Potent induction of total cellular GSH and NQO1 as well as mitochondrial GSH by 3H-1,2-dithiole-3-thione in SH-SY5Y neuroblastoma cells and primary human neurons: Protection against neurocytotoxicity elicited by dopamine, 6-hydroxydopamine, 4-hydroxy-2-nonenal, or hydrogen peroxide

Brain Research

Volumn 1197, Issue , 2008, Pages 159-169

  Jia, Zhenquan ^a   Zhu, Hong ^a   Misra, Hara P ^a,b   Li, Yunbo ^a,b  

^a EDWARD VIA COLLEGE OF OSTEOPATHIC MEDICINE   (United States)

^b VIRGINIA MARYLAND REGIONAL COLLEGE OF VETERINARY MEDICINE   (United States)

Author keywords

3H 1,2 dithiole 3 thione; 4 hydroxy 2 nonenal; 6 hydroxydopamine; Cytotoxicity; Dopamine; Glutathione; H2O2; NAD(P)H:quinone oxidoreductase 1; SH SY5Y neuroblastoma cell

Indexed keywords

1,2 DITHIOLE 3 THIONE DERIVATIVE; 3H 1,2 DITHIOLE 3 THIONE; 4 HYDROXYNONENAL; DOPAMINE; GAMMA GLUTAMYLCYSTEINE; GLUTATHIONE; HYDROGEN PEROXIDE; MESSENGER RNA; OXIDOPAMINE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); UNCLASSIFIED DRUG;

ARTICLE; CELL LINE; CELL PROTECTION; CELL VIABILITY; CONCENTRATION RESPONSE; CONTROLLED STUDY; CYTOTOXICITY; ELECTROPHILIC STRESS; ENZYME INDUCTION; ENZYME SUBUNIT; HUMAN; HUMAN CELL; NERVE CELL; NEUROBLASTOMA CELL; NEUROTOXICITY; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN EXPRESSION;

ALDEHYDES; ANTIOXIDANTS; CELL LINE, TUMOR; CELLS, CULTURED; DOPAMINE; GLUTATHIONE; HUMANS; HYDROGEN PEROXIDE; MITOCHONDRIA; NAD(P)H DEHYDROGENASE (QUINONE); NERVE DEGENERATION; NEURONS; NEUROPROTECTIVE AGENTS; OXIDATIVE STRESS; OXIDOPAMINE; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RNA, MESSENGER; THIONES; THIOPHENES;

EID: 39249084968     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.brainres.2007.12.044     Document Type: Article

References (54)

