Post-transcriptional elevation of mouse brain Mn-SOD protein by mercuric chloride

Brain Research

Volumn 769, Issue 1, 1997, Pages 178-182

  Kumagai, Yoshito ^a   Mizukado, Saho ^a   Nagafune, Jun ^a   Shinyashiki, Masaru ^b   Homma Takeda, Shino ^a   Shimojo, Nobuhiro ^a  

^a UNIVERSITY OF TSUKUBA   (Japan)

^b Univ T   (Japan)

Author keywords

Dexamethasone; Mercury; Mn SOD; Mouse brain; Oxidative stress; Post transcriptional modification

Indexed keywords

ANTIOXIDANT; DEXAMETHASONE; MANGANESE SUPEROXIDE DISMUTASE; MERCURIC CHLORIDE;

ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME INDUCTION; MALE; MOUSE; NEUROTOXICITY; NONHUMAN; NORTHERN BLOTTING; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN PROCESSING;

ANIMALS; BLOTTING, NORTHERN; BRAIN; DEXAMETHASONE; GLUCOCORTICOIDS; MALE; MERCURIC CHLORIDE; MERCURY; MICE; MICE, INBRED ICR; OSMOLAR CONCENTRATION; PROTEIN PROCESSING, POST-TRANSLATIONAL; SUPEROXIDE DISMUTASE;

EID: 0030669402     PISSN: 00068993     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-8993(97)00846-9     Document Type: Article

References (46)

