Intracellular oxidative stress caused by ionizing radiation

Oxidative Stress, Disease and Cancer

Volumn , Issue , 2006, Pages 61-84

  Majima, Hideyuki J ^a   Indo, Hiroko P ^a   Tomita, Kazuo ^a   Suenaga, Shigeaki ^a   Motoori, Shigeatsu ^b   Kato, Hirotoshi ^c   Yen, Hsiu Chuan ^d   Ozawa, Toshihiko ^c  

^a KAGOSHIMA UNIVERSITY   (Japan)

^b CHIBA UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^c NATIONAL INSTITUTE OF RADIOLOGICAL SCIENCES   (Japan)

^d CHANG GUNG UNIVERSITY   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 84967444696     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1142/9781860948046_0002     Document Type: Chapter

References (68)

1. Hall HJ (ed.) DNA strand breaks and chromosomal aberrations. In: Radiobiology for the Radiologist, 4th edn. J.B. Lippincott Company, Philadelphia, 1994, pp. 15-27.
2. Ito A. Electron track simulation for microdosometry. In: Jenkins TM, Melson WR, Rindi A (eds.) Monte Carlo Transport of Electrons and Photons. Plenum Publishers, New York, 1988, pp. 361-382.
3. Sakai K, Okada S. Radiation-induced DNA damage and cellular lethality in cultured mammalian cells. Radiat. Res. 98: 479-490 (1984).
4. Ito A. Calculation of double strand break probability of DNA for low LET radiations based on Track structure analysis. In: Okamoto K (ed.) Nuclear and Atomic Data for Radiotherapy and Related Radiobiology. TECDOC Series 413, IAEA Publication, Vienna, 1987.
5. Coggle JE (ed.) Biological Effects of Radiation. Taylor & Francis, London, 1983.
6. Riley PA. Free radicals in biology: oxidative stress and the effects of ionizing radiation. Int. J. Radiat. Biol. 65: 27-33 (1994).
7. Schmidt-Ullrich RK, Dent P, Grant S, Mikkelsen RB, Valerie K. Signal transduction and cellular radiation responses. Radiat. Res. 153: 245-257 (2000).
8. Wallace SS. Enzymatic processing of radiation-induced free radical damage in DNA. Radiat. Res. 150(5 Suppl): S60-S79 (1998).
9. Halliwell B, Gutteridge JMC (eds.) Oxidative stress: adaptation, damage, repair and death. In: Free Radicals in Biology and Medicine, 3rd edn. Oxford University Press, Oxford, 1999, pp. 246-350.
10. Buettner GR, Jurkiewicz BA. Catalytic metals, ascorbate and free radicals: combinations to avoid. Radiat. Res. 145: 532-541 (1996).
11. Chapman JD. Biophysical models of mammalian cell inactivation by radiation. In: Meyn RE, Withers HR (eds.) Radiation Biology in Cancer Research. Raven Press, New York, 1980, pp. 21-32.
12. Rudner J, Jendrossek V, Belka C. New insights in the role of Bcl-2, Bcl-2 and the endoplasmic reticulum. Apoptosis 7: 441-447 (2002).
13. Dent P, Yacoub A, Contessa J, Caron R, Amorino G, Valerie K, Hagan MP, Grant S, Schmidt-Ullrich R. Stress and radiation-induced activation of multiple intracellular signaling pathways. Radiat. Res. 159: 283-300 (2003).
14. Kerr JFR, Searle J. Apoptosis its nature and kinetic role. In: Radiation Biology in Cancer Research. Raven Press, New York, 1980, pp. 367-384.
15. Hengartner MO. The biochemistry of apoptosis. Nature 407: 770-776 (2000).
16. Rich T, Allen RL, Wyllie AH. Defying death after DNA damage. Nature 407: 777-783 (2000).
