Table of Contents Author Guidelines Submit a Manuscript
Parkinson’s Disease
Volume 2016, Article ID 6163934, 9 pages
http://dx.doi.org/10.1155/2016/6163934
Research Article

Deletion of Herpud1 Enhances Heme Oxygenase-1 Expression in a Mouse Model of Parkinson’s Disease

1Department of Neuroanatomy, Kanazawa University Graduate School of Medical Science, Kanazawa, Ishikawa 920-8640, Japan
2CREST, JST (Japan Science and Technology), Tokyo 102-8666, Japan
3Department of Molecular Pathogenesis, National Cerebral and Cardiovascular Center, Osaka 565-8565, Japan

Received 21 November 2015; Revised 25 January 2016; Accepted 28 January 2016

Academic Editor: Antonio Pisani

Copyright © 2016 Thuong Manh Le 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. W. Dauer and S. Przedborski, “Parkinson's disease: mechanisms and models,” Neuron, vol. 39, no. 6, pp. 889–909, 2003. View at Publisher · View at Google Scholar · View at Scopus
  2. M. Schröder and R. J. Kaufman, “The mammalian unfolded protein response,” Annual Review of Biochemistry, vol. 74, pp. 739–789, 2005. View at Publisher · View at Google Scholar · View at Scopus
  3. B. Thomas and M. F. Beal, “Parkinson's disease,” Human Molecular Genetics, vol. 16, no. 2, pp. R183–R194, 2007. View at Publisher · View at Google Scholar · View at Scopus
  4. E. J. Ryu, H. P. Harding, J. M. Angelastro, O. V. Vitolo, D. Ron, and L. A. Greene, “Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease,” The Journal of Neuroscience, vol. 22, no. 24, pp. 10690–10698, 2002. View at Google Scholar · View at Scopus
  5. W. A. Holtz, J. M. Turetzky, Y.-J. I. Jong, and K. L. O'Malley, “Oxidative stress-triggered unfolded protein response is upstream of intrinsic cell death evoked by parkinsonian mimetics,” Journal of Neurochemistry, vol. 99, no. 1, pp. 54–69, 2006. View at Publisher · View at Google Scholar · View at Scopus
  6. C. Zhou, Y. Huang, and S. Przedborski, “Oxidative stress in Parkinson's disease: a mechanism of pathogenic and therapeutic significance,” Annals of the New York Academy of Sciences, vol. 1147, pp. 93–104, 2008. View at Publisher · View at Google Scholar · View at Scopus
  7. W. W. Smith, H. Jiang, Z. Pei et al., “Endoplasmic reticulum stress and mitochondrial cell death pathways mediate A53T mutant alpha-synuclein-induced toxicity,” Human Molecular Genetics, vol. 14, no. 24, pp. 3801–3811, 2005. View at Publisher · View at Google Scholar · View at Scopus
  8. D. D. Song, C. W. Shults, A. Sisk, E. Rockenstein, and E. Masliah, “Enhanced substantia nigra mitochondrial pathology in human α-synuclein transgenic mice after treatment with MPTP,” Experimental Neurology, vol. 186, no. 2, pp. 158–172, 2004. View at Publisher · View at Google Scholar · View at Scopus
  9. P. Klivenyi, D. Siwek, G. Gardian et al., “Mice lacking alpha-synuclein are resistant to mitochondrial toxins,” Neurobiology of Disease, vol. 21, no. 3, pp. 541–548, 2006. View at Publisher · View at Google Scholar · View at Scopus
  10. M. Nieto, F. J. Gil-Bea, E. Dalfó et al., “Increased sensitivity to MPTP in human α-synuclein A30P transgenic mice,” Neurobiology of Aging, vol. 27, no. 6, pp. 848–856, 2006. View at Publisher · View at Google Scholar · View at Scopus
  11. Y. Imai, M. Soda, H. Inoue, N. Hattori, Y. Mizuno, and R. Takahashi, “An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin,” Cell, vol. 105, no. 7, pp. 891–902, 2001. View at Publisher · View at Google Scholar · View at Scopus
