International Journal of Cell Biology
Volume 2010 (2010), Article ID 214074, 23 pages
doi:10.1155/2010/214074
Review Article

Cellular Stress Responses: Cell Survival and Cell Death

Simone Fulda,1 Adrienne M. Gorman,2 Osamu Hori,3 and Afshin Samali2

1Children's Hospital, Ulm University, Eythstraße. 24, 89075 Ulm, Germany
2School of Natural Sciences, National University of Ireland, Galway, University Road, Galway, Ireland
3Kanazawa University Graduate School of Medical Science, Department of Neuroanatomy, Kanazawa City, Ishikawa, 920-8640 Japan, Japan

Received 4 August 2009; Accepted 20 November 2009

Academic Editor: Srinivasa M. Srinivasula

Copyright © 2010 Simone Fulda 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. R. A. Lockshin and Z. Zakeri, “Programmed cell death and apoptosis: origins of the theory,” Nature Reviews Molecular Cell Biology, vol. 2, no. 7, pp. 545–550, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  2. R. A. Lockshin and C. M. Williams, “Programmed cell death—I. Cytology of degeneration in the intersegmental muscles of the Pernyi silkmoth,” Journal of Insect Physiology, vol. 11, no. 2, pp. 123–133, 1965. View at Scopus
  3. R. A. Lockshin and C. M. Williams, “Programmed cell death—IV. The influence of drugs on the breakdown of the intersegmental muscles of silkmoths,” Journal of Insect Physiology, vol. 11, no. 6, pp. 803–809, 1965. View at Scopus
  4. R. A. Lockshin and C. M. Williams, “Programmed cell death—V. Cytolytic enzymes in relation to the breakdown of the intersegmental muscles of silkmoths,” Journal of Insect Physiology, vol. 11, no. 7, pp. 831–844, 1965. View at Scopus
  5. B. M. Pützer, “E2F1 death pathways as targets for cancer therapy,” Journal of Cellular and Molecular Medicine, vol. 11, no. 2, pp. 239–251, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  6. J. L. V. Reeve, A. M. Duffy, T. O'Brien, and A. Samali, “Don't lose heart—therapeutic value of apoptosis prevention in the treatment of cardiovascular disease,” Journal of Cellular and Molecular Medicine, vol. 9, no. 3, pp. 609–622, 2005. View at Scopus
  7. A. Samali, “A tribute to professor Richard A. Lockshin on his 70th birthday,” Journal of Cellular and Molecular Medicine, vol. 11, no. 6, pp. 1210–1211, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  8. Z. Zakeri, W. Bursch, M. Tenniswood, and R. A. Lockshin, “Cell death: programmed, apoptosis, necrosis, or other?” Cell Death and Differentiation, vol. 2, no. 2, pp. 87–96, 1995. View at Scopus
  9. J. F. Kerr, A. H. Wyllie, and A. R. Currie, “Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics,” British Journal of Cancer, vol. 26, no. 4, pp. 239–257, 1972. View at Scopus
  10. J. F. Kerr, “Shrinkage necrosis: a distinct mode of cellular death,” Journal of Pathology, vol. 105, no. 1, pp. 13–20, 1971. View at Scopus
  11. B. F. Trump, P. J. Goldblatt, and R. E. Stowell, “An electron microscopic study of early cytoplasmic alterations in hepatic parenchymal cells of mouse liver during necrosis in vitro (autolysis),” Laboratory Investigation, vol. 11, pp. 986–1015, 1962.
  12. M. Berenbom, P. I. Chang, H. E. Betz, and R. E. Stowell, “Chemical and enzymatic changes associated with mouse liver necrosis in vitro,” Cancer Research, vol. 15, no. 1, pp. 1–5, 1955.
  13. B. C. Trauth, C. Klas, A. M. J. Peters, et al., “Monoclonal antibody-mediated tumor regression by induction of apoptosis,” Science, vol. 245, no. 4915, pp. 301–305, 1989. View at Scopus
  14. J. Yang, X. Liu, K. Bhalla, et al., “Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked,” Science, vol. 275, no. 5303, pp. 1129–1132, 1997. View at Publisher · View at Google Scholar · View at Scopus
  15. D. L. Vaux, S. Cory, and J. M. Adams, “Bcl-2 gene promotes haemopoietic cell survival and cooperates with c-myc to immortalize pre-B cells,” Nature, vol. 335, no. 6189, pp. 440–442, 1988. View at Scopus
  16. D. Hockenbery, G. Nunez, C. Milliman, R. D. Schreiber, and S. J. Korsmeyer, “Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death,” Nature, vol. 348, no. 6299, pp. 334–336, 1990. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  17. N. Itoh, S. Yonehara, A. Ishii, et al., “The polypeptide encoded by the cDNA for human cell surface antigen fas can mediate apoptosis,” Cell, vol. 66, no. 2, pp. 233–243, 1991. View at Scopus
  18. J. Yuan, S. Shaham, S. Ledoux, H. M. Ellis, and H. R. Horvitz, “The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme,” Cell, vol. 75, no. 4, pp. 641–652, 1993. View at Publisher · View at Google Scholar · View at Scopus
  19. R. M. Kluck, E. Bossy-Wetzel, D. R. Green, and D. D. Newmeyer, “The release of cytochrome c from mitochondria: a primary site for Bcl- 2 regulation of apoptosis,” Science, vol. 275, no. 5303, pp. 1132–1136, 1997. View at Publisher · View at Google Scholar · View at Scopus
  20. E. Szegezdi, S. E. Logue, A. M. Gorman, and A. Samali, “Mediators of endoplasmic reticulum stress-induced apoptosis,” EMBO Reports, vol. 7, no. 9, pp. 880–885, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  21. A. Samali, B. Zhivotovsky, D. Jones, S. Nagata, and S. Orrenius, “Apoptosis: cell death defined by caspase activation,” Cell Death and Differentiation, vol. 6, no. 6, pp. 495–496, 1999. View at Scopus
  22. R. A. Lockshin and Z. Zakeri, “Cell death in health and disease,” Journal of Cellular & Molecular Medicine, vol. 11, no. 6, pp. 1214–1224, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  23. A. Samali, A. M. Gorman, and T. G. Cotter, “Apoptosis—the story so far,” Experientia, vol. 52, no. 10-11, pp. 933–941, 1996. View at Scopus
  24. R. T. Bree, C. Stenson-Cox, M. Grealy, L. Byrnes, A. M. Gorman, and A. Samali, “Cellular longevity: role of apoptosis and replicative senescence,” Biogerontology, vol. 3, no. 4, pp. 195–206, 2002. View at Publisher · View at Google Scholar · View at Scopus
  25. A. Degterev, M. Boyce, and J. Yuan, “A decade of caspases,” Oncogene, vol. 22, no. 53, pp. 8543–8567, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  26. A. Ashkenazi, “Targeting the extrinsic apoptosis pathway in cancer,” Cytokine and Growth Factor Reviews, vol. 19, no. 3-4, pp. 325–331, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  27. A. Samali, “Apoptosis: a mapped path to cell death,” Journal of Cellular and Molecular Medicine, vol. 11, no. 6, pp. 1212–1213, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  28. 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
  29. H. Zou, Y. Li, X. Liu, and X. Wang, “An APAf-1· cytochrome C multimeric complex is a functional apoptosome that activates procaspase-9,” Journal of Biological Chemistry, vol. 274, no. 17, pp. 11549–11556, 1999. View at Publisher · View at Google Scholar · View at Scopus
  30. E. C. LaCasse, D. J. Mahoney, H. H. Cheung, S. Plenchette, S. Baird, and R. G. Korneluk, “IAP-targeted therapies for cancer,” Oncogene, vol. 27, no. 48, pp. 6252–6275, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  31. 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
  32. A. Letai, M. C. Bassik, L. D. Walensky, M. D. Sorcinelli, S. Weiler, and S. J. Korsmeyer, “Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics,” Cancer Cell, vol. 2, no. 3, pp. 183–192, 2002. View at Publisher · View at Google Scholar · View at Scopus
  33. L. Chen, S. N. Willis, A. Wei, et al., “Differential targeting of prosurvival Bcl-2 proteins by their BH3-only ligands allows complementary apoptotic function,” Molecular Cell, vol. 17, no. 3, pp. 393–403, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  34. S. N. Willis, J. I. Fletcher, T. Kaufmann, et al., “Apoptosis initiated when BH3 ligands engage multiple Bcl-2 homologs, not Bax or Bak,” Science, vol. 315, no. 5813, pp. 856–859, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  35. E. Varfolomeev and D. Vucic, “(Un)expected roles of c-IAPs in apoptotic and NFκB signaling pathways,” Cell Cycle, vol. 7, no. 11, pp. 1511–1521, 2008. View at Scopus
  36. E.-L. Eskelinen, “New insights into the mechanisms of macroautophagy in Mammalian cells,” International Review of Cell and Molecular Biology, vol. 266, pp. 207–247, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  37. X. H. Liang, S. Jackson, M. Seaman, et al., “Induction of autophagy and inhibition of tumorigenesis by beclin 1,” Nature, vol. 402, no. 6762, pp. 672–676, 1999. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  38. Y. Ohsumi, “Molecular dissection of autophagy: two ubiquitin-like systems,” Nature Reviews Molecular Cell Biology, vol. 2, no. 3, pp. 211–216, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  39. Y. Kabeya, N. Mizushima, T. Ueno, et al., “LC3, a mammalian homologue of yeast Apg8p, is localized in autophagosome membranes after processing,” EMBO Journal, vol. 19, no. 21, pp. 5720–5728, 2000. View at Scopus
