Tellurium-induced dose-dependent impairment of antioxidant status: Differential effects in cerebrum, cerebellum, and brainstem of mice

Biological Trace Element Research

Volumn 94, Issue 3, 2003, Pages 247-258

  Kaur, Parvinder ^a   Yousuf, Seema ^a   Ansari, Mubeen Ahmad ^a   Siddiqui, Almas ^a   Ahmad, Abdullah Shafique ^a   Islam, Fakhrul ^a  

^a HAMDARD UNIVERSITY   (India)

Author keywords

Antioxidant enzymes; Brainstem; Cerebellum; Cerebrum; Glutathione; Sodium tellurite; Thiobarbituric acid reactive substance

Indexed keywords

ANTIOXIDANT; CATALASE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; GLUTATHIONE TRANSFERASE; SODIUM TELLURITE; TELLURIUM DERIVATIVE; THIOBARBITURIC ACID DERIVATIVE; UNCLASSIFIED DRUG;

ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; BODY WEIGHT; BRAIN; BRAIN STEM; CEREBELLUM; CONCENTRATION RESPONSE; CONTROLLED STUDY; DOSE RESPONSE; ENZYME ACTIVITY; INTERMETHOD COMPARISON; MALE; MOUSE; NEUROTOXICITY; NONHUMAN; PEROXIDATION; PROTEIN DEPLETION;

ANIMALS; ANTIOXIDANTS; BRAIN STEM; CATALASE; CEREBELLUM; DOSE-RESPONSE RELATIONSHIP, DRUG; GLUTATHIONE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; GLUTATHIONE TRANSFERASE; LIPID PEROXIDATION; MALE; MICE; TELENCEPHALON; TELLURIUM; THIOBARBITURIC ACID REACTIVE SUBSTANCES;

ANIMALIA;

EID: 0141427727     PISSN: 01634984     EISSN: None     Source Type: Journal    
DOI: 10.1385/BTER:94:3:247     Document Type: Article

References (47)