  12. Y. Kitao, Y. Imai, K. Ozawa et al., “Pael receptor induces death of dopaminergic neurons in the substantia nigra via endoplasmic reticulum stress and dopamine toxicity, which is enhanced under condition of parkin inactivation,” Human Molecular Genetics, vol. 16, no. 1, pp. 50–60, 2007. View at Publisher · View at Google Scholar · View at Scopus
  13. K. Kokame, K. L. Agarwal, H. Kato, and T. Miyata, “Herp, a new ubiquitin-like membrane protein induced by endoplasmic reticulum stress,” The Journal of Biological Chemistry, vol. 275, no. 42, pp. 32846–32853, 2000. View at Publisher · View at Google Scholar · View at Scopus
  14. X. Sai, Y. Kawamur, K. Kokame et al., “Endoplasmic reticulum stress-inducible protein, Herp, enhances presenilin-mediated generation of amyloid β-protein,” The Journal of Biological Chemistry, vol. 277, no. 15, pp. 12915–12920, 2002. View at Publisher · View at Google Scholar · View at Scopus
  15. O. Hori, F. Ichinoda, A. Yamaguchi et al., “Role of Herp in the endoplasmic reticulum stress response,” Genes to Cells, vol. 9, no. 5, pp. 457–469, 2004. View at Publisher · View at Google Scholar · View at Scopus
  16. Y. Okuda-Shimizu and L. M. Hendershot, “Characterization of an ERAD pathway for nonglycosylated BiP substrates, which require Herp,” Molecular Cell, vol. 28, no. 4, pp. 544–554, 2007. View at Publisher · View at Google Scholar · View at Scopus
  17. T.-Y. Kim, E. Kim, S. K. Yoon, and J.-B. Yoon, “Herp enhances ER-associated protein degradation by recruiting ubiquilins,” Biochemical and Biophysical Research Communications, vol. 369, no. 2, pp. 741–746, 2008. View at Publisher · View at Google Scholar · View at Scopus
  18. A. Schulze, S. Standera, E. Buerger et al., “The ubiquitin-domain protein HERP forms a complex with components of the endoplasmic reticulum associated degradation pathway,” Journal of Molecular Biology, vol. 354, no. 5, pp. 1021–1027, 2005. View at Publisher · View at Google Scholar · View at Scopus
  19. H. Slodzinski, L. B. Moran, G. J. Michael et al., “Homocysteine-induced endoplasmic reticulum protein (Herp) is up-regulated in parkinsonian substantia nigra and present in the core of Lewy bodies,” Clinical Neuropathology, vol. 28, no. 5, pp. 333–343, 2009. View at Publisher · View at Google Scholar · View at Scopus
  20. S. Chigurupati, Z. Wei, C. Belal et al., “The homocysteine-inducible endoplasmic reticulum stress protein counteracts calcium store depletion and induction of CCAAT enhancer-binding protein homologous protein in a neurotoxin model of Parkinson Disease,” The Journal of Biological Chemistry, vol. 284, no. 27, pp. 18323–18333, 2009. View at Publisher · View at Google Scholar · View at Scopus
  21. C. Belal, N. J. Ameli, A. El kommos et al., “The homocysteine-inducible endoplasmic reticulum (ER) stress protein herp counteracts mutant α-synuclein-induced ER stress via the homeostatic regulation of ER-resident calcium release channel proteins,” Human Molecular Genetics, vol. 21, no. 5, pp. 963–977, 2012. View at Publisher · View at Google Scholar · View at Scopus
  22. H. Miura, K. Hashida, H. Sudo et al., “Deletion of Herp facilitates degradation of cytosolic proteins,” Genes to Cells, vol. 15, no. 8, pp. 843–853, 2010. View at Publisher · View at Google Scholar · View at Scopus
