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BioMed Research International
Volume 2015, Article ID 798489, 10 pages
http://dx.doi.org/10.1155/2015/798489
Research Article

N-(1-Pyrenyl) Maleimide Induces Bak Oligomerization and Mitochondrial Dysfunction in Jurkat Cells

1Department of Molecular and Cellular Biology, College of Medicine, Chang Gung University, Kwei-San, Tao-Yuan 333, Taiwan
2Health Sciences Research Institute and School of Natural Sciences, University of California, Merced, CA 95343, USA
3Institute of Biomedical Sciences, College of Medicine, Chang Gung University, Kwei-San, Tao-Yuan 333, Taiwan

Received 10 November 2014; Revised 20 December 2014; Accepted 20 December 2014

Academic Editor: Sergio Lavandero

Copyright © 2015 Pei-Rong Huang 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. G. Kroemer, L. Galluzzi, and C. Brenner, “Mitochondrial membrane permeabilization in cell death,” Physiological Reviews, vol. 87, no. 1, pp. 99–163, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  2. J. Estaquier, F. Vallette, J.-L. Vayssiere, and B. Mignotte, “The mitochondrial pathways of apoptosis,” Advances in Experimental Medicine and Biology, vol. 942, pp. 157–183, 2012. View at Publisher · View at Google Scholar · View at Scopus
  3. B. Leibowitz and J. Yu, “Mitochondrial signaling in cell death via the Bcl-2 family,” Cancer Biology & Therapy, vol. 9, no. 6, pp. 417–422, 2010. View at Publisher · View at Google Scholar · View at Scopus
  4. G. J. Griffiths, B. M. Corfe, P. Savory et al., “Cellular damage signals promote sequential changes at the N-terminus and BH-1 domain of the pro-apoptotic protein Bak,” Oncogene, vol. 20, no. 52, pp. 7668–7676, 2001. View at Publisher · View at Google Scholar · View at Scopus
  5. D. Westphal, G. Dewson, P. E. Czabotar, and R. M. Kluck, “Molecular biology of Bax and Bak activation and action,” Biochimica et Biophysica Acta: Molecular Cell Research, vol. 1813, no. 4, pp. 521–531, 2011. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  6. X. Wang, “The expanding role of mitochondria in apoptosis,” Genes and Development, vol. 15, no. 22, pp. 2922–2933, 2001. View at Google Scholar · View at Scopus
  7. S. W. G. Tait and D. R. Green, “Mitochondria and cell death: outer membrane permeabilization and beyond,” Nature Reviews Molecular Cell Biology, vol. 11, no. 9, pp. 621–632, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  8. J. M. Adams and S. Cory, “The Bcl-2 apoptotic switch in cancer development and therapy,” Oncogene, vol. 26, no. 9, pp. 1324–1337, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  9. M. Brown and L. D. Attardi, “The role of apoptosis in cancer development and treatment response,” Nature Reviews Cancer, vol. 5, no. 3, pp. 231–237, 2005. View at Publisher · View at Google Scholar · View at Scopus
  10. S. Fulda, “Evasion of apoptosis as a cellular stress response in cancer,” International Journal of Cell Biology, vol. 2010, Article ID 370835, 6 pages, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  11. P. R. Huang, Y. M. Yeh, and T. C. V. Wang, “Potent inhibition of human telomerase by helenalin,” Cancer Letters, vol. 227, no. 2, pp. 169–174, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  12. Y. J. Chen, W. Y. Sheng, P. R. Huang, and T. C. V. Wang, “Potent inhibition of human telomerase by U-73122,” Journal of Biomedical Science, vol. 13, no. 5, pp. 667–674, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  13. P.-R. Huang, Y.-M. Yeh, C.-C. Pao, C.-Y. Chen, and T.-C. V. Wang, “N-(1-Pyrenyl) maleimide inhibits telomerase activity in a cell free system and induces apoptosis in Jurkat cells,” Molecular Biology Reports, vol. 39, no. 9, pp. 8899–8905, 2012. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  14. M. E. Shawgo, S. N. Shelton, and J. D. Robertson, “Caspase-mediated bak activation and cytochrome c release during intrinsic apoptotic cell death in jurkat cells,” Journal of Biological Chemistry, vol. 283, no. 51, pp. 35532–35538, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  15. C. C. Yu, S. C. Lo, and T. C. V. Wang, “Telomerase is regulated by protein kinase C-zeta in human nasopharyngeal cancer cells,” Biochemical Journal, vol. 355, no. 2, pp. 459–464, 2001. View at Publisher · View at Google Scholar · View at Scopus
  16. P. E. Czabotar, D. Westphal, G. Dewson et al., “Bax crystal structures reveal how BH3 domains activate Bax and nucleate its oligomerization to induce apoptosis,” Cell, vol. 152, no. 3, pp. 519–531, 2013. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  17. T. Moldoveanu, C. R. Grace, F. Llambi et al., “BID-induced structural changes in BAK promote apoptosis,” Nature Structural and Molecular Biology, vol. 20, no. 5, pp. 589–597, 2013. View at Publisher · View at Google Scholar · View at Scopus
  18. M. Brimmell, R. Mendiola, J. Mangion, and G. Packham, “BAX frameshift mutations in cell lines derived from human haemopoietic malignancies are associated with resistance to apoptosis and microsatellite instability,” Oncogene, vol. 16, no. 14, pp. 1803–1812, 1998. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  19. R. A. Winters, J. Zukowski, N. Ercal, R. H. Matthews, and D. R. Spitz, “Analysis of glutathione, glutathione disulfide, cysteine, homocysteine, and other biological thiols by high-performance liquid chromatography following derivatization by n-(1-Pyrenyl)maleimide,” Analytical Biochemistry, vol. 227, no. 1, pp. 14–21, 1995. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  20. W. Wu, G. Goldstein, C. Adams, R. H. Matthews, and N. Ercal, “Separation and quantification of N-acetyl-L-cysteine and N-acetyl-cysteine-amide by HPLC with fluorescence detection,” Biomedical Chromatography, vol. 20, no. 5, pp. 415–422, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  21. S. H. Kaufmann and W. C. Earnshaw, “Induction of apoptosis by cancer chemotherapy,” Experimental Cell Research, vol. 256, no. 1, pp. 42–49, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  22. G. Dewson, T. Kratina, H. W. Sim et al., “To trigger apoptosis, bak exposes its BH3 domain and homodimerizes via BH3: groove interactions,” Molecular Cell, vol. 30, no. 3, pp. 369–380, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  23. G. Dewson, T. Kratina, P. Czabotar, C. L. Day, J. M. Adams, and R. M. Kluck, “Bak activation for apoptosis involves oligomerization of dimers via their alpha6 helices,” Molecular Cell, vol. 36, no. 4, pp. 696–703, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  24. A. G. Letai, “Diagnosing and exploiting cancer's addiction to blocks in apoptosis,” Nature Reviews Cancer, vol. 8, no. 2, pp. 121–132, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus