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Journal of Ophthalmology
Volume 2016, Article ID 6392658, 11 pages
http://dx.doi.org/10.1155/2016/6392658
Research Article

SENP1-Mediated Desumoylation of DBC1 Inhibits Apoptosis Induced by High Glucose in Bovine Retinal Pericytes

Department of Ophthalmology, Shanghai First People’s Hospital, Shanghai Jiao Tong University, School of Medicine, Shanghai 200080, China

Received 13 December 2015; Revised 23 February 2016; Accepted 2 March 2016

Academic Editor: Jesús Pintor

Copyright © 2016 Jian Gao 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. Diabetic Retinopathy Clinical Research Network, J. A. Wells, A. R. Glassman et al., “Aflibercept, bevacizumab, or ranibizumab for diabetic macular edema,” The New England Journal of Medicine, vol. 372, no. 13, pp. 1193–1203, 2015. View at Publisher · View at Google Scholar
  2. Y.-J. Hsu, Y.-T. Hsieh, P.-T. Yeh, J.-Y. Huang, and C.-M. Yang, “Combined tractional and rhegmatogenous retinal detachment in proliferative diabetic retinopathy in the anti-VEGF era,” Journal of Ophthalmology, vol. 2014, Article ID 917375, 11 pages, 2014. View at Publisher · View at Google Scholar · View at Scopus
  3. H.-P. Hammes, J. Lin, O. Renner et al., “Pericytes and the pathogenesis of diabetic retinopathy,” Diabetes, vol. 51, no. 10, pp. 3107–3112, 2002. View at Publisher · View at Google Scholar · View at Scopus
  4. N. M. Mustapha, J. M. Tarr, E. M. Kohner et al., “NADPH oxidase versus mitochondria-derived ros in glucose-induced apoptosis of pericytes in early diabetic retinopathy,” Journal of Ophthalmology, vol. 2010, Article ID 746978, 10 pages, 2010. View at Publisher · View at Google Scholar
  5. C. M. Hickey, N. R. Wilson, and M. Hochstrasser, “Function and regulation of SUMO proteases,” Nature Reviews Molecular Cell Biology, vol. 13, no. 12, pp. 755–766, 2012. View at Publisher · View at Google Scholar · View at Scopus
  6. J. B. Hoppe, C. G. Salbego, and H. Cimarosti, “SUMOylation: novel neuroprotective approach for Alzheimer’s disease?” Aging and Disease, vol. 6, no. 5, pp. 322–330, 2015. View at Publisher · View at Google Scholar
  7. R. Geiss-Friedlander and F. Melchior, “Concepts in sumoylation: a decade on,” Nature Reviews Molecular Cell Biology, vol. 8, no. 12, pp. 947–956, 2007. View at Publisher · View at Google Scholar · View at Scopus
  8. J. Cheng, X. Kang, S. Zhang, and E. T. H. Yeh, “SUMO-specific protease 1 is essential for stabilization of HIF1α during hypoxia,” Cell, vol. 131, no. 3, pp. 584–595, 2007. View at Publisher · View at Google Scholar · View at Scopus
  9. Z. Xu, H. Y. Chan, W. L. Lam et al., “SUMO proteases: redox regulation and biological consequences,” Antioxidants and Redox Signaling, vol. 11, no. 6, pp. 1453–1484, 2009. View at Publisher · View at Google Scholar · View at Scopus
  10. Z. Jiang, Q. Fan, Z. Zhang et al., “SENP1 deficiency promotes ER stress-induced apoptosis by increasing XBP1 SUMOylation,” Cell Cycle, vol. 11, no. 6, pp. 1118–1122, 2012. View at Publisher · View at Google Scholar · View at Scopus
  11. J. Xu, H.-Y. Sun, F.-J. Xiao et al., “SENP1 inhibition induces apoptosis and growth arrest of multiple myeloma cells through modulation of NF-κB signaling,” Biochemical and Biophysical Research Communications, vol. 460, no. 2, pp. 409–415, 2015. View at Publisher · View at Google Scholar · View at Scopus
  12. B. Qin, K. Minter-Dykhouse, J. Yu et al., “DBC1 functions as a tumor suppressor by regulating p53 stability,” Cell Reports, vol. 10, no. 8, pp. 1324–1334, 2015. View at Publisher · View at Google Scholar · View at Scopus