  40. J. J. Lum, D. E. Bauer, M. Kong, et al., “Growth factor regulation of autophagy and cell survival in the absence of apoptosis,” Cell, vol. 120, no. 2, pp. 237–248, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  41. U. B. Pandey, Z. Nie, Y. Batlevi, et al., “HDAC6 rescues neurodegeneration and provides an essential link between autophagy and the UPS,” Nature, vol. 447, no. 7146, pp. 859–863, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  42. M. Høyer-Hansen, L. Bastholm, P. Szyniarowski, et al., “Control of macroautophagy by calcium, calmodulin-dependent kinase kinase-β, and Bcl-2,” Molecular Cell, vol. 25, no. 2, pp. 193–205, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  43. M. Ogata, S.-I. Hino, A. Saito, et al., “Autophagy is activated for cell survival after endoplasmic reticulum stress,” Molecular & Cellular Biology, vol. 26, no. 24, pp. 9220–9231, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  44. R. Scherz-Shouval, E. Shvets, E. Fass, H. Shorer, L. Gil, and Z. Elazar, “Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4,” EMBO Journal, vol. 26, no. 7, pp. 1749–1760, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  45. A. Nakai, O. Yamaguchi, T. Takeda, et al., “The role of autophagy in cardiomyocytes in the basal state and in response to hemodynamic stress,” Nature Medicine, vol. 13, no. 5, pp. 619–624, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  46. R. S. Decker and K. Wildenthal, “Lysosomal alterations in hypoxic and reoxygenated hearts. I. Ultrastructural and cytochemical changes,” American Journal of Pathology, vol. 98, no. 2, pp. 425–444, 1980. View at Scopus
  47. S. Khan, F. Salloum, A. Das, L. Xi, G. W. Vetrovec, and R. C. Kukreja, “Rapamycin confers preconditioning-like protection against ischemia-reperfusion injury in isolated mouse heart and cardiomyocytes,” Journal of Molecular and Cellular Cardiology, vol. 41, no. 2, pp. 256–264, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  48. S. Shimizu, T. Kanaseki, N. Mizushima, et al., “Role of Bcl-2 family proteins in a non-apoptopic programmed cell death dependent on autophagy genes,” Nature Cell Biology, vol. 6, no. 12, pp. 1221–1228, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  49. L. Yu, A. Alva, H. Su, et al., “Regulation of an ATG7-beclin 1 program of autophaglic cell death by caspase-8,” Science, vol. 304, no. 5676, pp. 1500–1502, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  50. E. Ullman, Y. Fan, M. Stawowczyk, H. M. Chen, Z. Yue, and W. X. Zong, “Autophagy promotes necrosis in apoptosis-deficient cells in response to ER stress,” Cell Death and Differentiation, vol. 15, no. 2, pp. 422–425, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  51. P. Boya, R. A. González-Polo, N. Casares, et al., “Inhibition of macroautophagy triggers apoptosis,” Molecular & Cellular Biology, vol. 25, no. 3, pp. 1025–1040, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  52. S. Pattingre, A. Tassa, X. Qu, et al., “Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy,” Cell, vol. 122, no. 6, pp. 927–939, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  53. U. Akar, A. Chaves-Reyez, M. Barria, et al., “Silencing of Bcl-2 expression by small interfering RNA induces autophagic cell death in MCF-7 breast cancer cells,” Autophagy, vol. 4, no. 5, pp. 669–679, 2008. View at Scopus
  54. S. Erlich, L. Mizrachy, O. Segev, et al., “Differential interactions between Beclin 1 and Bcl-2 family members,” Autophagy, vol. 3, no. 6, pp. 561–568, 2007. View at Scopus
  55. M. C. Maiuri, A. Criollo, E. Tasdemir, et al., “BH3-only proteins and BH3 mimetics induce autophagy by competitively disrupting the interaction between Beclin 1 and Bcl-2/Bcl-XL,” Autophagy, vol. 3, no. 4, pp. 374–376, 2007. View at Scopus
  56. M. C. Maiuri, G. Le Toumelin, A. Criollo, et al., “Functional and physical interaction between Bcl-XL and a BH3-like domain in Beclin-1,” EMBO Journal, vol. 26, no. 10, pp. 2527–2539, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  57. A. Oberstein, P. D. Jeffrey, and Y. Shi, “Crystal structure of the Bcl-XL-beclin 1 peptide complex: beclin 1 is a novel BH3-only protein,” Journal of Biological Chemistry, vol. 282, no. 17, pp. 13123–13132, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  58. N. Vanlangenakker, T. V. Berghe, D. V. Krysko, N. Festjens, and P. Vandenabeele, “Molecular mechanisms and pathophysiology of necrotic cell death,” Current Molecular Medicine, vol. 8, no. 3, pp. 207–220, 2008. View at Publisher · View at Google Scholar · View at Scopus
  59. P. Golstein and G. Kroemer, “Cell death by necrosis: towards a molecular definition,” Trends in Biochemical Sciences, vol. 32, no. 1, pp. 37–43, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  60. J. Hitomi, D. E. Christofferson, A. Ng, et al., “Identification of a molecular signaling network that regulates a cellular necrotic cell death pathway,” Cell, vol. 135, no. 7, pp. 1311–1323, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  61. W. X. Zong, D. Ditsworth, D. E. Bauer, Z. Q. Wang, and C. B. Thompson, “Alkylating DNA damage stimulates a regulated form of necrotic cell death,” Genes and Development, vol. 18, no. 11, pp. 1272–1282, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  62. M. Ankarcrona, J. M. Dypbukt, E. Bonfoco, et al., “Glutamate-induced neuronal death: a succession of necrosis or apoptosis depending on mitochondrial function,” Neuron, vol. 15, no. 4, pp. 961–973, 1995. View at Scopus
  63. C. Zhu, X. Wang, F. Xu, et al., “The influence of age on apoptotic and other mechanisms of cell death after cerebral hypoxia-ischemia,” Cell Death and Differentiation, vol. 12, no. 2, pp. 162–176, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  64. N. Festjens, T. Vanden Berghe, S. Cornelis, and P. Vandenabeele, “RIP1, a kinase on the crossroads of a cell's decision to live or die,” Cell Death and Differentiation, vol. 14, no. 3, pp. 400–410, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  65. E. Meylan and J. Tschopp, “The RIP kinases: crucial integrators of cellular stress,” Trends in Biochemical Sciences, vol. 30, no. 3, pp. 151–159, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  66. N. Holler, R. Zaru, O. Micheau, et al., “Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule,” Nature Immunology, vol. 1, no. 6, pp. 489–495, 2000. View at Scopus
  67. F. K. Chan, J. Shisler, J. G. Bixby, et al., “A role for tumor necrosis factor receptor-2 and receptor-interacting protein in programmed necrosis and antiviral responses,” Journal of Biological Chemistry, vol. 278, no. 51, pp. 51613–51621, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  68. Y. Ma, V. Temkin, H. Liu, and R. M. Pope, “NF-κB protects macrophages from lipopolysaccharide-induced cell death: the role of caspase 8 and receptor-interacting protein,” Journal of Biological Chemistry, vol. 280, no. 51, pp. 41827–41834, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  69. A. Degterev, Z. Huang, M. Boyce, et al., “Chemical inhibitor of nonapoptotic cell death with therapeutic potential for ischemic brain injury,” Nature Chemical Biology, vol. 1, no. 2, pp. 112–119, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  70. A. Degterev, J. Hitomi, M. Germscheid, et al., “Identification of RIP1 kinase as a specific cellular target of necrostatins,” Nature Chemical Biology, vol. 4, no. 5, pp. 313–321, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  71. Z. You, S. I. Savitz, J. Yang, et al., “Necrostatin-1 reduces histopathology and improves functional outcome after controlled cortical impact in mice,” Journal of Cerebral Blood Flow and Metabolism, vol. 28, no. 9, pp. 1564–1573, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  72. Y. S. Cho, S. Challa, D. Moquin, et al., “Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation,” Cell, vol. 137, no. 6, pp. 1112–1123, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  73. S. He, L. Wang, L. Miao, et al., “Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-α,” Cell, vol. 137, no. 6, pp. 1100–1111, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  74. D. W. Zhang, J. Shao, J. Lin, et al., “RIP3, an energy metabolism regulator that switches TNF-induced cell death from apoptosis to necrosis,” Science, vol. 325, no. 5938, pp. 332–336, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  75. K. Schulze-Osthoff, A. C. Bakker, B. Vanhaesebroeck, R. Beyaert, W. A. Jacob, and W. Fiers, “Cytotoxic activity of tumor necrosis factor is mediated by early damage of mitochondrial functions. Evidence for the involvement of mitochondrial radical generation,” Journal of Biological Chemistry, vol. 267, no. 8, pp. 5317–5323, 1992. View at Scopus