17. Muzio M, Stockwell BR, Stennicke HR, Salvesen GS, Dixit VM. An induced proximity model for caspase-8 activation. J. Biol. Chem. 273: 2926-2930 (1998).
18. Irmler M, Thome M, Hahne M, Schneider P, Hofmann K, Steiner V, Bodmer JL, Schroter M, Burns K, Mattmann C, Rimoldi D, French LE, Tschopp J. Inhibition of death receptor signals by cellular FLIP. Nature 388: 190-195 (1997).
19. Powell WC, Fingleton B, Wilson CL, Boothby M, Matrisian, LM. The metalloproteinase matrilysin proteolytically generates active soluble Fas ligand and potentiates epithelial cell apoptosis. Curr. Biol. 9: 1441-1447 (1999).
20. Brew K, Dinakarpandian D, Nagase H. Tissue inhibitors of metalloproteinases: evolution, structure and function. Biochim. Biophys. Acta 1477: 267-283 (2000).
21. Kuwabara M, Takahashi K, Inanami O. Induction of apoptosis through the activation of SAPK/JNK followed by the expression of death receptor Fas in X-irradiated cells. J. Radiat. Res. 44: 203-209 (2003).
22. Franklin CC, Srikanth S, Kraft AS. Conditional expression of mitogenactivated protein kinase phosphatase-1, MKP-1, is cytoprotective against UV-induced apoptosis. Proc. Natl. Acad. Sci. USA 95: 3014-3019 (1998).
23. Ruvolo PP, Deng X, May WS. Phosphorylation of Bcl2 and regulation of apoptosis. Leukemia 15: 515-52l (2001).
24. Liston P, Fong WG, Korneluk RG. The inhibitors of apoptosis: there is more to life than Bcl2. Oncogene 22: 8568-8580 (2003).
25. Robertson GS, Crocker SJ, Nicholson DW, Schulz JB. Neuroprotection by the inhibition of apoptosis. Brain Pathol. 10: 283-292 (2000).
26. Du C, Fang M, Li Y, Li L, Wang X. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 102: 33-42 (2000).
27. Verhagen AM, Ekert PG, Pakusch M, Silke J, Connolly LM, Reid GE, Moritz RL, Simpson RJ, Vaux DL. Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell 102: 43-53 (2000).
28. Barnhart BC, Alappat EC, Peter ME. The CD95 type I/type II model. Semin. Immunol. 15: 185-193 (2003).
29. Liu X, Li P, Widlak P, Zou H, Luo X, Garrard WT, Wang X. The 40-kDa subunit of DNA fragmentation factor induces DNA fragmentation and chromatin condensation during apoptosis. Proc. Natl. Acad. Sci. USA 95: 8461-8466 (1998).
30. Widlak, P. The DFF40/CAD endonuclease and its role in apoptosis. Acta Biochim. Pol. 47: 1037-1044 (2000).
31. Grand RJ, Milner AE, Mustoe T, Johnson GD, Owen D, Grant ML, Gregory CD. Anovel protein expressed inmammalian cells undergoing apoptosis. Exp. Cell Res. 218: 439-451 (1995).
32. Carstea ED, Morris JA, Coleman KG, Loftus SK, Zhang D, Cummings C, Gu J, Rosenfeld MA, Pavan WJ, Krizman DB, Nagle J, Polymeropoulos MH, Sturley SL, Ioannou YA, Higgins ME, Comly M, Cooney A, Brown A, Kaneski CR, Blanchette-Mackie EJ, Dwyer NK, Neufeld EB, Chang TY, Liscum L, Strauss JF III, Ohno K, Zeigler M, Carmi R, Sokol J, Markie D, O’Neill RR, van Diggelen OP, Elleder M, Patterson MC, Brady RO, Vanier MT, Pentchev PG, Tagle DA. Niemann-Pick C1 disease gene: homology to mediators of cholesterol homeostasis. Science 277: 228-231 (1997).
33. Erickson RP, Bernard O. Studies on neuronal death in the mouse model of Niemann-Pick C disease. J. Neurosci. Res. 68: 738-744 (2002).
