Table of Contents Author Guidelines Submit a Manuscript
BioMed Research International
Volume 2014, Article ID 254680, 12 pages
http://dx.doi.org/10.1155/2014/254680
Research Article

Pu-Erh Tea Extract Induces the Degradation of FET Family Proteins Involved in the Pathogenesis of Amyotrophic Lateral Sclerosis

1Key Laboratory for Molecular Enzymology and Engineering, The Ministry of Education, Jilin University, Changchun 130012, China
2Department of Pu-Erh Tea and Medical Science, Hyogo College of Medicine, 1-1 Mukogawa-cho, Nishinomiya, Hyogo 663-8501, Japan
3State Key Laboratory of Phytochemistry and Plant Resources in West China, Kunming Institute of Botany, Chinese Academy of Sciences, Kunming 650201, China
4Department of Microbiology, Hyogo College of Medicine, 1-1 Mukogawa-cho, Nishinomiya, Hyogo 663-8501, Japan
5Key Laboratory of Pu-Erh Tea Science, The Ministry of Education, Yunnan Agricultural University, Kunming 650201, China

Received 7 November 2013; Revised 1 March 2014; Accepted 10 March 2014; Published 7 April 2014

Academic Editor: Tibor Hortobagyi

Copyright © 2014 Yang Yu 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.