  76. M. Kalai, G. Van Loo, T. Vanden Berghe, et al., “Tipping the balance between necrosis and apoptosis in human and murine cells treated with interferon and dsRNA,” Cell Death and Differentiation, vol. 9, no. 9, pp. 981–994, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  77. F. Van Herreweghe, J. Mao, F. W. R. Chaplen, et al., “Tumor necrosis factor-induced modulation of glyoxalase I activities through phosphorylation by PKA results in cell death and is accompanied by the formation of a specific methylglyoxal-derived AGE,” Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 2, pp. 949–954, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  78. R. G. Hansford and D. Zorov, “Role of mitochondrial calcium transport in the control of substrate oxidation,” Molecular & Cellular Biochemistry, vol. 184, no. 1-2, pp. 359–369, 1998. View at Scopus
  79. B. T. Chua, K. Guo, and P. Li, “Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases,” Journal of Biological Chemistry, vol. 275, no. 7, pp. 5131–5135, 2000. View at Publisher · View at Google Scholar · View at Scopus
  80. A. Samali, H. Nordgren, B. Zhivotovsky, E. Peterson, and S. Orrenius, “A comparative study of apoptosis and necrosis in HepG2 cells: oxidant-induced caspase inactivation leads to necrosis,” Biochemical and Biophysical Research Communications, vol. 255, no. 1, pp. 6–11, 1999. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  81. C. R. Weston and R. J. Davis, “The JNK signal transduction pathway,” Current Opinion in Cell Biology, vol. 19, no. 2, pp. 142–149, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  82. N. D. Perkins and T. D. Gilmore, “Good cop, bad cop: the different faces of NF-κB,” Cell Death and Differentiation, vol. 13, no. 5, pp. 759–772, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  83. S. Lindquist, “The heat-shock response,” Annual Review of Biochemistry, vol. 55, pp. 1151–1191, 1986. View at Scopus
  84. E. A. Craig, “The heat shock response,” CRC Critical Reviews in Biochemistry, vol. 18, no. 3, pp. 239–280, 1985. View at Scopus
  85. A. Samali and S. Orrenius, “Heat shock proteins: regulators of stress response and apoptosis,” Cell Stress and Chaperones, vol. 3, no. 4, pp. 228–236, 1998. View at Publisher · View at Google Scholar · View at Scopus
  86. A. Samali and T. G. Cotter, “Heat shock proteins increase resistance to apoptosis,” Experimental Cell Research, vol. 223, no. 1, pp. 163–170, 1996. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  87. A. Samali, C. I. Holmberg, L. Sistonen, and S. Orrenius, “Thermotolerance and cell death are distinct cellular responses to stress: dependence on heat shock proteins,” FEBS Letters, vol. 461, no. 3, pp. 306–310, 1999. View at Publisher · View at Google Scholar · View at Scopus
  88. G. C. Li and Z. Werb, “Correlation between synthesis of heat shock proteins and development of thermotolerance in Chinese hamster fibroblasts,” Proceedings of the National Academy of Sciences of the United States of America, vol. 79, no. 10, pp. 3218–3222, 1982. View at Scopus
  89. R. I. Morimoto, P. E. Kroeger, and J. J. Cotto, “The transcriptional regulation of heat shock genes: a plethora of heat shock factors and regulatory conditions,” EXS, vol. 77, pp. 139–163, 1996. View at Scopus
  90. L. Pirkkala, P. Nykänen, and L. Sistonen, “Roles of the heat shock transcription factors in regulation of the heat shock response and beyond,” FASEB Journal, vol. 15, no. 7, pp. 1118–1131, 2001. View at Publisher · View at Google Scholar · View at Scopus
  91. A. Shabtay and Z. Arad, “Reciprocal activation of HSF1 and HSF3 in brain and blood tissues: is redundancy developmentally related?” American Journal of Physiology, vol. 291, no. 3, pp. R566–R572, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  92. D. R. McMillan, X. Xiao, L. Shao, K. Graves, and I. J. Benjamin, “Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis,” Journal of Biological Chemistry, vol. 273, no. 13, pp. 7523–7528, 1998. View at Publisher · View at Google Scholar · View at Scopus
  93. X. Xiao, X. Zuo, A. A. Davis, et al., “HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice,” EMBO Journal, vol. 18, no. 21, pp. 5943–5952, 1999. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  94. Y. Zhang, L. Huang, J. Zhang, D. Moskophidis, and N. F. Mivechi, “Targeted disruption of hsf1 leads to lack of thermotolerance and defines tissue-specific regulation for stress-inducible hsp molecular chaperones,” Journal of Cellular Biochemistry, vol. 86, no. 2, pp. 376–393, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  95. P. Östling, J. K. Björk, P. Roos-Mattjus, V. Mezger, and L. Sistonen, “Heat Shock Factor 2 (HSF2) contributes to inducible expression of hsp genes through interplay with HSF1,” Journal of Biological Chemistry, vol. 282, no. 10, pp. 7077–7086, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  96. I. Shamovsky and E. Nudler, “New insights into the mechanism of heat shock response activation,” Cellular and Molecular Life Sciences, vol. 65, no. 6, pp. 855–861, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  97. R. Voellmy, “On mechanisms that control heat shock transcription factor activity in metazoan cells,” Cell Stress and Chaperones, vol. 9, no. 2, pp. 122–133, 2004. View at Publisher · View at Google Scholar · View at Scopus
  98. M. Jäättelä, “Heat shock proteins as cellular lifeguards,” Annals of Medicine, vol. 31, no. 4, pp. 261–271, 1999. View at Scopus
  99. S. Lindquist and E. A. Craig, “The heat-shock proteins,” Annual Review of Genetics, vol. 22, pp. 631–677, 1988. View at Scopus
  100. C. Garrido, “Size matters: of the small HSP27 and its large oligomers,” Cell Death and Differentiation, vol. 9, no. 5, pp. 483–485, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  101. M. Jäättelä, D. Wissing, K. Kokholm, T. Kallunki, and M. Egeblad, “Hsp7O exerts its anti-apoptotic function downstream of caspase-3-like proteases,” EMBO Journal, vol. 17, no. 21, pp. 6124–6134, 1998. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  102. A. E. Kabakov and V. L. Gabai, “Heat-shock-induced accumulation of 70-kDa stress protein (HSP70) can protect ATP-depleted tumor cells from necrosis,” Experimental Cell Research, vol. 217, no. 1, pp. 15–21, 1995. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  103. P. Mehlen, X. Preville, P. Chareyron, J. Briolay, R. Klemenz, and A. P. Arrigo, “Constitutive expression of human hsp27, Drosophila hsp27, or human αB- crystallin confers resistance to TNF- and oxidative stress-induced cytotoxicity in stably transfected murine L929 fibroblasts,” Journal of Immunology, vol. 154, no. 1, pp. 363–374, 1995. View at Scopus
  104. M. J. Champagne, P. Dumas, S. N. Orlov, M. R. Bennett, P. Hamet, and J. Tremblay, “Protection against necrosis but not apoptosis by heat-stress proteins in vascular smooth muscle cells: evidence for distinct modes of cell death,” Hypertension, vol. 33, no. 3, pp. 906–913, 1999. View at Scopus
  105. F. U. Hartl and M. Hayer-Hartl, “Molecular chaperones in the cytosol: from nascent chain to folded protein,” Science, vol. 295, no. 5561, pp. 1852–1858, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  106. C. G. Concannon, A. M. Gorman, and A. Samali, “On the role of Hsp27 in regulating apoptosis,” Apoptosis, vol. 8, no. 1, pp. 61–70, 2003. View at Publisher · View at Google Scholar · View at Scopus
  107. C. G. Concannon, S. Orrenius, and A. Samali, “Hsp27 inhibits cytochrome c-mediated caspase activation by sequestering both pro-caspase-3 and cytochrome c,” Gene Expression, vol. 9, no. 4-5, pp. 195–201, 2001. View at Scopus
  108. P. Pandey, R. Farber, A. Nakazawa, et al., “Hsp27 functions as a negative regulator of cytochrome c-dependent activation of procaspase-3,” Oncogene, vol. 19, no. 16, pp. 1975–1981, 2000. View at Scopus
  109. J.-M. Bruey, C. Ducasse, P. Bonniaud, et al., “Hsp27 negatively regulates cell death by interacting with cytochrome c,” Nature Cell Biology, vol. 2, no. 9, pp. 645–652, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  110. A. Samali, J. D. Robertson, E. Peterson, et al., “Hsp27 protects mitochondria of thermotolerant cells against apoptotic stimuli,” Cell Stress and Chaperones, vol. 6, no. 1, pp. 49–58, 2001. View at Publisher · View at Google Scholar · View at Scopus
  111. D. Chauhan, G. Li, T. Hideshima, et al., “Hsp27 inhibits release of mitochondrial protein Smac in multiple myeloma cells and confers dexamethasone resistance,” Blood, vol. 102, no. 9, pp. 3379–3386, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  112. R. Steel, J. P. Doherty, K. Buzzard, N. Clemons, C. J. Hawkins, and R. L. Anderson, “Hsp72 inhibits apoptosis upstream of the mitochondria and not through interactions with Apaf-1,” Journal of Biological Chemistry, vol. 279, no. 49, pp. 51490–51499, 2004.
