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Oxidative Medicine and Cellular Longevity
Volume 2013 (2013), Article ID 817807, 6 pages
Diversity of Mitochondrial Pathology in a Mouse Model of Axonal Degeneration in Synucleinopathies
1Tokyo Metropolitan Institute of Medical Sciences, 2-1-6 Kamikitazawa, Setagaya-ku, Tokyo 156-0057, Japan
2Division of Animal Sciences, National Institute of Agrobiological Sciences, 1-2 Ohwashi, Tsukuba, Ibaraki 305-8634, Japan
3Nippon Medical School, 1-1-5 Sendagi, Bunkyo-ku, Tokyo 113-8602, Japan
Received 14 December 2012; Accepted 18 February 2013
Academic Editor: Grzegorz A. Czapski
Copyright © 2013 Akio Sekigawa et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
- A. R. Esteves, D. M. Arduíno, D. F. F. Silva, C. R. Oliveira, and S. M. Cardoso, “Mitochondrial dysfunction: the road to alpha-synuclein oligomerization in PD,” Parkinson's Disease, vol. 2011, Article ID 693761, 20 pages, 2011.
- N. Exner, A. K. Lutz, C. Haass, and K. F. Winklhofer, “Mitochondrial dysfunction in Parkinson's disease: molecular mechanisms and pathophysiological consequences,” The EMBO Journal, vol. 31, pp. 3038–3062, 2012.
- M. Hashimoto, E. Rockenstein, L. Crews, and E. Masliah, “Role of protein aggregation in mitochondrial dysfunction and neurodegeneration in Alzheimer's and Parkinson's diseases,” NeuroMolecular Medicine, vol. 4, no. 1-2, pp. 21–35, 2003.
- J. W. Langston, “The etiology of Parkinson's disease with emphasis on the MPTP story,” Neurology, vol. 47, no. 6, supplement 3, pp. S153–S160, 1996.
- A. H. V. Schapira, J. M. Cooper, D. Dexter, P. Jenner, J. B. Clark, and C. D. Marsden, “Mitochondrial complex I deficiency in Parkinson's disease,” The Lancet, vol. 1, no. 8649, p. 1269, 1989.
- A. Bender, K. J. Krishnan, C. M. Morris et al., “High levels of mitochondrial DNA deletions in substantia nigra neurons in aging and Parkinson disease,” Nature Genetics, vol. 38, no. 5, pp. 515–517, 2006.
- Y. Mizuno, N. Hattori, and H. Mochizuki, “Genetic aspects of Parkinson's disease,” Handbook of Clinical Neurology, vol. 83, pp. 217–244, 2007.
- A. Sekigawa, M. Fujita, K. Sekiyama, et al., “Distinct mechanisms of axonal globule formation in mice expressing human wild type alpha-synuclein or dementia with Lewy bodies-linked P123H beta-synuclein,” Molecular Brain, vol. 5, article 34, 2012.
- V. Bonifati, P. Rizzu, M. J. van Baren et al., “Mutations in the DJ-1 gene associated with autosomal recessive early-onset parkinsonism,” Science, vol. 299, no. 5604, pp. 256–259, 2003.
- E. M. Valente, P. M. Abou-Sleiman, V. Caputo et al., “Hereditary early-onset Parkinson's disease caused by mutations in PINK1,” Science, vol. 304, no. 5674, pp. 1158–1160, 2004.
- K. Okatsu, T. Oka, M. Iguchi, et al., “PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria,” Nature Communications, vol. 3, article 1016, 2012.
- J. M. M. Tan and T. M. Dawson, “Parkin blushed by PINK1,” Neuron, vol. 50, no. 4, pp. 527–529, 2006.
- R. J. Youle and D. P. Narendra, “Mechanisms of mitophagy,” Nature Reviews Molecular Cell Biology, vol. 12, pp. 9–14, 2011.
- D. M. Arduino, A. R. Esteves, L. Cortes, et al., “Mitochondrial metabolism in Parkinson's disease impairs quality control autophagy by hampering microtubule-dependent traffic,” Human Molecular Genetics, vol. 21, pp. 4680–4702, 2012.
- L. J. Hsu, Y. Sagara, A. Arroyo et al., “α-Synuclein promotes mitochondrial deficit and oxidative stress,” American Journal of Pathology, vol. 157, no. 2, pp. 401–410, 2000.
- K. Nakamura, V. M. Nemani, F. Azarbal et al., “Direct membrane association drives mitochondrial fission by the Parkinson disease-associated protein α-synuclein,” The Journal of Biological Chemistry, vol. 286, no. 23, pp. 20710–20726, 2011.