1. Albers R., Van Der Pijl A., Bol M., Seinen W., Pieters R. Stress proteins (HSP) and chemical-induced autoimmunity. Toxicol. Appl. Pharmacol. 140:1996;70-76.
2. Borrello S., De Leo M.E., Landriscina M., Palazzotti B., Galeotti T. Diethyldithiocarbamate treatment up regulates manganese superoxide dismutase gene expression in rat liver. Biochem. Biophys. Res. Commun. 220:1996;546-552.
3. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254.
4. Cetkovic-Cvrlje M., Sandler S., Eizirik D.L. Nicotinamide and dexamethasone inhibit interleukin 1-induced nitric oxide production by RINm5F cells without decreasing messenger ribonucleic acid expression for nitric oxide synthetase. Endocrinology. 133:1993;1739-1743.
5. Chomczynski P., Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:1987;156-159.
6. Chung A.S., Maines M.D., Reynolds W.A. Inhibition of the enzyme of glutathione metabolism by mercuric chloride in the rat kidney: reversal by selenium. Biochem. Pharmacol. 31:1982;3093-3110.
7. Clarkson T.W. The pharmacology of mercury compound. Annu. Rev. Pharmacol. 12:1972;375-406.
8. Dougall W.C., Nick H.S. Manganese superoxide dismutase: a hepatic acute phase protein regulated by interleukin-6 and glucocorticoids. Endocrinology. 129:1991;2376-2384.
9. Fowler B.A., Woods J.S. The transplacental toxicity of methyl mercury to fetal rat liver mitochondria: morphometric and biochemical studies. Lab. Invest. 36:1977;122-130.
10. Fridovich I. Superoxide radical: an endogenous toxicant. Annu. Rev. Pharmacol. Toxicol. 23:1983;239-257.
11. Girardi G., Elías M.M. Mercuric chloride effects on rat renal redox enzymes activities: SOD protection. Free Radic. Biol. Med. 18:1995;61-66.
12. Goering P.L., Fisher B.R., Chaudhary P., Dick C.A. Relationship between stress protein induction in rat kidney by mercuric chloride and nephrotoxicity. Toxicol. Appl. Pharmacol. 113:1992;184-191.
13. Gstraunthaler G., Pfaller W., Kotanko P. Glutathione depletion and in vitro lipid peroxidation in mercury or maleate induced acute renal failure. Biochem. Pharmacol. 32:1983;2969-2972.
14. Heinrich P.C., Castell J.V., Andus T. Interleukin-6 and the acute phase response. Biochem. J. 265:1990;621-636.
15. Iizuka S., Taniguchi N., Makita A. Enzyme-linked immunosorbent assay for human manganese superoxide dismutase and its content in lung cancer. J. Natl. Cancer Inst. 72:1984;1043-1049.
16. Jacobs M.B., Yamaguchi S., Goldwater L.J., Gilbert H. Determination of mercury in blood. Am. Ind. Hyg. Assoc. J. 21:1960;475-480.
17. Koch O.R., Deleo M.E., Borrello S., Palombini G., Galeotti T. Ethanol treatment up-regulates the expression of mitochondrial manganese superoxide dismutase in rat liver. Biochem. Biophys. Res. Commun. 201:1994;1356-1365.
18. Kramer K.K., Liu J., Choudhuri S., Klaassen C. Induction of metallothionein mRNA and protein in murine astrocyte cultures. Toxicol. Appl. Pharmacol. 136:1996;94-100.
19. Kumagai Y., Lin L.Y., Hiratsuka A., Narimatsu S., Suzuki T., Yamada H., Oguri K., Yoshimura H., Cho A.K. Participation of cytochrome P450-2B and -2D isozymes in the demethylenation of methylenedioxymethamphetamine enantiomers by rats. Mol. Pharmacol. 45:1994;359-365.
20. Y. Kumagai, S. Homma-Takeda, M. Shinyashiki, N. Shimojo, Alterations in superoxide dismutase isozymes by methylmercury, Appl. Organomet. Chem. (1997) in press.
21. Kunz D., Walker G., Pfeilschifter J. Dexamethasone differentially affects interleukin 1β- and cyclic AMP-induced nitric oxide synthase mRNA expression in renal mesangial cells. Biochem. J. 304:1994;337-340.
22. Kunz D., Walker G., Eberhardt W., Pfeilschifter J. Molecular mechanisms of dexamethasone inhibition of nitric oxide synthase expression in interleukin 1β-stimulated mesangial cells: evidence for the involvement of transcriptional and posttranscriptional regulation. Proc. Natl. Acad. Sci. USA. 93:1996;255-259.
23. LeBel C.P., Ali S.F., Mckee M., Bondy S.C. The potential of 2′,7′-dichlorofluorescin diacetate as index of neurotoxic damage. Toxicol. Appl. Pharmacol. 104:1990;17-24.
24. LeBel C.P., Ali S.F., Bondy S.C. Deferoxamine inhibits methyl mercury-induced increases in reactive oxygen species formation in rat brain. Toxicol. Appl. Pharmacol. 112:1992;161-165.
25. 2 production and lipid peroxidation in vitro in rat kidney mitochondria. Biochem Pharmacol. 42:1991;s181-s187.
26. 2 formation and oxidative stress in vivo and in vitro in rat kidney mitochondria. Biochem. Pharmacol. 45:1993;2017-2024.
27. Masuda A., Longo D.L., Kobayashi Y., Appella E., Oppenheim J.J., Matsushima K. Induction of mitochondrial manganese superoxide dismutase by interleukin 1. FASEB J. 2:1988;3087-3091.
28. Matsuda Y., Suzuki K., Ookawara T., Nakata T., Seo H.G., Kawata S., Tarui S., Deutsch H.F., Taniguchi T. A three-step purification of manganese superoxide dismutase from human liver on both large and small scales. Protein Expression Purif. 2:1991;170-174.
29. Miller D.M., Woods J.S. Urinary porphyrins as biological indicators of oxidative in the kidney. Interaction of mercury and cephaloridine. Biochem. Pharmacol. 46:1993;2235-2241.
30. Minami M., Koshi K., Homma K., Suzuki Y. Changes of activities of superoxide dismutase after exposure to the fume of heavy metals and the significance of zinc in the tissue. Arch. Toxicol. 49:1982;225-245.
31. Ono M., Kohda H., Kawaguchi T., Ohhira M., Seiya C., Namiki M., Takeyasu A., Taniguchi N. Induction of Mn-superoxide dismutase by tumor necrosis factor, interleukin-6 in human hepatoma cells. Biochem. Biophys. Res. Commun. 182:1992;1100-1107.
32. Piotrowski J.K., Trojanowska B., Wisniewska-Knypl J.M., Bolanowska W. Mercury binding in the kidney and liver of rats repeatedly expressed to mercuric chloride: induction of metallothionein by mercury and cadmium. Toxicol. Appl. Pharmacol. 27:1974;11-19.
33. Reddy C.C., Scholz R.W., Massaro E.J. Cadmium, mercury, and lead inhibition of calf liver glutathione S-transferase exhibiting selenium-independent glutathione peroxidase activity. Toxicol. Appl. Pharmacol. 61:1981;460-468.
34. Sarafian T., Verity A. Oxidative mechanisms underlying methyl mercury neurotoxicity. Int. J. Dev. Neurosci. 9:1991;147-153.
35. Shinyashiki M., Kumagai Y., Homma-Takeda S., Nagafune J., Suzuki J., Matsuzaki I., Satoh S., Sagai M., Shimojo N. Selective inhibition of the mouse brain Mn-SOD by methylmercury. Environ. Toxicol. Pharmacol. 2:1996;359-366.
36. Southard J.H., Nitisewojo P. Loss of oxidative phosphorylation in mitochondria isolated from kidneys of mercury poisoned rats. Biochem. Biophys. Res. Commun. 52:1973;921-927.
37. Stohs S.J., Bagchi D. Oxidative mechanisms in the toxicity of metal ions. Free Radic. Biol. Med. 18:1995;321-336.
38. Thomas P.S. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc. Natl. Acad. Sci. USA. 77:1980;5201-5205.
39. Valentine J.F., Nick H.S. Glucocorticoids repress basal and stimulated manganese superoxide dismutase levels in rat intestinal epithelial cells. Gastroenterology. 107:1994;1662-1670.
40. Viserl G.A., Dougall W.C., Wilson J.M., Barr I.A., Nick H.S. Regulation of manganese superoxide dismutase by lipopolysaccharide, interleukin-1 and tumor necrosis factor. J. Biol. Chem. 265:1990;2856-2863.
41. Weinberg J.M., Harding P.G., Humes H.D. Mitochondrial bioenergetics during the initiation of mercuric chloride-induced renal injury: II. Functional alterations of renal cortical mitochondria isolation of mercuric chloride treatment. J. Biol. Chem. 257:1982;68-72.
42. Wong G.H.W., Goeddel D.V. Induction of manganese superoxide dismutase by tumor necrosis factor: possible protective mechanism. Science. 242:1988;941-944.
43. Xiang K., Cox N.J., Hallewell R.A., Bell G.I. Multiple Taq I RFLPs at human manganese superoxide dismutase (SOD2) locus on chromosome 6. Nucleic Acids Res. 15:1987;7654.
44. Yiangou M., Kenneth X.G., Papaconstantinou J. Induction of several acute-phase protein gene by heavy metals: a new class of metal-responsive genes. Biochemistry. 30:1991;3798-3806.
45. Yiangou M., Papaconstantinou J. Differential induction of α1-acid glycoprotein and serum amiloid A genes by heavy metals. Biochim. Biophys. Acta. 1174:1993;123-132.
46. Yonaha M., Itoh E., Ohbayashi Y., Uchiyama M. Induction of lipid peroxidation in rat by mercuric chloride. Res. Commun. Chem. Pathol. Pharmacol. 28:1980;105-112.