Table of Contents Author Guidelines Submit a Manuscript
International Journal of Cell Biology
Volume 2012, Article ID 273549, 9 pages
http://dx.doi.org/10.1155/2012/273549
Research Article

S-Glutathionylation of Protein Disulfide Isomerase Regulates Estrogen Receptor Stability and Function

1Department of Cell and Molecular Pharmacology and Experimental Therapeutics, Medical University of South Carolina, Charleston, SC 29425, USA
2Department of Pharmaceutical and Biomedical Sciences, Medical University of South Carolina, Charleston, SC 29425, USA

Received 16 February 2012; Accepted 6 March 2012

Academic Editor: Giuseppe Filomeni

Copyright © 2012 Ying Xiong 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. K. D. Tew, “Glutathione-associated enzymes in anticancer drug resistance,” Cancer Research, vol. 54, no. 16, pp. 4313–4320, 1994. View at Google Scholar · View at Scopus
  2. D. M. Townsend, V. L. Findlay, and K. D. Tew, “Glutathione S-transferases as regulators of kinase pathways and anticancer drug targets,” Methods in Enzymology, vol. 401, article 19, pp. 287–307, 2005. View at Publisher · View at Google Scholar · View at Scopus
  3. Y. Xiong, J. D. Uys, K. D. Tew, and D. M. Townsend, “S-glutathionylation: from molecular mechanisms to health outcomes,” Antioxidants and Redox Signaling, vol. 15, no. 1, pp. 233–270, 2011. View at Publisher · View at Google Scholar · View at Scopus
  4. K. D. Tew, “TLK-286: a novel glutathione S-transferase-activated prodrug,” Expert Opinion on Investigational Drugs, vol. 14, no. 8, pp. 1047–1054, 2005. View at Publisher · View at Google Scholar · View at Scopus
  5. D. M. Townsend, V. J. Findlay, F. Fazilev et al., “A glutathione S-transferase pi-activated prodrug causes kinase activation concurrent with S-glutathionylation of proteins,” Molecular Pharmacology, vol. 69, no. 2, pp. 501–508, 2006. View at Publisher · View at Google Scholar · View at Scopus
  6. D. M. Townsend, “S-glutathionylation: indicator of cell stress and regulator of the unfolded protein response,” Molecular Interventions, vol. 7, no. 6, pp. 313–324, 2008. View at Publisher · View at Google Scholar · View at Scopus
  7. J. E. Saavedra, A. Srinivasan, G. S. Buzard et al., “PABA/NO as an anticancer lead: analogue synthesis, structure revision, solution chemistry, reactivity toward glutathione, and in vitro activity,” Journal of Medicinal Chemistry, vol. 49, no. 3, pp. 1157–1164, 2006. View at Publisher · View at Google Scholar · View at Scopus
  8. D. M. Townsend, Y. Manevich, H. Lin et al., “Nitrosative stress-induced S-glutathionylation of protein disulfide isomerase leads to activation of the unfolded protein response,” Cancer Research, vol. 69, no. 19, pp. 7626–7634, 2009. View at Publisher · View at Google Scholar · View at Scopus
  9. J. D. Uys, Y. Xiong, and D. M. Townsend, “Nitrosative stress-induced S-glutathionylation of protein disulfide isomerase,” Methods in Enzymology, vol. 490, pp. 321–332, 2011. View at Publisher · View at Google Scholar · View at Scopus
  10. X. Fu, P. Wang, and B. T. Zhu, “Protein disulfide isomerase is a multifunctional regulator of estrogenic status in target cells,” Journal of Steroid Biochemistry and Molecular Biology, vol. 112, no. 1–3, pp. 127–137, 2008. View at Publisher · View at Google Scholar · View at Scopus
  11. C. Turano, S. Coppari, F. Altieri, and A. Ferraro, “Proteins of the PDI family: unpredicted non-ER locations and functions,” Journal of Cellular Physiology, vol. 193, no. 2, pp. 154–163, 2002. View at Publisher · View at Google Scholar · View at Scopus
  12. C. C. Landel, P. J. Kushner, and G. L. Greene, “The interaction of human estrogen receptor with DNA is modulated by receptor-associated proteins,” Molecular Endocrinology, vol. 8, no. 10, pp. 1407–1419, 1994. View at Publisher · View at Google Scholar · View at Scopus
  13. J. R. Schultz-Norton, W. H. McDonald, J. R. Yates, and A. M. Nardulli, “Protein disulfide isomerase serves as a molecular chaperone to maintain estrogen receptor α structure and function,” Molecular Endocrinology, vol. 20, no. 9, pp. 1982–1995, 2006. View at Publisher · View at Google Scholar · View at Scopus
  14. T. Mosmann, “Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays,” Journal of Immunological Methods, vol. 65, no. 1-2, pp. 55–63, 1983. View at Google Scholar · View at Scopus
  15. T. Uehara, T. Nakamura, D. Yao et al., “S-Nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration,” Nature, vol. 441, no. 7092, pp. 513–517, 2006. View at Publisher · View at Google Scholar · View at Scopus
  16. D. M. Townsend, Y. Manevich, L. He, S. Hutchens, C. J. Pazoles, and K. D. Tew, “Novel role for glutathione S-transferase pi. Regulator of protein S-glutathionylation following oxidative and nitrosative stress,” The Journal of Biological Chemistry, vol. 284, no. 1, pp. 436–445, 2009. View at Publisher · View at Google Scholar · View at Scopus
  17. A. Holmgren, “Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide,” The Journal of Biological Chemistry, vol. 254, no. 19, pp. 9627–9632, 1979. View at Google Scholar · View at Scopus
  18. V. J. Findlay, D. M. Townsend, J. E. Saavedra et al., “Tumor cell responses to a novel glutathione S-transferase-activated nitric oxide-releasing prodrug,” Molecular Pharmacology, vol. 65, no. 5, pp. 1070–1079, 2004. View at Publisher · View at Google Scholar · View at Scopus
  19. S. Hutchens, Y. Manevich, L. He, K. D. Tew, and D. M. Townsend, “Cellular resistance to a nitric oxide releasing glutathione S-transferase P-activated prodrug, PABA/NO,” Investigational New Drugs, vol. 29, no. 5, pp. 719–729, 2010. View at Publisher · View at Google Scholar · View at Scopus
  20. Y. Manevich, D. M. Townsend, S. Hutchens, and K. D. Tew, “Diazeniumdiolate mediated nitrosative stress alters nitric oxide homeostasis through intracellular calcium and s-glutathionylation of nitric oxide synthetase,” PLoS ONE, vol. 5, no. 11, Article ID e14151, 2010. View at Publisher · View at Google Scholar · View at Scopus
  21. J. C. M. Tsibris, L. T. Hunt, G. Ballejo, W. C. Barker, L. J. Toney, and W. N. Spellacy, “Selective inhibition of protein disulfide isomerase by estrogens,” The Journal of Biological Chemistry, vol. 264, no. 24, pp. 13967–13970, 1989. View at Google Scholar · View at Scopus
  22. F. Hatahet and L. W. Ruddock, “Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation,” Antioxidants and Redox Signaling, vol. 11, no. 11, pp. 2807–2850, 2009. View at Publisher · View at Google Scholar · View at Scopus
  23. G. Tian, S. Xiang, R. Noiva, W. J. Lennarz, and H. Schindelin, “The crystal structure of yeast protein disulfide isomerase suggests cooperativity between its active sites,” Cell, vol. 124, no. 1, pp. 61–73, 2006. View at Publisher · View at Google Scholar · View at Scopus