34. Feng B, Yao PM, Li Y, Devlin CM, Zhang D, Harding HP, Sweeney M, Rong JX, Kuriakose G, Fisher EA, Marks AR, Ron D, Tabas I. The endoplasmic reticulum is the site of cholesterol-induced cytotoxicity in macrophages. Nat. Cell Biol. 9: 781-792 (2003).
35. Weitzman JB, Fiette L, Matsuo K, Yaniv M. JunD protects cells from p53-dependent senescence and apoptosis. Mol. Cell 6: 1109-1119 (2000).
36. Pidgeon GP, Kandouz M, Meram A, Honn KV. Mechanisms controlling cell cycle arrest and induction of apoptosis after 12-lipoxygenase inhibition in prostate cancer cells. Cancer Res. 62: 2721-2727 (2002).
37. Shi C, Yu L, Yang F, Yan J, Zeng H. A novel organoselenium compound induces cell cycle arrest and apoptosis in prostate cancer cell lines. Biochem. Biophys. Res. Commun. 309: 578-583 (2003).
38. Jaattela, M. Escaping cell death: survival proteins in cancer. Exp. Cell Res. 248: 30-43 (1999).
39. Xanthoudakis S, Nicholson DW. Heat-shock proteins as death determinants. Nat. Cell Biol. 2: E163-E165 (2000).
40. Setsukinai K, Urano Y, Kakinuma K, Majima HJ, Nagano T. Development of novel fluorescence probes that can reliably detect reactive oxygen species and distinguish specific species. J. Biol. Chem. 278: 3170-3175 (2003).
41. Halliwell B, Gutteridge JMC (eds.) Antioxidant defences. In: Free Radicals in Biology and Medicine, 3rd edn. Oxford University Press, Oxford, Oxford, 1999, pp. 105-245.
42. Fridovich I. Superoxide radical and superoxide dismutases. Annu. Rev. Biochem. 64: 97-112 (1995).
43. Sawyer DT, Valentine JS. How super is superoxide? Acc. Chem. Res. 14: 393-400 (1981).
44. Winterbourn CC. Comparison of superoxide with other reducing agents in the biological production of hydroxyl radicals. Biochem. J. 182: 625-628 (1979).
45. Babbs CF, Griffin DW. Scatchard analysis of methane sulfinic acid production from dimethyl sulfoxide: a method to quantify hydroxyl radical formation in physiologic systems. Free Radic. Biol. Med. 6: 493-503 (1989).
46. Blough NV, Zafiriou OC. Reaction of superoxide with nitric oxide to form peroxonitrite in alkaline aqueous solution. Inorg. Chem. 24: 3502-3504 (1985).
47. Beckman JS, Beckman TW, Chen J, Marshall PA, Freeman, BA. Apparent hydroxyl radical production by peroxynitrite: implications for endothelial injury from nitric oxide and superoxide. Proc. Natl. Acad. Sci. USA 87: 1620-1624 (1990).
48. Keller JN, Kindy MS, Holtsberg FW, St. Clair DK, Yen HC, Germeyer A, Steiner SM, Bruce-Keller AJ, Hutchins JB, Mattson MP. Mitochondrial manganese superoxide dismutase prevents neural apoptosis and reduces ischemic brain injury: suppression of peroxynitrite production, lipid peroxidation, and mitochondrial dysfunction. J. Neurosci. 18: 687-697 (1998).
49. Radi R, Beckman JS, Bush KM, Freeman BA. Peroxynitrite-induced membrane lipid peroxidation: the cytotoxic potential of superoxide and nitric oxide. Arch. Biochem. Biophys. 288: 481-487 (1991).
50. Esterbauer H, Schaur RJ, Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic. Biol. Med. 11: 81-128 (1991).
51. Pryor WA, Porter NA. Suggested mechanismsfor the production of 4-hydroxy-2-nonenal from the autoxidation of polyunsaturated fatty acids. Free Radic. Biol. Med. 8: 541-543 (1990).
