 2
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Ferrucci, M., & Fornai, F. (2022) · Springer eBooks · doi:10.1007/978-3-031-15080-7_239 · Cited by 1
Ries, V., & Burke, R. E. (2008) · Elsevier eBooks · doi:10.1016/b978-0-12-374028-1.00010-5 · Cited by 1
Robb, E. L. (2013) · Brock University Digital Repository (Brock University) · Cited by 1
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Kuhn, D. M. (2002) · Humana Press eBooks · doi:10.1007/978-1-59259-165-7_7 · Cited by 1
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Kolhe, A. (2009) · FIU - Digital Commons (Florida International University) · doi:10.25148/etd.fi10022526
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Przedborski, S. (2008) · doi:10.21236/ada494929
Buettner, G. R., Oberley, L. W., Spitz, D. R., & Domann, F. E. (2003)
alpha-Synuclein: Synaptische Funktion und Rolle bei der Pathogenese der Parkinson-Syndrome
Schlüter, O. M. (2002) · eDiss (Georg-August-Universität Göttingen) · doi:10.53846/goediss-680
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Ikeno, Y., & Remmen, H. V. (2003) · Springer eBooks · doi:10.1007/978-94-017-0671-1_9
New Animal Models in Toxicology
Floyd, E. (2002) · Elsevier eBooks · doi:10.1016/b978-012330215-1/50014-4
The Environmental Contribution to Redox Dyshomeostasis in Parkinson’s Disease
Garza-Lombó, C., & Franco, R. (2022) · Molecular and integrative toxicology · doi:10.1007/978-3-030-87451-3_4
Metadata
- Authors
- Klivenyi, P., St. Clair, D., Wermer, M., Yen, H.-C., Oberley, T., Yang, L., & Beal, M. F.
- Affiliations
- Harvard University (US)
- University of Kentucky (US)
- University of Wisconsin–Madison (US)
- Venue
- Neurobiology of Disease
- Publisher
- Elsevier BV
- Published
- 1998-10
- Volume
- 5
- Issue
- 4
- Pages
- 253-258
- ISSN
- 0969-9961 (ISSN-L)
- OpenAlex
- W2009842580
- Cited by
- 142
- References
- 25
- Citations by year
- 2024: 3 · 2023: 2 · 2022: 3 · 2021: 1 · 2020: 3 · 2019: 1 · 2018: 2 · 2017: 5 · 2016: 5 · 2015: 3 · 2014: 6 · 2013: 3 · 2012: 6
- FWCI
- 5.93
- Type
- journal article
- Language
- en
- Open access
- green
- doaj.org
- Licence
- Locations
- Neurobiology of Disease (publishedVersion)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institutes of Health (5r01ns032365-03, 5p01ns031579-05)
- National Cancer Institute (CA49797)
- National Institute of Neurological Disorders and Stroke (NS31579, NS32365)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Parkinson's Disease Mechanisms and Treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Keywords
- manganese superoxide dismutase, MPTP-induced neurotoxicity, Parkinson's disease, mitochondrial dysfunction, oxidative stress, superoxide, dopamine levels, MPP+, nitrotyrosine, neuroprotection, transgenic mice, antioxidant enzymes
- MeSH terms
- Animals, Brain, Brain Diseases, Cerebral Cortex, Dopamine, Humans, Mice, Transgenic, Mitochondria, Neurons, Superoxide Dismutase, 3,4-Dihydroxyphenylacetic Acid, Dopamine Agents, 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine, 1-Methyl-4-phenylpyridinium, Gene Expression, Microscopy, Immunoelectron, Transgenes, Mice
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