Linked References

  1. J. Mitchell and G. Borasio, “Amyotrophic lateral sclerosis,” The Lancet, vol. 369, no. 9578, pp. 2031–2041, 2007. View at Publisher · View at Google Scholar · View at Scopus
  2. D. R. Rosen, T. Siddique, D. Patterson et al., “Mutations in Cu/Zn superoxide dismutase gene are associated with familial amyotrophic lateral sclerosis,” Nature, vol. 362, no. 6415, pp. 59–62, 1993. View at Publisher · View at Google Scholar · View at Scopus
  3. M. Neumann, D. M. Sampathu, L. K. Kwong et al., “Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis,” Science, vol. 314, no. 5796, pp. 130–133, 2006. View at Publisher · View at Google Scholar · View at Scopus
  4. J. Sreedharan, I. P. Blair, V. B. Tripathi et al., “TDP-43 mutations in familial and sporadic amyotrophic lateral sclerosis,” Science, vol. 319, no. 5870, pp. 1668–1672, 2008. View at Publisher · View at Google Scholar · View at Scopus
  5. E. Kabashi, P. N. Valdmanis, P. Dion et al., “TARDBP mutations in individuals with sporadic and familial amyotrophic lateral sclerosis,” Nature Genetics, vol. 40, no. 5, pp. 572–574, 2008. View at Publisher · View at Google Scholar · View at Scopus
  6. T. J. Kwiatkowski Jr., D. A. Bosco, A. L. LeClerc et al., “Mutations in the FUS/TLS gene on chromosome 16 cause familial amyotrophic lateral sclerosis,” Science, vol. 323, no. 5918, pp. 1205–1208, 2009. View at Publisher · View at Google Scholar · View at Scopus
  7. C. Vance, B. Rogelj, T. Hortobágyi et al., “Mutations in FUS, an RNA processing protein, cause familial amyotrophic lateral sclerosis type 6,” Science, vol. 323, no. 5918, pp. 1208–1211, 2009. View at Publisher · View at Google Scholar · View at Scopus
  8. J. Couthouisa, M. P. Harta, J. Shorter et al., “A yeast functional screen predicts new candidate ALS disease genes,” Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 52, pp. 20881–20890, 2011. View at Publisher · View at Google Scholar · View at Scopus
  9. J. Couthouis, M. P. Hart, R. Erion et al., “Evaluating the role of the FUS/TLS-related gene EWSR1 in amyotrophic lateral sclerosis,” Human Molecular Genetics, vol. 21, no. 13, pp. 2899–2911, 2012. View at Publisher · View at Google Scholar
  10. J. R. Tollervey, T. Curk, B. Rogelj et al., “Characterizing the RNA targets and position-dependent splicing regulation by TDP-43,” Nature Neuroscience, vol. 14, no. 4, pp. 452–458, 2011. View at Publisher · View at Google Scholar · View at Scopus
  11. M. Polymenidou, C. Lagier-Tourenne, K. R. Hutt et al., “Long pre-mRNA depletion and RNA missplicing contribute to neuronal vulnerability from loss of TDP-43,” Nature Neuroscience, vol. 14, no. 4, pp. 459–468, 2011. View at Publisher · View at Google Scholar · View at Scopus
  12. C. Lagier-Tourenne, M. Polymenidou, and D. W. Cleveland, “TDP-43 and FUS/TLS: emerging roles in RNA processing and neurodegeneration,” Human Molecular Genetics, vol. 19, no. 1, Article ID ddq137, pp. R46–R64, 2010. View at Publisher · View at Google Scholar · View at Scopus
  13. I. R. A. Mackenzie, O. Ansorge, M. Strong et al., “Pathological heterogeneity in amyotrophic lateral sclerosis with FUS mutations: two distinct patterns correlating with disease severity and mutation,” Acta Neuropathologica, vol. 122, no. 1, pp. 87–98, 2011. View at Publisher · View at Google Scholar · View at Scopus
  14. N. Suzuki, M. Aoki, H. Warita et al., “FALS with FUS mutation in Japan, with early onset, rapid progress and basophilic inclusion,” Journal of Human Genetics, vol. 55, no. 4, pp. 252–254, 2010. View at Publisher · View at Google Scholar · View at Scopus
  15. S. Watanabe, K. Kaneko, and K. Yamanaka, “Accelerated disease onset with stabilized familial amyotrophic lateral sclerosis (ALS)-linked mutant TDP-43 proteins,” The Journal of Biological Chemistry, vol. 288, no. 5, pp. 364–354, 2013. View at Google Scholar
  16. N. Egawa, S. Kitaoka, K. Tsukita et al., “Drug screening for ALS using patient-specific induced pluripotent stem cells,” Science Translational Medicine, vol. 4, no. 145, 2012. View at Publisher · View at Google Scholar
  17. J. C. Mitchell, P. McGoldrick, C. Vance et al., “Overexpression of human wild-type FUS causes progressive motor neuron degeneration in an age- and dose-dependent fashion,” Acta Neuropathologica, vol. 125, no. 2, pp. 273–288, 2013. View at Publisher · View at Google Scholar
  18. C. Huang, H. Zhou, J. Tong et al., “FUS transgenic rats develop the phenotypes of amyotrophic lateral sclerosis and frontotemporal lobar degeneration,” PLoS Genetics, vol. 7, no. 3, Article ID e1002011, 2011. View at Publisher · View at Google Scholar · View at Scopus
  19. A. Rietveld and S. Wiseman, “Antioxidant effects of tea: evidence from human clinical trials,” Journal of Nutrition, vol. 133, no. 10, pp. 3285S–3292S, 2003. View at Google Scholar · View at Scopus