52. 2-resistant cell lines. Do aldehydic by-products of lipid peroxidation contribute to oxidative stress? Biochem. J. 267: 453-459 (1990).
53. McCord JM, Fridovich I. Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein). J. Biol. Chem. 244: 6049-6055 (1969).
54. Weisiger RA, Fridovich I. Mitochondrial superoxide dismutase: site of synthesis and intramitochondrial localization. J. Biol. Chem. 248: 4793-4796 (1973).
55. Fukai T, Siegfried MR, Ushio-Fukai M, Cheng Y, Kojda G, Harrison DG. Regulation of the vascular extracellular superoxide dismutase by nitric oxide and exercise training. J. Clin. Invest. 105: 1631-1639 (2000).
56. Boveris A, Cadenas E. Mitochondrial production of superoxide anions and its relationship to the antimycin insensitive respiration. FEBS Lett. 54: 311-314 (1975).
57. Takeshige K, Minakami S. NADH- and NADPH-dependent formation of superoxide anions by bovine heart submitochondrial particles and NADH-ubiquinone reductase preparation. Biochem. J. 180: 129-135 (1979).
58. Majima HJ, Oberley TD, Furukawa K, Mattson MP, Yen HC, Szweda LI, St. Clair DK. Prevention of mitochondrial injury by manganese superoxide dismutase reveals a primary mechanismfor alkaline-induced cell death. J. Biol. Chem. 273: 8217-8224 (1998).
59. Mattson MP. Apoptosis in neurodegenerative disorders. Nat. Rev. Mol. Cell Biol. 1: 120-129 (2000).
60. Mattson MP, Duan W, Pedersen WA, Culmsee C. Neurodegenerative disorders and ischemic brain diseases. Apoptosis 6: 69-81 (2001).
61. Motoori S, Majima HJ, Ebara M, Kato H, Hirai F, Kakinuma S, Yamaguchi C, Ozawa T, Nagano T, Tsujii H, Saisho H. Overexpression of mitochondrial manganese superoxide dismutase protects against radiation-induced cell death in the human hepatocellular carcinoma cell line, HLE. Cancer Res. 61: 5382-5388 (2001).
62. Hirai F, Motoori S, Kakinuma S, Tomita K, Indo HP, Kato H, Yamaguchi T, Yen H-C, St. Clair DK, Nagano T, Ozawa T, Saisho H, Majima HJ. Mitochondrial signal lacking manganese superoxide dismutase failed to prevent cell death by reoxygenation following hypoxia in a human pancreatic cancer cell line, KP4. Antioxid. Redox Signal. 6: 523-535 (2004).
63. Doonan S, Marra E, Passarella S, Saccone C, Quagliariello E. Transport of proteins into mitochondria. Int. Rev. Cytol. 91: 141-186 (1984).
64. Martinus RD, Ryan MT, Naylor DJ, Herd SM, Hoogeraad NJ, Høj PB. Role of chaperones in the biogenesis and maintenance of the mitochondrion. FASEB J. 9: 371-378 (1995).
65. Mihara K, Omura T. Cytoplasmic chaperones in precursor targeting to mitochondria: the role of MSF and hsp70. Trends Cell Biol. 6: 104-108 (1996).
66. Lithgow T. Targeting of proteins to mitochondria. FEBS Lett. 476: 22-26 (2000).
67. Kruman I, Bruce-Keller AJ, Bredesen D, Waeg G, Mattson MP. Evidence that 4-hydroxynonenal mediates oxidative stress-induced neuronal apoptosis. J. Neurosci. 17: 5089-5100 (1997).
68. Cheng J-Z, Singhal SS, Saini M, Singhal J, Piper JT, Van Kuijk FJ, Zimniak P, Awasthi YC, Awasthi S. Effects of mGST A4 transfection on 4-hydroxynonenalmediated apoptosis and differentiation of K562 human erythroleukemia cells. Arch. Biochem. Biophys. 372: 29-36 (1999).