  13. J. H. Park, S. W. Lee, S. W. Yang et al., “Modification of DBC1 by SUMO2/3 is crucial for p53-mediated apoptosis in response to DNA damage,” Nature Communications, vol. 5, article 5483, 2014. View at Publisher · View at Google Scholar · View at Scopus
  14. J. F. Arboleda-Velasquez, V. Primo, M. Graham, A. James, J. Manent, and P. A. D'Amore, “Notch signaling functions in retinal pericyte survival,” Investigative Ophthalmology & Visual Science, vol. 55, no. 8, pp. 5191–5199, 2014. View at Publisher · View at Google Scholar · View at Scopus
  15. C. A. Schneider, W. S. Rasband, and K. W. Eliceiri, “NIH Image to ImageJ: 25 years of image analysis,” Nature Methods, vol. 9, no. 7, pp. 671–675, 2012. View at Publisher · View at Google Scholar · View at Scopus
  16. B. A. Bryan and P. A. Damore, “Pericyte isolation and use in endothelial/pericyte coculture models,” Methods Enzymol, vol. 443, no. 8, pp. 315–331, 2008. View at Publisher · View at Google Scholar
  17. M. Wu, S. Yang, M. H. Elliott et al., “Oxidative and endoplasmic reticulum stresses mediate apoptosis induced by modified LDL in human retinal Müller cells,” Investigative Ophthalmology and Visual Science, vol. 53, no. 8, pp. 4595–4604, 2012. View at Publisher · View at Google Scholar · View at Scopus
  18. L. Chen, Y. Tao, J. Feng, and Y. R. Jiang, “Apelin protects primary rat retinal pericytes from chemical hypoxia-induced apoptosis,” Journal of Ophthalmology, vol. 2015, Article ID 186946, 14 pages, 2015. View at Publisher · View at Google Scholar · View at Scopus
  19. S. W. Lee, M. H. Lee, J. H. Park et al., “SUMOylation of hnRNP-K is required for p53-mediated cell-cycle arrest in response to DNA damage,” The EMBO Journal, vol. 31, no. 23, pp. 4441–4452, 2012. View at Publisher · View at Google Scholar · View at Scopus
  20. M. Sacher, B. Pfander, C. Hoege, and S. Jentsch, “Control of Rad52 recombination activity by double-strand break-induced SUMO modification,” Nature Cell Biology, vol. 8, no. 11, pp. 1284–1290, 2006. View at Publisher · View at Google Scholar · View at Scopus
  21. A. M. Andreou and N. Tavernarakis, “SUMOylation and cell signalling,” Biotechnology Journal, vol. 4, no. 12, pp. 1740–1752, 2009. View at Publisher · View at Google Scholar · View at Scopus
  22. M. Drag and G. S. Salvesen, “DeSUMOylating enzymes—SENPs,” IUBMB Life, vol. 60, no. 11, pp. 734–742, 2008. View at Publisher · View at Google Scholar · View at Scopus
  23. F. A. Khan, N. S. Pandupuspitasari, C.-J. Huang, X. Hao, and S. Zhang, “SUMOylation: a link to future therapeutics,” Current Issues in Molecular Biology, vol. 18, no. 1, pp. 49–56, 2016. View at Google Scholar · View at Scopus
  24. L. Shao, H. J. Zhou, H. Zhang et al., “SENP1-mediated NEMO deSUMOylation in adipocytes limits inflammatory responses and type-1 diabetes progression,” Nature Communications, vol. 6, article 8917, 2015. View at Publisher · View at Google Scholar
  25. L. Zannini, G. Buscemi, J.-E. Kim, E. Fontanella, and D. Delia, “DBC1 phosphorylation by ATM/ATR inhibits SIRT1 deacetylase in response to DNA damage,” Journal of Molecular Cell Biology, vol. 4, no. 5, pp. 294–303, 2012. View at Publisher · View at Google Scholar · View at Scopus
  26. C. C. S. Chini, C. Escande, V. Nin, and E. N. Chini, “HDAC3 is negatively regulated by the nuclear protein DBC1,” The Journal of Biological Chemistry, vol. 285, no. 52, pp. 40830–40837, 2010. View at Publisher · View at Google Scholar · View at Scopus
  27. E. N. Chini, C. C. S. Chini, V. Nin, and C. Escande, “Deleted in breast cancer-1 (DBC-1) in the interface between metabolism, aging and cancer,” Bioscience Reports, vol. 33, no. 4, pp. 637–643, 2013. View at Publisher · View at Google Scholar · View at Scopus