  113. A. Saleh, S. M. Srinivasula, L. Balkir, P. D. Robbins, and E. S. Alnemri, “Negative regulation of the Apaf-1 apoptosome by Hsp70,” Nature Cell Biology, vol. 2, no. 8, pp. 476–483, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  114. H. M. Beere, B. B. Wolf, K. Cain, et al., “Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome,” Nature Cell Biology, vol. 2, no. 8, pp. 469–475, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  115. E. Yu. Komarova, E. A. Afanasyeva, M. M. Bulatova, M. E. Cheetham, B. A. Margulis, and I. V. Guzhova, “Downstream caspases are novel targets for the antiapoptotic activity of the molecular chaperone Hsp70,” Cell Stress and Chaperones, vol. 9, no. 3, pp. 265–275, 2004. View at Scopus
  116. E. M. Creagh, R. J. Carmody, and T. G. Cotter, “Heat shock protein 70 inhibits caspase-dependent and -independent apoptosis in Jurkat T cells,” Experimental Cell Research, vol. 257, no. 1, pp. 58–66, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  117. L. Ravagnan, S. Gurbuxani, S. A. Susin, et al., “Heat-shock protein 70 antagonizes apoptosis-inducing factor,” Nature Cell Biology, vol. 3, no. 9, pp. 839–843, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  118. S. J. Charette and J. Landry, “The interaction of HSP27 with Daxx identifies a potential regulatory role of HSP27 in Fas-induced apoptosis,” Annals of the New York Academy of Sciences, vol. 926, pp. 126–131, 2000. View at Scopus
  119. V. L. Gabai, J. A. Yaglom, V. Volloch, et al., “Hsp72-mediated suppression of c-Jun N-terminal kinase is implicated in development of tolerance to caspase-independent cell death,” Molecular & Cellular Biology, vol. 20, no. 18, pp. 6826–6836, 2000. View at Publisher · View at Google Scholar · View at Scopus
  120. D. D. Mosser, A. W. Caron, L. Bourget, C. Denis-Larose, and B. Massie, “Role of the human heat shock protein hsp70 in protection against stress-induced apoptosis,” Molecular & Cellular Biology, vol. 17, no. 9, pp. 5317–5327, 1997. View at Scopus
  121. J. Park and A. Y. C. Liu, “JNK phosphorylates the HSF1 transcriptional activation domain: role of JNK in the regulation of the heat shock response,” Journal of Cellular Biochemistry, vol. 82, no. 2, pp. 326–338, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  122. H. Konishi, H. Matsuzaki, M. Tanaka, et al., “Activation of protein kinase B (Akt/RAC-protein kinase) by cellular stress and its association with heat shock protein Hsp27,” FEBS Letters, vol. 410, no. 2-3, pp. 493–498, 1997. View at Publisher · View at Google Scholar · View at Scopus
  123. K. M. Mearow, M. E. Dodge, M. Rahimtula, and C. Yegappan, “Stress-mediated signaling in PC12 cells—the role of the small heat shock protein, Hsp27, and Akt in protecting cells from heat stress and nerve growth factor withdrawal,” Journal of Neurochemistry, vol. 83, no. 2, pp. 452–462, 2002. View at Publisher · View at Google Scholar · View at Scopus
  124. M. J. Rane, Y. Pan, S. Singh, et al., “Heat shock protein 27 controls apoptosis by regulating Akt activation,” Journal of Biological Chemistry, vol. 278, no. 30, pp. 27828–27835, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  125. X.-B. Qiu, Y.-M. Shao, S. Miao, and L. Wang, “The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones,” Cellular & Molecular Life Sciences, vol. 63, no. 22, pp. 2560–2570, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  126. S. Takayama, D. N. Bimston, S.-I. Matsuzawa, et al., “BAG-1 modulates the chaperone activity of Hsp70/Hsc70,” EMBO Journal, vol. 16, no. 16, pp. 4887–4896, 1997. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  127. 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 PubMed · View at Scopus
  128. D. Ron and P. Walter, “Signal integration in the endoplasmic reticulum unfolded protein response,” Nature Reviews Molecular Cell Biology, vol. 8, no. 7, pp. 519–529, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  129. S. Kondo, T. Murakami, K. Tatsumi, et al., “OASIS, a CREB/ATF-family member, modulates UPR signalling in astrocytes,” Nature Cell Biology, vol. 7, no. 2, pp. 186–194, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  130. K. Zhang, X. Shen, J. Wu, et al., “Endoplasmic reticulum stress activates cleavage of CREBH to induce a systemic inflammatory response,” Cell, vol. 124, no. 3, pp. 587–599, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  131. I. Nagamori, K. Yomogida, M. Ikawa, M. Okabe, N. Yabuta, and H. Nojima, “The testes-specific bZip type transcription factor Tisp40 plays a role in ER stress responses and chromatin packaging during spermiogenesis,” Genes to Cells, vol. 11, no. 10, pp. 1161–1171, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  132. G. Liang, T. E. Audas, Y. Li, et al., “Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein herp through an ER stress response element,” Molecular & Cellular Biology, vol. 26, no. 21, pp. 7999–8010, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  133. J. S. Cox and P. Walter, “A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response,” Cell, vol. 87, no. 3, pp. 391–404, 1996. View at Publisher · View at Google Scholar · View at Scopus
  134. K. Mori, T. Kawahara, H. Yoshida, H. Yanagi, and T. Yura, “Signalling from endoplasmic reticulum to nucleus: transcription factor with a basic-leucine zipper motif is required for the unfolded protein-response pathway,” Genes to Cells, vol. 1, no. 9, pp. 803–817, 1996. View at Scopus
  135. H. Yoshida, T. Matsui, A. Yamamoto, T. Okada, and K. Mori, “XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor,” Cell, vol. 107, no. 7, pp. 881–891, 2001. View at Publisher · View at Google Scholar · View at Scopus
  136. M. Calfon, H. Zeng, F. Urano, et al., “IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA,” Nature, vol. 415, no. 6867, pp. 92–96, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  137. H. P. Harding, Y. Zhang, and D. Ron, “Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase,” Nature, vol. 397, no. 6716, pp. 271–274, 1999. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  138. P. D. Lu, H. P. Harding, and D. Ron, “Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress response,” Journal of Cell Biology, vol. 167, no. 1, pp. 27–33, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  139. S. B. Cullinan, D. Zhang, M. Hannink, E. Arvisais, R. J. Kaufman, and J. A. Diehl, “Nrf2 is a direct PERK substrate and effector of PERK-dependent cell survival,” Molecular & Cellular Biology, vol. 23, no. 20, pp. 7198–7209, 2003. View at Publisher · View at Google Scholar · View at Scopus
  140. S. B. Cullinan and J. A. Diehl, “PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress,” Journal of Biological Chemistry, vol. 279, no. 19, pp. 20108–20117, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  141. K. Haze, H. Yoshida, H. Yanagi, T. Yura, and K. Mori, “Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress,” Molecular Biology of the Cell, vol. 10, no. 11, pp. 3787–3799, 1999. View at Scopus
  142. J. Ye, R. B. Rawson, R. Komuro, et al., “ER stress induces cleavage of membrane-bound ATF6 by the same proteases that process SREBPs,” Molecular Cell, vol. 6, no. 6, pp. 1355–1364, 2000. View at Publisher · View at Google Scholar · View at Scopus
  143. M. Tamatani, T. Matsuyama, A. Yamaguchi, et al., “ORP150 protects against hypoxia/ischemia-induced neuronal death,” Nature Medicine, vol. 7, no. 3, pp. 317–323, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  144. O. Hori, M. Miyazaki, T. Tamatani, et al., “Deletion of SERP1/RAMP4, a component of the endoplasmic reticulum (ER) translocation sites, leads to ER stress,” Molecular & Cellular Biology, vol. 26, no. 11, pp. 4257–4267, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  145. T. Nakagawa, H. Zhu, N. Morishima, et al., “Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β,” Nature, vol. 403, no. 6765, pp. 98–103, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  146. J. Hitomi, T. Katayama, Y. Eguchi, et al., “Involvement of caspase-4 in endoplasmic reticulum stress-induced apoptosis and Aβ-induced cell death,” Journal of Cell Biology, vol. 165, no. 3, pp. 347–356, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  147. R. V. Rao, S. Castro-Obregon, H. Frankowski, et al., “Coupling endoplasmic reticulum stress to the cell death program. An Apaf-1-independent intrinsic pathway,” Journal of Biological Chemistry, vol. 277, no. 24, pp. 21836–21842, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  148. K. D. McCullough, J. L. Martindale, L.-O. Klotz, T.-Y. Aw, and N. J. Holbrook, “Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bc12 and perturbing the cellular redox state,” Molecular & Cellular Biology, vol. 21, no. 4, pp. 1249–1259, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  149. H. Puthalakath, L. A. O'Reilly, P. Gunn, et al., “ER stress triggers apoptosis by activating BH3-only protein Bim,” Cell, vol. 129, no. 7, pp. 1337–1349, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  150. F. Urano, X. Wang, A. Bertolotti, et al., “Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1,” Science, vol. 287, no. 5453, pp. 664–666, 2000. View at Publisher · View at Google Scholar · View at Scopus
  151. H. Nishitoh, A. Matsuzawa, K. Tobiume, et al., “ASK1 is essential for endoplasmic reticulum stress-induced neuronal cell death triggered by expanded polyglutamine repeats,” Genes and Development, vol. 16, no. 11, pp. 1345–1355, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  152. M. Ni and A. S. Lee, “ER chaperones in mammalian development and human diseases,” FEBS Letters, vol. 581, no. 19, pp. 3641–3651, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  153. A. M. Gorman, “Neuronal cell death in neurodegenerative diseases: recurring themes around protein handling,” Journal of Cellular & Molecular Medicine, vol. 12, no. 6, pp. 2263–2280, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  154. A. N. Mhaille, S. McQuaid, A. Windebank, et al., “Increased expression of endoplasmic reticulum stress-related signaling pathway molecules in multiple sclerosis lesions,” Journal of Neuropathology & Experimental Neurology, vol. 67, no. 3, pp. 200–211, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  155. C. Holohan, E. Szegezdi, T. Ritter, T. O'Brien, and A. Samali, “Cytokine-induced β-cell apoptosis is NO-dependent, mitochondria-mediated and inhibited by BCL-XL,” Journal of Cellular & Molecular Medicine, vol. 12, no. 2, pp. 591–606, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  156. R. P. C. Shiu, J. Pouyssegur, and I. Pastan, “Glucose depletion accounts for the induction of two transformation-sensitive membrane proteins in Rous sarcoma virus-transformed chick embryo fibroblasts,” Proceedings of the National Academy of Sciences of the United States of America, vol. 74, no. 9, pp. 3840–3844, 1977. View at Scopus
  157. H. Yoshida, K. Haze, H. Yanagi, T. Yura, and K. Mori, “Identification of the cis-acting endoplasmic reticulum stress response element responsible for transcriptional induction of mammalian glucose-regulated proteins: involvement of basic leucine zipper transcription factors,” Journal of Biological Chemistry, vol. 273, no. 50, pp. 33741–33749, 1998. View at Publisher · View at Google Scholar · View at Scopus
  158. S. Tanaka, T. Uehara, and Y. Nomura, “Up-regulation of protein-disulfide isomerase in response to hypoxia/brain ischemia and its protective effect against apoptotic cell death,” Journal of Biological Chemistry, vol. 275, no. 14, pp. 10388–10393, 2000. View at Publisher · View at Google Scholar · View at Scopus