1. Aebi H. Catalase in vitro. Methods Enzymol. 105 (1984) 121-126
2. Ahlskog J.E. Parkinson's disease: new treatment strategies. Compr. Ther. 16 (1990) 41-46
3. Alam Z.I., Daniel S.E., Lees A.J., Marsden D.C., Jenner P., and Halliwell B. A generalised increase in protein carbonyls in the brain in Parkinson's but not incidental Lewy body disease. J. Neurochem. 69 (1997) 1326-1329
4. Alam Z.I., Jenner A., Daniel S.E., Lees A.J., Cairns N., Marsden C.D., Jenner P., and Halliwell B. Oxidative DNA damage in the parkinsonian brain: an apparent selective increase in 8-hydroxyguanine levels in substantia nigra. J. Neurochem. 69 (1997) 1196-1203
5. Anderson M.E. Glutathione: an overview of biosynthesis and modulation. Chem. Biol. Interact. 111-112 (1998) 1-14
6. Beal M.F. Mitochondria, oxidative damage, and inflammation in Parkinson's disease. Ann. N. Y. Acad. Sci. 991 (2003) 120-131
7. Benson A.M., Hunkeler M.J., and Talalay P. Increase of NAD(P)H:quinone reductase by dietary antioxidants: possible role in protection against carcinogenesis and toxicity. Proc. Natl. Acad. Sci. U. S. A. 77 (1980) 5216-5220
8. Berman S.B., and Hastings T.G. Dopamine oxidation alters mitochondrial respiration and induces permeability transition in brain mitochondria: implications for Parkinson's disease. J. Neurochem. 73 (1999) 1127-1137
9. Cao Z., Hardej D., Trombetta L.D., and Li Y. The role of chemically induced glutathione and glutathione S-transferase in protecting against 4-hydroxy-2-nonenal-mediated cytotoxicity in vascular smooth muscle cells. Cardiovasc. Toxicol. 3 (2003) 165-177
10. Cao Z., Hardej D., Trombetta L.D., Trush M.A., and Li Y. Induction of cellular glutathione and glutathione S-transferase by 3H-1,2-dithiole-3-thione in rat aortic smooth muscle A10 cells: protection against acrolein-induced toxicity. Atherosclerosis 166 (2003) 291-301
11. Cao Z., Zhu H., Zhang L., Zhao X., Zweier J.L., and Li Y. Antioxidants and phase 2 enzymes in cardiomyocytes: chemical inducibility and chemoprotection against oxidant and simulated ischemia-reperfusion injury. Exp. Biol. Med. (Maywood) 231 (2006) 1353-1364
12. Christen Y. Oxidative stress and Alzheimer disease. Am. J. Clin. Nutr. 71 (2000) 621S-629S
13. Ebadi M., Srinivasan S.K., and Baxi M.D. Oxidative stress and antioxidant therapy in Parkinson's disease. Prog. Neurobiol. 48 (1996) 1-19
14. Fernandez-Checa J.C., Yi J.R., Garcia Ruiz C., Ookhtens M., and Kaplowitz N. Plasma membrane and mitochondrial transport of hepatic reduced glutathione. Semin. Liver Dis. 16 (1996) 147-158
15. Flohe L., and Gunzler W.A. Assays of glutathione peroxidase. Methods Enzymol. 105 (1984) 114-121
16. Fong C.S., Wu R.M., Shieh J.C., Chao Y.T., Fu Y.P., Kuao C.L., and Cheng C.W. Pesticide exposure on southwestern Taiwanese with MnSOD and NQO1 polymorphisms is associated with increased risk of Parkinson's disease. Clin. Chim. Acta 378 (2007) 136-141
17. Grant C.M., Perrone G., and Dawes I.W. Glutathione and catalase provide overlapping defenses for protection against hydrogen peroxide in the yeast Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 253 (1998) 893-898
18. Habig W.H., Pabst M.J., and Jakoby W.B. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249 (1974) 7130-7139
19. Hissin P.J., and Hilf R. A fluorometric method for determination of oxidized and reduced glutathione in tissues. Anal. Biochem. 74 (1976) 214-226
20. Jenner P. Oxidative stress as a cause of Parkinson's disease. Acta Neurol. Scand., Suppl. 136 (1991) 6-15
21. Jenner P., Dexter D.T., Sian J., Schapira A.H., and Marsden C.D. Oxidative stress as a cause of nigral cell death in Parkinson's disease and incidental Lewy body disease. The Royal Kings and Queens Parkinson's Disease Research Group. Ann. Neurol. 32 (1992) S82-S87 Suppl
22. Jia, Z., Hallur, S., Zhu, H., Li, Y., Misra, H.P., in press. Potent upregulation of glutathione and NAD(P)H:quinone oxidoreductase 1 by alpha-lipoic acid in human neuroblastoma SH-SY5Y cells: protection against neurotoxicant-elicited cytotoxicity. Neurochem. Res. doi:10.1007/s11064-007-9496-5.
23. Kehrer J.P. Free radicals as mediators of tissue injury and disease. Crit. Rev. Toxicol. 23 (1993) 21-48
24. Kobayashi M., and Yamamoto M. Nrf2-Keap1 regulation of cellular defense mechanisms against electrophiles and reactive oxygen species. Adv. Enzyme Regul. 46 (2006) 113-140
25. Korytowski W., Sarna T., and Zar ba M. Antioxidant action of neuromelanin: the mechanism of inhibitory effect on lipid peroxidation. Arch. Biochem. Biophys. 319 (1995) 142-148
26. Kwak M.K., Egner P.A., Dolan P.M., Ramos-Gomez M., Groopman J.D., Itoh K., Yamamoto M., and Kensler T.W. Role of phase 2 enzyme induction in chemoprotection by dithiolethiones. Mutat. Res. 480-481 (2001) 305-315
27. Li Y., Zhu H., and Trush M.A. Detection of mitochondria-derived reactive oxygen species production by the chemilumigenic probes lucigenin and luminol. Biochim. Biophys. Acta 1428 (1999) 1-12
28. Merad-Boudia M., Nicole A., Santiard-Baron D., Saille C., and Ceballos-Picot I. Mitochondrial impairment as an early event in the process of apoptosis induced by glutathione depletion in neuronal cells: relevance to Parkinson's disease. Biochem. Pharmacol. 56 (1998) 645-655