1. S. Glozman, P. Green, and E. Yavin, Intra-amniotic ethyl docosahexaenoate administration protects fetal rat brain from ischemic stress, J. Neurochem. 70, 2484-2491 (1998).
2. Y. Ikeda and D. M. Long, Comparative effects of direct and indirect hydroxyl radical scavengers on traumatic brain edema, Acta Neurochir. 51(Suppl.) 74-76 (1990).
3. L. Sokoloff, Neurophysiology, in Handbook of Physiology, J. Field, ed., American Physiological Society, Washington, DC, Vol. 3, pp. 1843-1864 (1960).
4. V. Darley-Usmar and B. Halliwell, Blood radicals: reactive nitrogen species, reactive oxygen species, transition metal ions, and the vascular system. Pharm. Res. 13(5), 649-662 (1996).
5. J. Liu and A. Mori, Monoamine metabolism provides an antioxidant defense in the brain against oxidant- and free radical-induced damage, Arch. Biochem. Biophys. 302, 118-127 (1993).
6. S. M. Black and C. R. Wolf, The role of glutathione-dependent enzymes in drug resistance, Pharmacol. Therap. 51, 139-154 (1991).
7. A. Miester and M. E. Anderson, Glutathione, Annu. Rev. Biochem. 52, 711-760 (1983).
8. M. J. Pennincks and M. T. Elskens, Metabolism and function of glutathione in microorganisms, Adv. Microb. Physiol. 34, 239-301 (1993).
9. M. M. Romero and A. T. Canada, The evaluation of Escherichia coli as a model for oxidative stress in mammalian hepatocytes: Role of glutathione, Toxicol. Appl. Pharmacol. 111, 485-495 (1991).
10. M. Rougemont, K. Q. Do, and V. Castagne, New model of glutathione deficit during development: effect on lipid peroxidation in the rat brain, J. Neurosci. Res. 70(6), 774-783 (2002).
11. P. J. O'Brien, in Cellular Antioxidant Defense Mechanism, C. K. Chow, ed., CRC, Boca Raton, FL, Vol. 1, pp. 73-87 (1988).
12. L. J. Marnett, Peroxyl free radicals: potential mediators of tumor initiation and promotion, Carcinogenesis 8, 1365-1373 (1987).
13. F. Ursini, Selenium dependent proxidases; Thoughts on physiological functions from enzymology and molecular structure in Oxidative Processes and Antioxidants, R. Paoletti, ed., Raven, New York, pp. 25-31 (1994).
14. B. Halliwell, Reactive oxygen species and the central nervous system. J. Neurochem. 59, 1609-1623 (1992).
15. K. N. Islam, Y. Kayanoki, H. Kaneto, et al., TGF-a1 triggers oxidative modifications and enhances apoptosis in HIT cells through accumulation of reactive oxygen species by suppression of catalase and glutathione peroxidase, Free Radical Biol. Med. 22, 1007-1017 (1997).
16. P. A. Sandstrom and T. M. Buttke, Autocrine production of extracellular catalase prevents apoptosis of the human CEM T-cell line in serum-free medium, Proc. Natl. Acad. Sci. USA 90, 4708-4712 (1993).
17. M. Yabuki, S. Kariya, R. Ishisaka, et al., Resistance to nitric oxide-mediated apoptosis in the HL-60 variant cells is associated with increased activities of Cu, Zn-superoxide dismutase and catalase, Free Radical Biol. Med. 26, 325-332 (1999).
18. S. Baez, J. Segura-Aguilar, M. Widersten, A. S. Johansson, and B. Mannervik, Glutathione transferases catalyse the detoxication of oxidized metabolites (o-quinones) of catecholamines and may serve as an antioxidant system preventing degenerative cellular processes. Biochem. J. 324, 5-8 (1997).
19. A. Taylor, Biochemistry of tellurium, Biol. Trace Element Res. 55(3), 231-239 (1996).
20. P. Kaur, S. Yousuf, M. A. Ansari, A. S. Ahmad, and F. Islam, Dose and duration dependent alterations by tellurium on lipid levels: differential effects in cerebrum, cerebellum and brain stem of mice, Biol. Trace Element Res., 2002, in press.
21. B. Halliwell, Oxidants and the central nervous system: some fundamental questions. Is oxidant damage relevant to Parkinson's disease, Alzheimer's disease, traumatic injury or stroke? Acta Neurol. Scand. 126, 23-33 (1989).
22. A. O. Summers and G. A. Jacoy, Plasmid-determined resistance to tellurium compounds, J. Bacteriol. 129, 276-281 (1977).
23. D. E. Taylor, Bacterial tellurite resistance: widespread determinants for resistance to a rare oxyanion, Trends Microbiol. 7, 111-115 (1999).