  159. Y. Kitao, K. Ozawa, M. Miyazaki, et al., “Expression of the endoplasmic reticulum molecular chaperone (ORP150) rescues hippocampal neurons from glutamate toxicity,” Journal of Clinical Investigation, vol. 108, no. 10, pp. 1439–1450, 2001. View at Publisher · View at Google Scholar · View at Scopus
  160. 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 PubMed · View at Scopus
  161. 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 PubMed · View at Scopus
  162. T. Hoshino, T. Nakaya, W. Araki, K. Suzuki, T. Suzuki, and T. Mizushima, “Endoplasmic reticulum chaperones inhibit the production of amyloid-β peptides,” Biochemical Journal, vol. 402, no. 3, pp. 581–589, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  163. R. E. Feaver, N. E. Hastings, A. Pryor, and B. R. Blackman, “GRP78 upregulation by atheroprone shear stress via p38-, α2β1-dependent mechanism in endothelial cells,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 28, no. 8, pp. 1534–1541, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  164. C. Zhang, Y. Cai, M. T. Adachi, et al., “Homocysteine induces programmed cell death in human vascular endothelial cells through activation of the unfolded protein response,” Journal of Biological Chemistry, vol. 276, no. 38, pp. 35867–35874, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  165. G. H. Werstuck, S. R. Lentz, S. Dayal, et al., “Homocysteine-induced endoplasmic reticulum stress causes dysregulation of the cholesterol and triglyceride biosynthetic pathways,” Journal of Clinical Investigation, vol. 107, no. 10, pp. 1263–1273, 2001. View at Scopus
  166. L. M. Watson, A. K. C. Chan, L. R. Berry, et al., “Overexpression of the 78-kDa glucose-regulated protein/immunoglobulin-binding protein (GRP78/BiP) inhibits tissue factor procoagulant activity,” Journal of Biological Chemistry, vol. 278, no. 19, pp. 17438–17447, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  167. S. Luo, C. Mao, B. Lee, and A. S. Lee, “GRP78/BiP is required for cell proliferation and protecting the inner cell mass from apoptosis during early mouse embryonic development,” Molecular & Cellular Biology, vol. 26, no. 15, pp. 5688–5697, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  168. N. Mesaeli, K. Nakamura, E. Zvaritch, et al., “Calreticulin is essential for cardiac development,” Journal of Cell Biology, vol. 144, no. 5, pp. 857–868, 1999. View at Publisher · View at Google Scholar · View at Scopus
  169. Y. Kitao, K. Hashimoto, T. Matsuyama, et al., “ORP150/HSP12A regulates purkinje cell survival: a role for endoplasmic reticulum stress in cerebellar development,” Journal of Neuroscience, vol. 24, no. 6, pp. 1486–1496, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  170. K. Kubota, Y. Niinuma, M. Kaneko, et al., “Suppressive effects of 4-phenylbutyrate on the aggregation of Pael receptors and endoplasmic reticulum stress,” Journal of Neurochemistry, vol. 97, no. 5, pp. 1259–1268, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  171. S.-E. Choi, Y.-J. Lee, H.-J. Jang, et al., “A chemical chaperone 4-PBA ameliorates palmitate-induced inhibition of glucose-stimulated insulin secretion (GSIS),” Archives of Biochemistry and Biophysics, vol. 475, no. 2, pp. 109–114, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  172. T. Kudo, S. Kanemoto, H. Hara, et al., “A molecular chaperone inducer protects neurons from ER stress,” Cell Death and Differentiation, vol. 15, no. 2, pp. 364–375, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  173. K. Takano, Y. Tabata, Y. Kitao, et al., “Methoxyflavones protect cells against endoplasmic reticulum stress and neurotoxin,” American Journal of Physiology, vol. 292, no. 1, pp. C353–C361, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  174. W. P. Roos and B. Kaina, “DNA damage-induced cell death by apoptosis,” Trends in Molecular Medicine, vol. 12, no. 9, pp. 440–450, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  175. M. Christmann, M. T. Tomicic, W. P. Roos, and B. Kaina, “Mechanisms of human DNA repair: an update,” Toxicology, vol. 193, no. 1-2, pp. 3–34, 2003. View at Publisher · View at Google Scholar · View at Scopus
  176. D. J. Richard, E. Bolderson, and K. K. Khanna, “Multiple human single-stranded DNA binding proteins function in genome maintenance: structural, biochemical and functional analysis,” Critical Reviews in Biochemistry and Molecular Biology, vol. 44, no. 2-3, pp. 98–116, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  177. L. Staresincic, A. F. Fagbemi, J. H. Enzlin, et al., “Coordination of dual incision and repair synthesis in human nucleotide excision repair,” EMBO Journal, vol. 28, no. 8, pp. 1111–1120, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  178. J. W. Harper and S. J. Elledge, “The DNA damage response: ten years after,” Molecular Cell, vol. 28, no. 5, pp. 739–745, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  179. K. H. Vousden and D. P. Lane, “p53 in health and disease,” Nature Reviews Molecular Cell Biology, vol. 8, no. 4, pp. 275–283, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  180. A. V. Vaseva and U. M. Moll, “The mitochondrial p53 pathway,” Biochimica et Biophysica Acta, vol. 1787, no. 5, pp. 414–420, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  181. S. P. Jackson, “Sensing and repairing DNA double-strand breaks,” Carcinogenesis, vol. 23, no. 5, pp. 687–696, 2002. View at Scopus
  182. K. Valerie and L. F. Povirk, “Regulation and mechanisms of mammalian double-strand break repair,” Oncogene, vol. 22, no. 37, pp. 5792–5812, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  183. D. E. Barnes and T. Lindahl, “Repair and genetic consequences of endogenous DNA base damage in mammalian cells,” Annual Review of Genetics, vol. 38, pp. 445–476, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  184. L. Stojic, R. Brun, and J. Jiricny, “Mismatch repair and DNA damage signalling,” DNA Repair, vol. 3, no. 8-9, pp. 1091–1101, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  185. J. H. J. Hoeijmakers, “Genome maintenance mechanisms for preventing cancer,” Nature, vol. 411, no. 6835, pp. 366–374, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  186. D. Trachootham, W. Lu, M. A. Ogasawara, N. R.-D. Valle, and P. Huang, “Redox regulation of cell survival,” Antioxidants & Redox Signaling, vol. 10, no. 8, pp. 1343–1374, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  187. B. Brune, “The intimate relation between nitric oxide and superoxide in apoptosis and cell survival,” Antioxidants & Redox Signaling, vol. 7, no. 3-4, pp. 497–507, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  188. K. Niizuma, H. Endo, and P. H. Chan, “Oxidative stress and mitochondrial dysfunction as determinants of ischemic neuronal death and survival,” Journal of Neurochemistry, vol. 109, supplement 1, pp. 133–138, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  189. S. Orrenius, V. Gogvadze, and B. Zhivotovsky, “Mitochondrial oxidative stress: implications for cell death,” Annual Review of Pharmacology & Toxicology, vol. 47, pp. 143–183, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  190. M. Genestra, “Oxyl radicals, redox-sensitive signalling cascades and antioxidants,” Cellular Signalling, vol. 19, no. 9, pp. 1807–1819, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  191. P. Zaccagnino, M. Saltarella, S. D'Oria, A. Corcelli, M. S. Saponetti, and M. Lorusso, “N-arachidonylglycine causes ROS production and cytochrome c release in liver mitochondria,” Free Radical Biology & Medicine, vol. 47, no. 5, pp. 585–592, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  192. A. Sapone, A. Affatato, D. Canistro, et al., “Induction and suppression of cytochrome P450 isoenzymes and generation of oxygen radicals by procymidone in liver, kidney and lung of CD1 mice,” Mutation Research, vol. 527, no. 1-2, pp. 67–80, 2003. View at Publisher · View at Google Scholar · View at Scopus
  193. X. Gong, R. Gutala, and A. K. Jaiswal, “Quinone oxidoreductases and vitamin K metabolism,” Vitamins and Hormones, vol. 78, pp. 85–101, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  194. J. D. Robertson, J. Chandra, V. Gogvadze, and S. Orrenius, “Biological reactive intermediates and mechanisms of cell death,” Advances in Experimental Medicine and Biology, vol. 500, pp. 1–10, 2001. View at Scopus
  195. A. M. Gorman, B. Heavey, E. Creagh, T. G. Cotter, and A. Samali, “Antioxidant-mediated inhibition of the heat shock response leads to apoptosis,” FEBS Letters, vol. 445, no. 1, pp. 98–102, 1999. View at Publisher · View at Google Scholar · View at Scopus
  196. A. M. Gorman, E. Szegezdi, D. J. Quigney, and A. Samali, “Hsp27 inhibits 6-hydroxydopamine-induced cytochrome c release and apoptosis in PC12 cells,” Biochemical & Biophysical Research Communications, vol. 327, no. 3, pp. 801–810, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  197. W. R. Swindell, M. Huebner, and A. P. Weber, “Transcriptional profiling of arabidopsis heat shock proteins and transcription factors reveals extensive overlap between heat and non-heat stress response pathways,” BMC Genomics, vol. 8, article 125, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  198. S. B. Cullinan and J. A. Diehl, “Coordination of ER and oxidative stress signaling: the PERK/Nrf2 signaling pathway,” International Journal of Biochemistry & Cell Biology, vol. 38, no. 3, pp. 317–332, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  199. S. B. Cullinan and J. A. Diehl, “PERK-dependent activation of Nrf2 contributes to redox homeostasis and cell survival following endoplasmic reticulum stress,” Journal of Biological Chemistry, vol. 279, no. 19, pp. 20108–20117, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  200. Y. Chen, M. B. Azad, and S. B. Gibson, “Superoxide is the major reactive oxygen species regulating autophagy,” Cell Death and Differentiation, vol. 16, no. 7, pp. 1040–1052, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  201. A. Gorman, A. McGowan, and T. G. Cotter, “Role of peroxide and superoxide anion during tumour cell apoptosis,” FEBS Letters, vol. 404, no. 1, pp. 27–33, 1997. View at Publisher · View at Google Scholar · View at Scopus
  202. M. Meyer, R. Schreck, and P. A. Baeuerle, “H2O2 and antioxidants have opposite effects on activation of NF-kappa B and AP-1 in intact cells: AP-1 as secondary antioxidant-responsive factor,” EMBO Journal, vol. 12, no. 5, pp. 2005–2015, 1993. View at Scopus
  203. T. L. Denning, H. Takaishi, S. E. Crowe, I. Boldogh, A. Jevnikar, and P. B. Ernst, “Oxidative stress induces the expression of Fas and Fas ligand and apoptosis in murine intestinal epithelial cells,” Free Radical Biology & Medicine, vol. 33, no. 12, pp. 1641–1650, 2002. View at Publisher · View at Google Scholar · View at Scopus
  204. H. Hug, S. Strand, A. Grambihler, et al., “Reactive oxygen intermediates are involved in the induction of CD95 ligand mRNA expression by cytostatic drugs in hepatoma cells,” Journal of Biological Chemistry, vol. 272, no. 45, pp. 28191–28193, 1997. View at Publisher · View at Google Scholar · View at Scopus
  205. K. Dobashi, K. Pahan, A. Chahal, and I. Singh, “Modulation of endogenous antioxidant enzymes by nitric oxide in rat C6 glial cells,” Journal of Neurochemistry, vol. 68, no. 5, pp. 1896–1903, 1997. View at Scopus
  206. M. Asahi, J. Fujii, K. Suzuki, et al., “Inactivation of glutathione peroxidase by nitric oxide. Implication for cytotoxicity,” Journal of Biological Chemistry, vol. 270, no. 36, pp. 21035–21039, 1995. View at Publisher · View at Google Scholar · View at Scopus
  207. L. Bosca and S. Hortelano, “Mechanisms of nitric oxide-dependent apoptosis: involvement of mitochondrial mediators,” Cellular Signalling, vol. 11, no. 4, pp. 239–244, 1999. View at Publisher · View at Google Scholar · View at Scopus