- C. Paisán-Ruíz, S. Jain, E. W. Evans et al., “Cloning of the gene containing mutations that cause PARK8-linked Parkinson's disease,” Neuron, vol. 44, no. 4, pp. 595–600, 2004.
- A. Zimprich, S. Biskup, P. Leitner et al., “Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology,” Neuron, vol. 44, no. 4, pp. 601–607, 2004.
- M. R. Cookson, “The role of leucine-rich repeat kinase 2 (LRRK2) in Parkinson's disease,” Nature Reviews Neuroscience, vol. 11, no. 12, pp. 791–797, 2010.
- S. Biskup, D. J. Moore, F. Celsi et al., “Localization of LRRK2 to membranous and vesicular structures in mammalian brain,” Annals of Neurology, vol. 60, no. 5, pp. 557–569, 2006.
- X. Wang, M. H. Yan, H. Fujioka, et al., “LRRK2 regulates mitochondrial dynamics and function through direct interaction with DLP1,” Human Molecular Genetics, vol. 21, pp. 1931–1944, 2012.
- M. Poulopoulos, O. A. Levy, and R. N. Alcalay, “The neuropathology of genetic Parkinson's disease,” Movement Disorders, vol. 27, pp. 831–842, 2012.
- F. Seitelberger, “Neuropathological conditions related to neuroaxonal dystrophy,” Acta Neuropathologica, vol. 5, supplement 5, pp. 17–29, 1971.
- M. Fujita, S. Sugama, K. Sekiyama et al., “A β-synuclein mutation linked to dementia produces neurodegeneration when expressed in mouse brain,” Nature Communications, vol. 1, no. 8, article 110, 2010.
- D. MacLeod, J. Dowman, R. Hammond, T. Leete, K. Inoue, and A. Abeliovich, “The familial Parkinsonism gene LRRK2 regulates neurite process morphology,” Neuron, vol. 52, no. 4, pp. 587–593, 2006.
- Y. Li, W. Liu, T. F. Oo et al., “Mutant LRRK2R1441G BAC transgenic mice recapitulate cardinal features of Parkinson's disease,” Nature Neuroscience, vol. 12, no. 7, pp. 826–828, 2009.
- M. K. Lee, W. Stirling, Y. Xu et al., “Human α-synuclein-harboring familial Parkinson's disease-linked Ala-53 → Thr mutation causes neurodegenerative disease with α-synuclein aggregation in transgenic mice,” Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 13, pp. 8968–8973, 2002.
- H. Ohtake, P. Limprasert, Y. Fan et al., “β-synuclein gene alterations in dementia with Lewy bodies,” Neurology, vol. 63, no. 5, pp. 805–811, 2004.
- M. Hashimoto and A. R. La Spada, “β-synuclein in the pathogenesis of Parkinson's disease and related α-synucleinopathies: emerging roles and new directions,” Future Neurology, vol. 7, pp. 155–163, 2012.
- M. Fujita, A. Sekigawa, K. Sekiyama, Y. Takamatsu, and M. Hashimoto, “Possible alterations in beta-synuclein, the non-amyloidogenic homologue of alpha-synuclein, during progression of sporadic alpha-synucleinopathies,” International Journal of Molecular Sciences, vol. 13, pp. 11584–11592, 2012.
- J. E. Galvin, K. Uryu, V. M. Y. Lee, and J. Q. Trojanowski, “Axon pathology in Parkinson's disease and Lewy body dementia hippocampus contains α-, β-, and γ-synuclein,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 23, pp. 13450–13455, 1999.
- J. E. Galvin, B. Giasson, H. I. Hurtig, V. M. Y. Lee, and J. Q. Trojanowski, “Neurodegeneration with brain iron accumulation, type 1 is characterized by α-, β-, and γ-synuclein neuropathology,” American Journal of Pathology, vol. 157, no. 2, pp. 361–368, 2000.
- Y. L. Wang, A. Takeda, H. Osaka et al., “Accumulation of β- and γ-synucleins in the ubiquitin carboxyl-terminal hydrolase L1-deficient gad mouse,” Brain Research, vol. 1019, no. 1-2, pp. 1–9, 2004.
- A. Tatsioni, N. G. Bonitsis, and J. P. A. Ioannidis, “Persistence of contradicted claims in the literature,” Journal of the American Medical Association, vol. 298, no. 21, pp. 2517–2526, 2007.
- R. C. Petersen, R. G. Thomas, M. Grundman et al., “Vitamin E and donepezil for the treatment of mild cognitive impairment,” The New England Journal of Medicine, vol. 352, no. 23, pp. 2379–2388, 2005.