  23. C. Quiroga, D. Gatica, F. Paredes et al., “Herp depletion protects from protein aggregation by up-regulating autophagy,” Biochimica et Biophysica Acta—Molecular Cell Research, vol. 1833, no. 12, pp. 3295–3305, 2013. View at Publisher · View at Google Scholar · View at Scopus
  24. Y. Eura, H. Yanamoto, Y. Arai, T. Okuda, T. Miyata, and K. Kokame, “Derlin-1 deficiency is embryonic lethal, derlin-3 deficiency appears normal, and herp deficiency is intolerant to glucose load and ischemia in mice,” PLoS ONE, vol. 7, no. 3, Article ID e34298, 2012. View at Publisher · View at Google Scholar · View at Scopus
  25. K. Kühn, J. Wellen, N. Link, L. Maskri, H. Lübbert, and C. C. Stichel, “The mouse MPTP model: gene expression changes in dopaminergic neurons,” The European Journal of Neuroscience, vol. 17, no. 1, pp. 1–12, 2003. View at Publisher · View at Google Scholar · View at Scopus
  26. O. Hori, M. Matsumoto, Y. Maeda et al., “Metabolic and biosynthetic alterations in cultured astrocytes exposed to hypoxia/reoxygenation,” Journal of Neurochemistry, vol. 62, no. 4, pp. 1489–1495, 1994. View at Google Scholar · View at Scopus
  27. K. Hashida, Y. Kitao, H. Sudo et al., “ATF6alpha promotes astroglial activation and neuronal survival in a chronic mouse model of Parkinson's disease,” PLoS ONE, vol. 7, no. 10, Article ID e47950, 2012. View at Publisher · View at Google Scholar · View at Scopus
  28. Y. Kitao, K. Hashimoto, T. Matsuyama et al., “ORP150/HSP12A regulates Purkinje cell survival: a role for endoplasmic reticulum stress in cerebellar development,” The Journal of Neuroscience, vol. 24, no. 6, pp. 1486–1496, 2004. View at Publisher · View at Google Scholar · View at Scopus
  29. N. Egawa, K. Yamamoto, H. Inoue et al., “The endoplasmic reticulum stress sensor, ATF6α, protects against neurotoxin-induced dopaminergic neuronal death,” The Journal of Biological Chemistry, vol. 286, no. 10, pp. 7947–7957, 2011. View at Publisher · View at Google Scholar · View at Scopus
  30. W. A. Holtz and K. L. O'Malley, “Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons,” The Journal of Biological Chemistry, vol. 278, no. 21, pp. 19367–19377, 2003. View at Publisher · View at Google Scholar · View at Scopus
  31. K. Kokame, H. Kato, and T. Miyata, “Identification of ERSE-II, a new cis-acting element responsible for the ATF6-dependent mammalian unfolded protein response,” The Journal of Biological Chemistry, vol. 276, no. 12, pp. 9199–9205, 2001. View at Publisher · View at Google Scholar · View at Scopus
  32. H. M. Schipper, “Heme oxygenase-1: role in brain aging and neurodegeneration,” Experimental Gerontology, vol. 35, no. 6-7, pp. 821–830, 2000. View at Publisher · View at Google Scholar · View at Scopus
  33. H. M. Schipper, W. Song, H. Zukor, J. R. Hascalovici, and D. Zeligman, “Heme oxygenase-1 and neurodegeneration: expanding frontiers of engagement,” Journal of Neurochemistry, vol. 110, no. 2, pp. 469–485, 2009. View at Publisher · View at Google Scholar · View at Scopus
  34. W. Song, H. Zukor, S.-H. Lin et al., “Unregulated brain iron deposition in transgenic mice over-expressing HMOX1 in the astrocytic compartment,” Journal of Neurochemistry, vol. 123, no. 2, pp. 325–336, 2012. View at Publisher · View at Google Scholar · View at Scopus
  35. E. Csongradi, T. Vera, J. M. Rimoldi, R. S. V. Gadepalli, and D. E. Stec, “In vivo inhibition of renal heme oxygenase with an imidazole-dioxolane inhibitor,” Pharmacological Research, vol. 61, no. 6, pp. 525–530, 2010. View at Publisher · View at Google Scholar · View at Scopus