  208. Z. X. Chen and S. Pervaiz, “BCL-2: pro-or anti-oxidant?” Frontiers in Bioscience, vol. 1, pp. 263–268, 2009.
  209. N. Mirkovic, D. W. Voehringer, M. D. Story, D. J. McConkey, T. J. McDonnell, and R. E. Meyn, “Resistance to radiation-induced apoptosis in bcl-2-expressing cells is reversed by depleting cellular thiols,” Oncogene, vol. 15, no. 12, pp. 1461–1470, 1997. View at Scopus
  210. N. M. Robertson, J. Zangrilli, T. Fernandes-Alnemri, P. D. Friesen, G. Litwack, and E. S. Alnemri, “Baculovirus P35 inhibits the glucocorticoid-mediated pathway of cell death,” Cancer Research, vol. 57, no. 1, pp. 43–47, 1997. View at Scopus
  211. N. K. Sah, T. K. Taneja, N. Pathak, R. Begum, M. Athar, and S. E. Hasnain, “The baculovirus antiapoptotic p35 gene also functions via an oxidant-dependent pathway,” Proceedings of the National Academy of Sciences of the United States of America, vol. 96, no. 9, pp. 4838–4843, 1999. View at Scopus
  212. E. S. Alnemri, D. J. Livingston, D. W. Nicholson, et al., “Human ICE/CED-3 protease nomenclature,” Cell, vol. 87, no. 2, p. 171, 1996. View at Scopus
  213. J. Chandra, A. Samali, and S. Orrenius, “Triggering and modulation of apoptosis by oxidative stress,” Free Radical Biology & Medicine, vol. 29, no. 3-4, pp. 323–333, 2000. View at Publisher · View at Google Scholar · View at Scopus
  214. G. Melino, F. Bernassola, R. A. Knight, M. T. Corasaniti, G. Nistico, and A. Finazzi-Agro, “S-nitrosylation regulates apoptosis,” Nature, vol. 388, no. 6641, pp. 432–433, 1997. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  215. M. Leist, B. Single, H. Naumann, et al., “Inhibition of mitochondrial ATP generation by nitric oxide switches apoptosis to necrosis,” Experimental Cell Research, vol. 249, no. 2, pp. 396–403, 1999. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  216. Y. Tsujimoto, S. Shimizu, Y. Eguchi, W. Kamiike, and H. Matsuda, “BCL-2 and Bcl-xL block apoptosis as well as necrosis: possible involvement of common mediators in apoptotic and necrotic signal transduction pathways,” Leukemia, vol. 11, supplement 3, pp. 380–382, 1997. View at Scopus
  217. M. C. Maiuri, E. Zalckvar, A. Kimchi, and G. Kroemer, “Self-eating and self-killing: crosstalk between autophagy and apoptosis,” Nature Reviews Molecular Cell Biology, vol. 8, no. 9, pp. 741–752, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  218. B. Kalmar and L. Greensmith, “Activation of the heat shock response in a primary cellular model of motoneuron neurodegeneration-evidence for neuroprotective and neurotoxic effects,” Cellular & Molecular Biology Letters, vol. 14, no. 2, pp. 319–335, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  219. J. H. Lin, H. Li, D. Yasumura, et al., “IRE1 signaling affects cell fate during the unfolded protein response,” Science, vol. 318, no. 5852, pp. 944–949, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  220. A. Jorns, A. Gunther, H.-J. Hedrich, D. Wedekind, M. Tiedge, and S. Lenzen, “Immune cell infiltration, cytokine expression, and β-cell apoptosis during the development of type 1 diabetes in the spontaneously diabetic LEW.1AR1/Ztm-iddm rat,” Diabetes, vol. 54, no. 7, pp. 2041–2052, 2005. View at Publisher · View at Google Scholar · View at Scopus
  221. D. L. Eizirik and T. Mandrup-Poulsen, “A choice of death—the signal-transduction of immune-mediated beta-cell apoptosis,” Diabetologia, vol. 44, no. 12, pp. 2115–2133, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  222. K. L. A. Souza, E. Gurgul-Convey, M. Elsner, and S. Lenzen, “Interaction between pro-inflammatory and anti-inflammatory cytokines in insulin-producing cells,” Journal of Endocrinology, vol. 197, no. 1, pp. 139–150, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  223. P. Pirot, D. L. Eizirik, and A. K. Cardozo, “Interferon-γ potentiates endoplasmic reticulum stress-induced death by reducing pancreatic beta cell defence mechanisms,” Diabetologia, vol. 49, no. 6, pp. 1229–1236, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  224. S. Lortz, E. Gurgul-Convey, S. Lenzen, and M. Tiedge, “Importance of mitochondrial superoxide dismutase expression in insulin-producing cells for the toxicity of reactive oxygen species and proinflammatory cytokines,” Diabetologia, vol. 48, no. 8, pp. 1541–1548, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  225. A. K. Azevedo-Martins, S. Lortz, S. Lenzen, R. Curi, D. L. Eizirik, and M. Tiedge, “Improvement of the mitochondrial antioxidant defense status prevents cytokine-induced nuclear factor-κB activation in insulin-producing cells,” Diabetes, vol. 52, no. 1, pp. 93–101, 2003. View at Publisher · View at Google Scholar · View at Scopus
  226. S. Lenzen, J. Drinkgern, and M. Tiedge, “Low antioxidant enzyme gene expression in pancreatic islets compared with various other mouse tissues,” Free Radical Biology & Medicine, vol. 20, no. 3, pp. 463–466, 1996. View at Publisher · View at Google Scholar · View at Scopus
  227. M. Tiedge, S. Lortz, J. Drinkgern, and S. Lenzen, “Relation between antioxidant enzyme gene expression and antioxidative defense status of insulin-producing cells,” Diabetes, vol. 46, no. 11, pp. 1733–1742, 1997. View at Scopus
  228. E. Gurgul, S. Lortz, M. Tiedge, A. Jorns, and S. Lenzen, “Mitochondrial catalase overexpression protects insulin-producing cells against toxicity of reactive oxygen species and proinflammatory cytokines,” Diabetes, vol. 53, no. 9, pp. 2271–2280, 2004. View at Publisher · View at Google Scholar · View at Scopus
  229. D. L. Eizirik, A. K. Cardozo, and M. Cnop, “The role for endoplasmic reticulum stress in diabetes mellitus,” Endocrine Reviews, vol. 29, no. 1, pp. 42–61, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  230. J. L. Evans, I. D. Goldfine, B. A. Maddux, and G. M. Grodsky, “Are oxidative stress-activated signaling pathways mediators of insulin resistance and β-cell dysfunction?” Diabetes, vol. 52, no. 1, pp. 1–8, 2003. View at Publisher · View at Google Scholar · View at Scopus
  231. E. Diakogiannaki, S. Dhayal, C. E. Childs, P. C. Calder, H. J. Welters, and N. G. Morgan, “Mechanisms involved in the cytotoxic and cytoprotective actions of saturated versus monounsaturated long-chain fatty acids in pancreatic β-cells,” Journal of Endocrinology, vol. 194, no. 2, pp. 283–291, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  232. R. Robertson, H. Zhou, T. Zhang, and J. S. Harmon, “Chronic oxidative stress as a mechanism for glucose toxicity of the beta cell in type 2 diabetes,” Cell Biochemistry & Biophysics, vol. 48, no. 2-3, pp. 139–146, 2007. View at Publisher · View at Google Scholar · View at Scopus
  233. M. Cnop, N. Welsh, J.-C. Jonas, A. Jorns, S. Lenzen, and D. L. Eizirik, “Mechanisms of pancreatic β-cell death in type 1 and type 2 diabetes: many differences, few similarities,” Diabetes, vol. 54, supplement 2, pp. S97–S107, 2005. View at Publisher · View at Google Scholar · View at Scopus
  234. A. Jorns, K. J. Rath, O. Bock, and S. Lenzen, “Beta cell death in hyperglycaemic Psammomys obesus is not cytokine-mediated,” Diabetologia, vol. 49, no. 11, pp. 2704–2712, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  235. I. Kharroubi, L. Ladriere, A. K. Cardozo, Z. Dogusan, M. Cnop, and D. L. Eizirik, “Free fatty acids and cytokines induce pancreatic β-cell apoptosis by different mechanisms: role of nuclear factor-κB and endoplasmic reticulum stress,” Endocrinology, vol. 145, no. 11, pp. 5087–5096, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  236. F. M. Ashcroft, “KATP channels and insulin secretion: a key role in health and disease,” Biochemical Society Transactions, vol. 34, part 2, pp. 243–246, 2006. View at Scopus
  237. M. C. Saleh, M. B. Wheeler, and C. B. Chan, “Uncoupling protein-2: evidence for its function as a metabolic regulator,” Diabetologia, vol. 45, no. 2, pp. 174–187, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  238. J. H. Moffitt, B. A. Fielding, R. Evershed, R. Berstan, J. M. Currie, and A. Clark, “Adverse physicochemical properties of tripalmitin in beta cells lead to morphological changes and lipotoxicity in vitro,” Diabetologia, vol. 48, no. 9, pp. 1819–1829, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  239. M. Delepine, M. Nicolino, T. Barrett, M. Golamaully, G. M. Lathrop, and C. Julier, “EIF2AK3, encoding translation initiation factor 2-α kinase 3, is mutated in patients with Wolcott-Rallison syndrome,” Nature Genetics, vol. 25, no. 4, pp. 406–409, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  240. H. P. Harding, H. Zeng, Y. Zhang, et al., “Diabetes mellitus and exocrine pancreatic dysfunction in perk-/- mice reveals a role for translational control in secretory cell survival,” Molecular Cell, vol. 7, no. 6, pp. 1153–1163, 2001. View at Publisher · View at Google Scholar · View at Scopus
  241. J. Wang, T. Takeuchi, S. Tanaka, et al., “A mutation in the insulin 2 gene induces diabetes with severe pancreatic β-cell dysfunction in the Mody mouse,” Journal of Clinical Investigation, vol. 103, no. 1, pp. 27–37, 1999. View at Scopus
  242. S. Oyadomari, A. Koizumi, K. Takeda, et al., “Targeted disruption of the Chop gene delays endoplasmic reticulum stress-mediated diabetes,” Journal of Clinical Investigation, vol. 109, no. 4, pp. 525–532, 2002. View at Publisher · View at Google Scholar · View at Scopus