  20. K.-C. Jeng, C.-S. Chen, Y.-P. Fang, R. C.-W. Hou, and Y.-S. Chen, “Effect of microbial fermentation on content of statin, GABA, and polyphenols in Pu-erh tea,” Journal of Agricultural and Food Chemistry, vol. 55, no. 21, pp. 8787–8792, 2007. View at Publisher · View at Google Scholar · View at Scopus
  21. H. Zhao, M. Zhang, L. Zhao, Y.-K. Ge, J. Sheng, and W. Shi, “Changes of constituents and activity to apoptosis and cell cycle during fermentation of tea,” International Journal of Molecular Sciences, vol. 12, no. 3, pp. 1862–1875, 2011. View at Publisher · View at Google Scholar · View at Scopus
  22. S.-J. Yan, L. Wang, Z. Li et al., “Inhibition of advanced glycation end product formation by Pu-erh Tea ameliorates progression of experimental diabetic nephropathy,” Journal of Agricultural and Food Chemistry, vol. 60, no. 16, pp. 4102–4110, 2012. View at Publisher · View at Google Scholar · View at Scopus
  23. L. X. Luo, X. C. Wu, Y. L. Deng, and S. W. Fu, “Variations of main biochemical components and their relations to quality formation during pile-fermentation process of Yunnan puerh tea,” Journal of Tea Science, vol. 18, pp. 53–60, 1998. View at Google Scholar
  24. D. A. Bosco, N. Lemay, H. K. Ko et al., “Mutant FUS proteins that cause amyotrophic lateral sclerosis incorporate into stress granules,” Human Molecular Genetics, vol. 19, no. 21, Article ID ddq335, pp. 4160–4175, 2010. View at Publisher · View at Google Scholar · View at Scopus
  25. D. Dormann, R. Rodde, D. Edbauer et al., “ALS-associated fused in sarcoma (FUS) mutations disrupt transportin-mediated nuclear import,” EMBO Journal, vol. 29, no. 16, pp. 2841–2857, 2010. View at Publisher · View at Google Scholar · View at Scopus
  26. J. Gal, J. Zhang, D. M. Kwinter et al., “Nuclear localization sequence of FUS and induction of stress granules by ALS mutants,” Neurobiology of Aging, vol. 32, no. 12, pp. 2323–e27, 2011. View at Publisher · View at Google Scholar · View at Scopus
  27. C. Vance, E. L. Scotter, A. L. Nishimura et al., “ALS mutant FUS disrupts nuclear localization and sequesters wild-type FUS within cytoplasmic stress granules,” Human Molecular Genetics, vol. 22, no. 13, pp. 2676–2688, 2013. View at Publisher · View at Google Scholar
  28. C.-K. Lii, A.-H. Lin, S.-L. Lee, H.-W. Chen, and T.-S. Wang, “Oxidative modifications of proteins by sodium arsenite in human umbilical vein endothelial cells,” Environmental Toxicology, vol. 26, no. 5, pp. 459–471, 2011. View at Publisher · View at Google Scholar · View at Scopus
  29. M. G. Thomas, L. J. M. Tosar, M. A. Desbats, C. C. Leishman, and G. L. Boccaccio, “Mammalian Staufen 1 is recruited to stress granules and impairs their assembly,” Journal of Cell Science, vol. 122, no. 4, pp. 563–573, 2009. View at Publisher · View at Google Scholar · View at Scopus
  30. J. Bieschke, J. Russ, R. P. Friedrich et al., “EGCG remodels mature α-synuclein and amyloid-β fibrils and reduces cellular toxicity,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 17, pp. 7710–7715, 2010. View at Publisher · View at Google Scholar · View at Scopus
  31. F. Meng, A. Abedini, A. Plesner, C. B. Verchere, and D. P. Raleigh, “The Flavanol (-)-epigallocatechin 3-gallate inhibits amyloid formation by islet amyloid polypeptide, disaggregates amyloid fibrils, and protects cultured cells against IAPP-induced toxicity,” Biochemistry, vol. 49, no. 37, pp. 8127–8133, 2010. View at Publisher · View at Google Scholar · View at Scopus
  32. G. Grelle, A. Otto, M. Lorenz, R. F. Frank, E. E. Wanker, and J. Bieschke, “Black tea theaflavins inhibit formation of toxic amyloid-β and α-synuclein fibrils,” Biochemistry, vol. 50, no. 49, pp. 10624–10636, 2011. View at Publisher · View at Google Scholar · View at Scopus
  33. D. E. Ehrnhoefer, M. Duennwald, P. Markovic et al., “Green tea (-)-epigallocatechin-gallate modulates early events in huntingtin misfolding and reduces toxicity in Huntington's disease models,” Human Molecular Genetics, vol. 15, no. 18, pp. 2743–2751, 2006. View at Publisher · View at Google Scholar · View at Scopus
  34. S. A. Mandel, T. Amit, L. Kalfon, L. Reznichenko, and M. B. H. Youdim, “Targeting multiple neurodegenerative diseases etiologies with multimodal-acting green tea catechins,” Journal of Nutrition, vol. 138, no. 8, pp. 1578S–1583S, 2008. View at Google Scholar · View at Scopus
  35. C. Vance, E. L. Scotter, A. L. Nishimura et al., “ALS mutant FUS disrupts nuclear localization and sequesters wild-type FUS within cytoplasmic stress granules,” Human Molecular Genetics, vol. 22, no. 13, pp. 2676–2688, 2013. View at Publisher · View at Google Scholar