29. Munch G., Gerlach M., Sian J., Wong A., and Riederer P. Advanced glycation end products in neurodegeneration: more than early markers of oxidative stress?. Ann. Neurol. 44 (1998) S85-S88
30. Peng X., and Li Y. Induction of cellular glutathione-linked enzymes and catalase by the unique chemoprotective agent, 3H-1,2-dithiole-3-thione in rat cardiomyocytes affords protection against oxidative cell injury. Pharmacol. Res. 45 (2002) 491-497
31. Perry T.L., Godin D.V., and Hansen S. Parkinson's disease: a disorder due to nigral glutathione deficiency?. Neurosci. Lett. 33 (1982) 305-310
32. Perry T.L., and Yong V.W. Idiopathic Parkinson's disease, progressive supranuclear palsy and glutathione metabolism in the substantia nigra of patients. Neurosci. Lett. 67 (1986) 269-274
33. Ratnam D.V., Ankola D.D., Bhardwaj V., Sahana D.K., and Kumar M.N. Role of antioxidants in prophylaxis and therapy: a pharmaceutical perspective. J. Control. Release 113 (2006) 189-207
34. Ross D. Quinone reductases multitasking in the metabolic world. Drug Metab. Rev. 36 (2004) 639-654
35. Ross D., Kepa J.K., Winski S.L., Beall H.D., Anwar A., and Siegel D. NAD(P)H:quinone oxidoreductase 1 (NQO1): chemoprotection, bioactivation, gene regulation and genetic polymorphisms. Chem. Biol. Interact. 129 (2000) 77-97
36. Sechi G., Deledda M.G., Bua G., Satta W.M., Deiana G.A., Pes G.M., and Rosati G. Reduced intravenous glutathione in the treatment of early Parkinson's disease. Prog. Neuropsychopharmacol. Biol. Psychiatry 20 (1996) 1159-1170
37. Selley M.L. (E)-4-hydroxy-2-nonenal may be involved in the pathogenesis of Parkinson's disease. Free Radic. Biol. Med. 25 (1998) 169-174
38. Shimizu E., Hashimoto K., Komatsu N., and Iyo M. Roles of endogenous glutathione levels on 6-hydroxydopamine-induced apoptotic neuronal cell death in human neuroblastoma SK-N-SH cells. Neuropharmacology 43 (2002) 434-443
39. Siegel D., Bolton E.M., Burr J.A., Liebler D.C., and Ross D. The reduction of a-tocopherolquinone by human NAD(P)H: quinone oxidoreductase: the role of a-tocopherolhydroquinone as a cellular antioxidant. Mol. Pharmacol. 52 (1997) 300-305
40. Siegel D., Gustafson D.L., Dehn D.L., Han J.Y., Boonchoong P., Berliner L.J., and Ross D. NAD(P)H:quinone oxidoreductase 1: role as a superoxide scavenger. Mol. Pharmacol. 65 (2004) 1238-1247
41. Smythies J. The neurotoxicity of glutamate, dopamine, iron and reactive oxygen species: functional interrelationships in health and disease: a review-discussion. Neurotox. Res. 1 (1999) 27-39
42. Sofic E., Lange K.W., Jellinger K., and Riederer P. Reduced and oxidized glutathione in the substantia nigra of patients with Parkinson's disease. Neurosci. Lett. 142 (1992) 128-130
43. Spencer J.P., Jenner P., Daniel S.E., Lees A.J., Marsden D.C., and Halliwell B. Conjugates of catecholamines with cysteine and GSH in Parkinson's disease: possible mechanisms of formation involving reactive oxygen species. J. Neurochem. 71 (1998) 2112-2122
44. Spencer J.P., Jenner P., and Halliwell B. Superoxide-dependent depletion of reduced glutathione by L-DOPA and dopamine. Relevance to Parkinson's disease. Neuroreport 6 (1995) 1480-1484
45. Spina M.B., and Cohen G. Dopamine turnover and glutathione oxidation: implications for Parkinson disease. Proc. Natl. Acad. Sci. U. S. A. 86 (1989) 1398-1400
46. Storey K.B. Oxidative stress: animal adaptations in nature. Braz. J. Med. Biol. Res. 29 (1996) 1715-1733
47. Volkel W., Sicilia T., Pahler A., Gsell W., Tatschner T., Jellinger K., Leblhuber F., Riederer P., Lutz W.K., and Gotz M.E. Increased brain levels of 4-hydroxy-2-nonenal glutathione conjugates in severe Alzheimer's disease. Neurochem. Int. 48 (2006) 679-686
48. Wheeler C.R., Salzman J.A., Elsayed N.M., Omaye S.T., and Korte Jr. D.W. Automated assays for superoxide dismutase, catalase, glutathione peroxidase, and glutathione reductase activity. Anal. Biochem. 184 (1990) 193-199
49. Yoritaka A., Hattori N., Uchida K., Tanaka M., Stadtman E.R., and Mizuno Y. Immunohistochemical detection of 4-hydroxynonenal protein adducts in Parkinson disease. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 2696-2701
50. Young A.J., Johnson S., Steffens D.C., and Doraiswamy P.M. Coenzyme Q10: a review of its promise as a neuroprotectant. CNS Spectr. 12 (2007) 62-68
51. Zafar K.S., Inayat-Hussain S.H., Siegel D., Bao A., Shieh B., and Ross D. Overexpression of NQO1 protects human SK-N-MC neuroblastoma cells against dopamine-induced cell death. Toxicol. Lett. 166 (2006) 261-267
52. Zhu H., Itoh K., Yamamoto M., Zweier J.L., and Li Y. Role of Nrf2 signaling in regulation of antioxidants and phase 2 enzymes in cardiac fibroblasts: protection against reactive oxygen and nitrogen species-induced cell injury. FEBS Lett. 579 (2005) 3029-3036
53. Zhu H., Zhang L., Itoh K., Yamamoto M., Ross D., Trush M.A., Zweier J.L., and Li Y. Nrf2 controls bone marrow stromal cell susceptibility to oxidative and electrophilic stress. Free Radic. Biol. Med. 41 (2006) 132-143
54. Zhu H., Zhang L., Trush M.A., and Li Y. Upregulation of endogenous glutathione system by 3H-1,2-dithiole-3-thione in pancreatic RINm5F beta-cells as a novel strategy for protecting against oxidative beta-cell injury. Free Radic. Res. 41 (2007) 242-250