  243. W. C. Ladiges, S. E. Knoblaugh, J. F. Morton, et al., “Pancreatic β-cell failure and diabetes in mice with a deletion mutation of the endoplasmic reticulum molecular chaperone gene P58IPK,” Diabetes, vol. 54, no. 4, pp. 1074–1081, 2005. View at Publisher · View at Google Scholar · View at Scopus
  244. P. Kovacs, X. Yang, P. A. Permana, C. Bogardus, and L. J. Baier, “Polymorphisms in the oxygen-regulated protein 150 gene (ORP150) are associated with insulin resistance in Pima Indians,” Diabetes, vol. 51, no. 5, pp. 1618–1621, 2002. View at Scopus
  245. K. Ozawa, M. Miyazaki, M. Matsuhisa, et al., “The endoplasmic reticuluin chaperone improves insulin resistance in type 2 diabetes,” Diabetes, vol. 54, no. 3, pp. 657–663, 2005. View at Publisher · View at Google Scholar · View at Scopus
  246. U. Ozcan, E. Yilmaz, L. Ozcan, et al., “Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes,” Science, vol. 313, no. 5790, pp. 1137–1140, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  247. S. Gandhi and N. W. Wood, “Molecular pathogenesis of Parkinson's disease,” Human Molecular Genetics, vol. 14, no. 18, pp. 2749–2755, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  248. S. Przedborski, “Pathogenesis of nigral cell death in Parkinson's disease,” Parkinsonism and Related Disorders, vol. 11, supplement 1, pp. S3–S7, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  249. D. Sulzer, “Multiple hit hypotheses for dopamine neuron loss in Parkinson's disease,” Trends in Neurosciences, vol. 30, no. 5, pp. 244–250, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  250. K. Steece-Collier, E. Maries, and J. H. Kordower, “Etiology of Parkinson's disease: genetics and environment revisited,” Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 22, pp. 13972–13974, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  251. J. M. Hatcher, K. D. Pennell, and G. W. Miller, “Parkinson's disease and pesticides: a toxicological perspective,” Trends in Pharmacological Sciences, vol. 29, no. 6, pp. 322–329, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  252. H. Mochizuki, “Gene therapy for Parkinson's disease,” Expert Review of Neurotherapeutics, vol. 7, no. 8, pp. 957–960, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  253. M. J. Farrer, “Genetics of Parkinson's disease: paradigm shifts and future prospects,” Nature Reviews Genetics, vol. 7, no. 4, pp. 306–318, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  254. M. W. Dodson and M. Guo, “Pink1, Parkin, DJ-1 and mitochondrial dysfunction in Parkinson's disease,” Current Opinion in Neurobiology, vol. 17, no. 3, pp. 331–337, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  255. R. Banerjee, A. A. Starkov, M. F. Beal, and B. Thomas, “Mitochondrial dysfunction in the limelight of Parkinson's disease pathogenesis,” Biochimica et Biophysica Acta, vol. 1792, no. 7, pp. 651–663, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  256. J. L. St Martin, J. Klucken, T. F. Outeiro, et al., “Dopaminergic neuron loss and up-regulation of chaperone protein mRNA induced by targeted over-expression of alpha-synuclein in mouse substantia nigra,” Journal of Neurochemistry, vol. 100, no. 6, pp. 1449–1457, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  257. J. Klucken, Y. Shin, E. Masliah, B. T. Hyman, and P. J. McLean, “Hsp70 reduces α-synuclein aggregation and toxicity,” Journal of Biological Chemistry, vol. 279, no. 24, pp. 25497–25502, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  258. P. F. Durrenberger, M. D. Filiou, L. B. Moran, et al., “DnaJB6 is present in the core of Lewy bodies and is highly up-regulated in Parkinsonian astrocytes,” Journal of Neuroscience Research, vol. 87, no. 1, pp. 238–245, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  259. J. Fargnoli, T. Kunisada, A. J. Fornace Jr., E. L. Schneider, and N. J. Holbrook, “Decreased expression of heat shock protein 70 mRNA and protein after heat treatment in cells of aged rats,” Proceedings of the National Academy of Sciences of the United States of America, vol. 87, no. 2, pp. 846–850, 1990. View at Scopus
  260. J. J. M. Hoozemans, E. S. van Haastert, P. Eikelenboom, R. A. I. de Vos, J. M. Rozemuller, and W. Scheper, “Activation of the unfolded protein response in Parkinson's disease,” Biochemical & Biophysical Research Communications, vol. 354, no. 3, pp. 707–711, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  261. W. A. Holtz and K. L. O'Malley, “Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons,” Journal of Biological Chemistry, vol. 278, no. 21, pp. 19367–19377, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  262. 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,” Journal of Neuroscience, vol. 22, no. 24, pp. 10690–10698, 2002. View at Scopus
  263. R. M. Silva, V. Ries, T. F. Oo, et al., “CHOP/GADD153 is a mediator of apoptotic death in substantia nigra dopamine neurons in an in vivo neurotoxin model of parkinsonism,” Journal of Neurochemistry, vol. 95, no. 4, pp. 974–986, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  264. S. A. Fisher, B. L. Langille, and D. Srivastava, “Apoptosis during cardiovascular development,” Circulation Research, vol. 87, no. 10, pp. 856–864, 2000. View at Scopus
  265. T. N. James, “Normal and abnormal consequences of apoptosis in the human heart: from postnatal morphogenesis to paroxysmal arrhythmias,” Circulation, vol. 90, no. 1, pp. 556–573, 1994. View at Scopus
  266. C. Gill, R. Mestril, and A. Samali, “Losing heart: the role of apoptosis in heart disease—a novel therapeutic target?” FASEB Journal, vol. 16, no. 2, pp. 135–146, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  267. A. B. Gustafsson and R. A. Gottlieb, “Mechanisms of apoptosis in the heart,” Journal of Clinical Immunology, vol. 23, no. 6, pp. 447–459, 2003. View at Publisher · View at Google Scholar · View at Scopus
  268. H. Fliss and D. Gattinger, “Apoptosis in ischemic and reperfused rat myocardium,” Circulation Research, vol. 79, no. 5, pp. 949–956, 1996. View at Scopus
  269. R. A. Gottlieb, K. O. Burleson, R. A. Kloner, B. M. Babior, and R. L. Engler, “Reperfusion injury induces apoptosis in rabbit cardiomyocytes,” Journal of Clinical Investigation, vol. 94, no. 4, pp. 1621–1628, 1994. View at Scopus
  270. J. Misao, Y. Hayakawa, M. Ohno, S. Kato, T. Fujiwara, and H. Fujiwara, “Expression of bcl-2 protein, an inhibitor of apoptosis, and Bax, an accelerator of apoptosis, in ventricular myocytes of human hearts with myocardial infarction,” Circulation, vol. 94, no. 7, pp. 1506–1512, 1996. View at Scopus
  271. J. Narula, N. Haider, R. Virmani, et al., “Apoptosis in myocytes in end-stage heart failure,” New England Journal of Medicine, vol. 335, no. 16, pp. 1182–1189, 1996. View at Publisher · View at Google Scholar · View at Scopus
  272. G. Olivetti, R. Abbi, F. Quaini, et al., “Apoptosis in the failing human heart,” New England Journal of Medicine, vol. 336, no. 16, pp. 1131–1141, 1997. View at Publisher · View at Google Scholar · View at Scopus
  273. G. Olivetti, F. Quaini, R. Sala, et al., “Acute myocardial infarction in humans is associated with activation of programmed myocyte cell death in the surviving portion of the heart,” Journal of Molecular & Cellular Cardiology, vol. 28, no. 9, pp. 2005–2016, 1996. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  274. A. Saraste, K. Pulkki, M. Kallajoki, K. Henriksen, M. Parvinen, and L.-M. Voipio-Pulkki, “Apoptosis in human acute myocardial infarction,” Circulation, vol. 95, no. 2, pp. 320–323, 1997. View at Scopus
  275. S. A. Cook, P. H. Sugden, and A. Clerk, “Regulation of bcl-2 family proteins during development and in response to oxidative stress in cardiac myocytes association with changes in mitochondrial membrane potential,” Circulation Research, vol. 85, no. 10, pp. 940–949, 1999. View at Scopus
  276. R. von Harsdorf, P.-F. Li, and R. Dietz, “Signaling pathways in reactive oxygen species-induced cardiomyocyte apoptosis,” Circulation, vol. 99, no. 22, pp. 2934–2941, 1999. View at Scopus
  277. M. Neuss, R. Monticone, M. S. Lundberg, A. T. Chesley, E. Fleck, and M. T. Crow, “The apoptotic regulatory protein ARC (apoptosis repressor with caspase recruitment domain) prevents oxidant stress-mediated cell death by preserving mitochondrial function,” Journal of Biological Chemistry, vol. 276, no. 36, pp. 33915–33922, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  278. C. Fleury, B. Mignotte, and J.-L. Vayssiere, “Mitochondrial reactive oxygen species in cell death signaling,” Biochimie, vol. 84, no. 2-3, pp. 131–141, 2002. View at Publisher · View at Google Scholar · View at Scopus
  279. J. McMurray, J. McLay, M. Chopra, A. Bridges, and J. J. F. Belch, “Evidence for enhanced free radical activity in chronic congestive heart failure secondary to coronary artery disease,” American Journal of Cardiology, vol. 65, no. 18, pp. 1261–1262, 1990. View at Publisher · View at Google Scholar · View at Scopus