24. R. Wheeler, A. S. Jhiane, M. N. Elsayeed, T. S. Omaye, and J. W. D. Korte, Automated assays for superoxide dismutase, catalase, glutathione peroxidase and glutathione reductase activity, Anal. Biochem. 184, 193-199 (1990).
25. W. H. Habig, M. Pabst, and W. B. Jakoby, Glutathione-S-transferase: the first enzymatic step in mercapturic acid formation, J. Biol. Chem. 249, 7130-7139 (1974).
26. A. Claiborne, Catalase activity, in CRC Handbook of Methods for Oxygen Radical Research, R. A. Greenwald, ed., CRC, Boca Raton, FL, pp. 283-284 (1985).
27. I. Carlberg and B. Mannervick, Glutathione reductase level in rat brain, J. Biol. Chem. 250, 5475-5480 (1975).
28. D. J. Jollow, J. R. Mitchell, N. Zampaghone, and J. R. Gillete, Bromobenzene induced liver necrosis: protective role of glutathione and evidence of 3,4-bromobenzene oxide as the hepatotoxic intermediate, Pharmacology 11, 161-169 (1974).
29. H. C. Utley, F. Bernhein, and P. Hochsleim, Effects of sulfhydryl reagent on peroxidation in microsomes, Arch. Biochem. Biophys. 260, 521-531 (1967).
30. F. Islam, S. Zia, I. Sayeed, K. S. Zafar, and A. S. Ahmad, Selenium induced alteration on lipids, lipid peroxidation, and thiol group in circadian rhythm centers of rat, Biol. Trace Element Res. 90, 1-12 (2002).
31. O. H. Lowry, N. J. Rosenbrough, A. L. Farr, and R. J. Randall, Protein measurement with folin phenol reagent, J. Biol. Chem. 193, 265-275 (1951).
32. N. A. Simonian, and J. T. Coyle, Oxidative stress in neurodegenerative diseases, Annu. Rev. Pharmacol. Toxicol. 36, 83-106 (1996).
33. T. Finkel and N. J. Holbrook, Oxidants, oxidative stress and the biology of ageing, Nature 408, 239-247 (2000).
34. T. Bersin and W. Longemann, Mercaptides of selenium and tellurium, Liebigs Ann. Chem. 505, 1-16 (1933).
35. A.H.W. Albeck, B. Sredni, and M. Albeck, Tellurium compounds: selective inhibition of cysteine proteases and model reaction with thiols, Inorg. Chem. 37, 1704-1712 (1998).
36. N. Patel, J. Fullone, and M. W. Andrs, Brain uptake and metabolism of S-(1,2 dichloro venyl) glutathione (DCVE) and S-(1,2 dichloro vinyl)-L cysteine (DCVC), Toxicologist 12, 343-348 (1992).
37. S. Zia and F. Islam, Selenium altered the levels of lipids, lipid peroxidation, and sulfhydryl groups in striatum and thalamus of rat, Biol. Trace Element Res. 77, 251-259 (2000).
38. B. Deuticke, P. Lutkemeier, and B. Poser, Tellurite-induced damage of erythrocyte membrane. Manifestations and mechanisms, Biochim. Biophys. Acta 1109, 97-107 (1992).
39. J. D. Young, C. Crowley, and E. M. Tucker, Hemolysis of normal and glutathione-deficient sheep erythrocytes by selenite and tellurite, Biochem. Pharmacol. 30, 2527-2530 (1981).
40. H. Sies, V. S. Sharov, L. O. Klotz, and K. Briviba, Glutathione peroxidase protects against Peroxinitrite-mediated oxidations: a new function for selenoproteins as peroxinitrite reductase, J. Biol. Chem. 272, 27,812-27, 817 (1997).
41. P. Garberg, L. Engman, V. Tolmachev, et al., Binding of tellurium to hepatocellular seleno-proteins during incubation with inorganic tellurite: consequences for the activity of selenium-dependent glutathione peroxidase, Int. J. Biochem. Cell Biol. 31(2), 291-301 (1999).
42. E. Niki, Antioxidant defences in eukariotic cells: an overview, in Free Radicals: From Basic Science to Medicine, G. Poli, E. Albino, and M. U. Dianzani, eds., Birhauser Verlag, Basel, pp. 365-373 (1993).
43. G. Rhie, J. Y. Seo, and J. H. Chung, Modulation of catalase in human skin in vivo by acute and chronic UV radiation, Mol. Cells 11(3), 399-404 (2001).
44. J. Booth, E. Boyland, and P. Sims, An enzyme from rat liver catalyzing conjugation with glutathione, J. Biochem. 79, 516-524 (1961).
45. E. Boyland and L. F. Chasseaud, The role of glutathione and glutathione-S-transferase in mercapturic acid biosynthesis, in Advances in Enzymology, F. F. Nord, ed., Fordham University Press, Bronx, NY, Vol. 32, pp. 172-219 (1969).
46. J. L. Wood, Hydrolysis in Metabolic Conjugation and Metabolic Hydrolysis, W. H. Fishman, ed., Academic, New York, Vol. 2, pp. 261-299 (1970).
47. R. C. Srivastava, R. Srivastava, T. N. Srivastava, and S. P. Jain, Effect of organotellurium compounds on the enzymatic alterations in rats, Toxicol. Lett. 16(3-4), 311-316 (1983).