  280. N. Singh and S. Aggarwal, “The effect of active oxygen generated by xanthine/xanthine oxidase on genes and signal transduction in mouse epidermal JB6 cells,” International Journal of Cancer, vol. 62, no. 1, pp. 107–114, 1995. View at Publisher · View at Google Scholar · View at Scopus
  281. J. L. Zweier, J. T. Flaherty, and M. L. Weisfeldt, “Direct measurement of free radical generation following reperfusion of ischemic myocardium,” Proceedings of the National Academy of Sciences of the United States of America, vol. 84, no. 5, pp. 1404–1407, 1987. View at Scopus
  282. S. E. Logue, A. B. Gustafsson, A. Samali, and R. A. Gottlieb, “Ischemia/reperfusion injury at the intersection with cell death,” Journal of Molecular & Cellular Cardiology, vol. 38, no. 1, pp. 21–33, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  283. K. Suzuki, Y. Sawa, Y. Kaneda, H. Ichikawa, R. Shirakura, and H. Matsuda, “In vivo gene transfection with heat shock protein 70 enhances myocardial tolerance to ischemia-reperfusion injury in rat,” Journal of Clinical Investigation, vol. 99, no. 7, pp. 1645–1650, 1997. View at Scopus
  284. A. N. Aleshin, Y. Sawa, S. Kitagawa-Sakakida, et al., “150-kDa oxygen-regulated protein attenuates myocardial ischemia-reperfusion injury in rat heart,” Journal of Molecular & Cellular Cardiology, vol. 38, no. 3, pp. 517–525, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  285. C.-Y. Li, J.-S. Lee, Y.-G. Ko, J.-I. Kim, and J.-S. Seo, “Heat shock protein 70 inhibits apoptosis downstream of cytochrome c release and upstream of caspase-3 activation,” Journal of Biological Chemistry, vol. 275, no. 33, pp. 25665–25671, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  286. M. A. H. Talukder, A. Kalyanasundaram, X. Zhao, et al., “Expression of SERCA isoform with faster Ca2+ transport properties improves postischemic cardiac function and Ca2+ handling and decreases myocardial infarction,” American Journal of Physiology, vol. 293, no. 4, pp. H2418–H2428, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  287. S. W. Lowe and A. W. Lin, “Apoptosis in cancer,” Carcinogenesis, vol. 21, no. 3, pp. 485–495, 2000. View at Scopus
  288. D. Hanahan and R. A. Weinberg, “The hallmarks of cancer,” Cell, vol. 100, no. 1, pp. 57–70, 2000. View at Scopus
  289. S. W. Lowe, E. Cepero, and G. Evan, “Intrinsic tumour suppression,” Nature, vol. 432, no. 7015, pp. 307–315, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  290. R. W. Johnstone, A. A. Ruefli, and S. W. Lowe, “Apoptosis: a link between cancer genetics and chemotherapy,” Cell, vol. 108, no. 2, pp. 153–164, 2002. View at Publisher · View at Google Scholar · View at Scopus
  291. S. Fulda and K.-M. Debatin, “Targeting apoptosis pathways in cancer therapy,” Current Cancer Drug Targets, vol. 4, no. 7, pp. 569–576, 2004. View at Publisher · View at Google Scholar · View at Scopus
  292. G. Makin and C. Dive, “Apoptosis and cancer chemotherapy,” Trends in Cell Biology, vol. 11, no. 11, pp. S22–S26, 2001. View at Publisher · View at Google Scholar · View at Scopus
  293. C. Friesen, S. Fulda, and K.-M. Debatin, “Deficient activation of the CD95 (APO-1/Fas) system in drug-resistant cells,” Leukemia, vol. 11, no. 11, pp. 1833–1841, 1997. View at Scopus
  294. S. Fulda, M. Los, C. Friesen, and K.-M. Debatin, “Chemosensitivity of solid tumor cells in vitro is related to activation of the CD95 system,” International Journal of Cancer, vol. 76, no. 1, pp. 105–114, 1998. View at Publisher · View at Google Scholar · View at Scopus
  295. T. Maeda, Y. Yamada, R. Moriuchi, et al., “Fas gene mutation in the progression of adult T cell leukemia,” Journal of Experimental Medicine, vol. 189, no. 7, pp. 1063–1071, 1999. View at Publisher · View at Google Scholar · View at Scopus
  296. T. H. Landowski, N. Qu, I. Buyuksal, J. S. Painter, and W. S. Dalton, “Mutations in the Fas antigen in patients with multiple myeloma,” Blood, vol. 90, no. 11, pp. 4266–4270, 1997. View at Scopus
  297. K. Gronbaek, P. T. Straten, E. Ralfkiaer, et al., “Somatic fas mutations in non-Hodgkin's lymphoma: association with extranodal disease and autoimmunity,” Blood, vol. 92, no. 9, pp. 3018–3024, 1998. View at Scopus
  298. S. H. Lee, M. S. Shin, W. S. Park, et al., “Alterations of Fas (Apo-1/CD95) gene in non-small cell lung cancer,” Oncogene, vol. 18, no. 25, pp. 3754–3760, 1999. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  299. S. H. Lee, M. S. Shin, W. S. Park, et al., “Alterations of Fas (APO-1/CD95) gene in transitional cell carcinomas of urinary bladder,” Cancer Research, vol. 59, no. 13, pp. 3068–3072, 1999. View at Scopus
  300. W. S. Park, R. R. Oh, Y. S. Kim, et al., “Somatic mutations in the death domain of the Fas (Apo-I/CD95) gene in gastric cancer,” Journal of Pathology, vol. 193, no. 2, pp. 162–168, 2001. View at Publisher · View at Google Scholar · View at Scopus
  301. I. I. Wistuba, C. Behrens, A. K. Virmani, et al., “Allelic losses at chromosome 8p21–23 are early and frequent events in the pathogenesis of lung cancer,” Cancer Research, vol. 59, no. 8, pp. 1973–1979, 1999. View at Scopus
  302. M. Emi, Y. Fujiwara, T. Nakajima, et al., “Frequent loss of heterozygosity for loci on chromosome 8p in hepatocellular carcinoma, colorectal cancer, and lung cancer,” Cancer Research, vol. 52, no. 19, pp. 5368–5372, 1992. View at Scopus
  303. O. Micheau, “Cellular FLICE-inhibitory protein: an attractive therapeutic target?” Expert Opinion on Therapeutic Targets, vol. 7, no. 4, pp. 559–573, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  304. A. M. Hunter, E. C. LaCasse, and R. G. Korneluk, “The inhibitors of apoptosis (IAPs) as cancer targets,” Apoptosis, vol. 12, no. 9, pp. 1543–1568, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  305. S. Fulda, “Caspase-8 in cancer biology and therapy,” Cancer Letters, vol. 281, no. 2, pp. 128–133, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  306. S. Kitada, I. M. Pedersen, A. D. Schimmer, and J. C. Reed, “Dysregulation of apoptosis genes in hematopoietic malignancies,” Oncogene, vol. 21, no. 21, pp. 3459–3474, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  307. N. Rampino, H. Yamamoto, Y. Ionov, et al., “Somatic frameshift mutations in the BAX gene in colon cancers of the microsatellite mutator phenotype,” Science, vol. 275, no. 5302, pp. 967–969, 1997. View at Publisher · View at Google Scholar · View at Scopus
  308. S. S. Zinkel, C. C. Ong, D. O. Ferguson, et al., “Proapoptotic BID is required for myeloid homeostasis and tumor suppression,” Genes and Development, vol. 17, no. 2, pp. 229–239, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  309. H. Tagawa, S. Karnan, R. Suzuki, et al., “Genome-wide array-based CGH for mantle cell lymphoma: identification of homozygous deletions of the proapoptotic gene BIM,” Oncogene, vol. 24, no. 8, pp. 1348–1358, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  310. C. Mestre-Escorihuela, F. Rubio-Moscardo, J. A. Richter, et al., “Homozygous deletions localize novel tumor suppressor genes in B-cell lymphomas,” Blood, vol. 109, no. 1, pp. 271–280, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  311. D. R. Fels and C. Koumenis, “The PERK/eIF2α/ATF4 module of the UPR in hypoxia resistance and tumor growth,” Cancer Biology & Therapy, vol. 5, no. 7, pp. 723–728, 2006. View at Scopus
  312. C. Koumenis and B. G. Wouters, ““Translating” tumor hypoxia: unfolded protein response (UPR)-dependent and UPR-independent pathways,” Molecular Cancer Research, vol. 4, no. 7, pp. 423–436, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  313. H.-C. Zheng, H. Takahashi, X.-H. Li, et al., “Overexpression of GRP78 and GRP94 are markers for aggressive behavior and poor prognosis in gastric carcinomas,” Human Pathology, vol. 39, no. 7, pp. 1042–1049, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  314. P. Pyrko, A. H. Schonthal, F. M. Hofman, T. C. Chen, and A. S. Lee, “The unfolded protein response regulator GRP78/BiP as a novel target for increasing chemosensitivity in malignant gliomas,” Cancer Research, vol. 67, no. 20, pp. 9809–9816, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  315. A. C. Koong, V. Chauhan, and L. Romero-Ramirez, “Targeting XBP-1 as a novel anti-cancer strategy,” Cancer Biology & Therapy, vol. 5, no. 7, pp. 756–759, 2006. View at Scopus
  316. S. Qin and P. B. Chock, “Implication of phosphatidylinositol 3-kinase membrane recruitment in hydrogen peroxide-induced activation of PI3K and Akt,” Biochemistry, vol. 42, no. 10, pp. 2995–3003, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  317. S. Pervaiz, J. Cao, O. S. P. Chao, Y. Y. Chin, and M.-V. Clement, “Activation of the RacGTPase inhibits apoptosis in human tumor cells,” Oncogene, vol. 20, no. 43, pp. 6263–6268, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  318. D. Mahalingam, R. Swords, J. S. Carew, S. T. Nawrocki, K. Bhalla, and F. J. Giles, “Targeting HSP90 for cancer therapy,” British Journal of Cancer, vol. 100, no. 10, pp. 1523–1529, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  319. C. Garrido, M. Brunet, C. Didelot, Y. Zermati, E. Schmitt, and G. Kroemer, “Heat shock proteins 27 and 70: anti-apoptotic proteins with tumorigenic properties,” Cell Cycle, vol. 5, no. 22, pp. 2592–2601, 2006. View at Scopus