Further insight into the impact of sodium selenite on selenoenzymes: High-dose selenite enhances hepatic thioredoxin reductase 1 activity as a consequence of liver injury

Toxicology Letters

Volumn 176, Issue 3, 2008, Pages 223-229

  Zhang, Jinsong ^a   Wang, Huali ^a,b   Peng, Dungeng ^a   Taylor, Ethan W ^c  

^a UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

^b Shandong Drug and Food Vocational College   (China)

^c UNIVERSITY OF NORTH CAROLINA AT GREENSBORO   (United States)

Author keywords

Glutathione S transferase; Liver injury; Sodium selenite; Thioredoxin reductase

Indexed keywords

ALANINE AMINOTRANSFERASE; ASPARTATE AMINOTRANSFERASE; CARBON TETRACHLORIDE; GLUTATHIONE TRANSFERASE; SELENIUM; SODIUM SELENITE; THIOACETAMIDE; THIOREDOXIN REDUCTASE;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; LIVER INJURY; LIVER TOXICITY; MALE; MOUSE; NONHUMAN; NUTRITIONAL STATUS; PRIORITY JOURNAL; PROTEIN EXPRESSION;

ANIMALS; DOSE-RESPONSE RELATIONSHIP, DRUG; GLUTATHIONE TRANSFERASE; LIVER DISEASES; MALE; MICE; MICE, INBRED C57BL; RATS; RATS, SPRAGUE-DAWLEY; SODIUM SELENITE; THIOREDOXIN REDUCTASE 1;

EID: 38749141350     PISSN: 03784274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxlet.2007.12.002     Document Type: Article

References (36)

1. Arnér E.S.J., and Holmgren A. Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 267 (2000) 6102-6109
2. Banning A., Deubel S., Kluth D., Zhou Z.W., and Brigelius-Flohe R. The GI-GPx gene is a target for Nrf2. Mol. Cell. Biol. 25 (2005) 4914-4923
3. Barbosa N.B., Rocha J.B., Zeni G., Emanuelli T., Beque M.C., and Braga A.L. Effect of organic forms of selenium on delta-aminolevulinate dehydratase from liver, kidney, and brain of adult rats. Toxicol. Appl. Pharmacol. 149 (1998) 243-253
4. Berggren M.M., Mangin J.F., Gasdaka J.R., and Powis G. Effect of selenium on rat thioredoxin reductase activity: increase by supranutritional selenium and decrease by selenium deficiency. Biochem. Pharmacol. 57 (1999) 187-193
5. Berry M. Insights into the hierarchy of selenium incorporation. Nat. Genet. 37 (2005) 1162-11623
6. Chen Z.H., Saito Y., Yoshida Y., Sekine A., Noguchi N., and Niki E. 4-Hydroxynonenal induces adaptive response and enhances PC12 cell tolerance primarily through induction of thioredoxin reductase 1 via activation of Nrf2. J. Biol. Chem. 280 (2005) 41921-41927
7. Conterato G.M., Augusti P.R., Somacal S., Einsfeld L., Sobieski R., Torres J.R., and Emanuelli T. Effect of lead acetate on cytosolic thioredoxin reductase activity and oxidative stress parameters in rat kidneys. Basic Clin. Pharmacol. Toxicol. 101 (2007) 96-100
8. Diskin C.J., Tomasso C.L., Alper J.C., Glaser M.L., and Fliegel S.E. Long-term selenium exposure. Arch. Intern. Med. 139 (1979) 824-826
9. El-Sayed W.M., Aboul-Fadl T., Lamb J.G., Roberts J.C., and Franklin M.R. Effect of selenium-containing compounds on hepatic chemoprotective enzymes in mice. Toxicology 220 (2006) 179-188
10. Ganther H., and Ip C. Thioredoxin reductase activity in rat liver is not affected by supranutritional levels of monomethylated selenium in vivo and is inhibited only by high levels of selenium in vitro. J. Nutr. 131 (2001) 301-304
11. Gronbaek H., Frystyk J., Orskov H., and Flyvbjerg A. Effect of sodium selenite on growth, insulin-like growth factor-binding proteins and insulin-like growth factor-I in rats. J. Endocrinol. 145 (1995) 105-112
12. 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
13. Hadley K.B., and Sunde R.A. Selenium regulation of thioredoxin reductase activity and mRNA levels in rat liver. J. Nutr. Biochem. 12 (2001) 693-702
14. Hayes J.D., Flanagan J.U., and Jowsey I.R. Glutathione transferases. Annu. Rev. Pharmacol. Toxicol. 45 (2005) 51-88
15. Hintze K.J., Wald K.A., Zeng H., Jeffery E.H., and Finley J.W. Thioredoxin reductase in human hepatoma cells is transcriptionally regulated by sulforaphane and other electrophiles via an antioxidant response element. J. Nutr. 133 (2003) 2721-2727
16. Holmgren A., and Bjornstedt M. Thioredoxin and thioredoxin reductase. Methods Enzymol. 252 (1995) 199-208
17. Ip C., and Lisk D.J. Modulation of phase I and phase II xenobiotic-metabolizing enzymes by selenium-enriched garlic in rats. Nutr. Cancer 28 (1997) 184-188
18. Kumar S., Bjornstedt M., and Holmgren A. Selenite is a substrate for calf thymus thioredoxin reductase and thioredoxin and elicits a large nonstoichiometric oxidation of NADPH in the presence of oxygen. Eur. J. Biochem. 207 (1992) 435-439
19. Madeja Z., Sroka J., Nystrom C., Bjorkhem-Bergman L., Nordman T., Damdimopoulos A., Nalvarte I., Eriksson L.C., Spyrou G., Olsson J.M., and Bjornstedt M. The role of thioredoxin reductase activity in selenium-induced cytotoxicity. Biochem. Pharmacol. 69 (2005) 1765-1772
20. Nordberg J., and Arnér E.S. Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic. Biol. Med. 31 (2001) 1287-1312
21. Ramos-Gomez M., Kwak M.K., Dolan P.M., Itoh K., Yamamoto M., Talalay P., and Kensler T.W. Sensitivity to carcinogenesis is increased and chemoprotective efficacy of enzyme inducers is lost in Nrf2 transcription factor-deficient mice. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 3410-3415
22. Reeves P.G., Leary P.D., Gregoire B.R., Finley J.W., Lindlauf J.E., and Johnson L.K. Selenium bioavailability from buckwheat bran in rats fed a modified AIN-93G torula yeast-based diet. J. Nutr. 135 (2005) 2627-2633
23. Rotruck J.T., Pope A.L., Ganther H.E., Swanson A.B., Hafeman D.G., and Hoekstra W.G. Selenium: biochemical role as a component of glutathione peroxidase. Science 179 (1973) 588-590
24. Sakurai A., Nishimoto M., Himeno S., Imura N., Tsujimoto M., Kunimoto M., and Hara S. Transcriptional regulation of thioredoxin reductase 1 expression by cadmium in vascular endothelial cells: role of NF-E2-related factor-2. J. Cell. Physiol. 203 (2005) 529-537
25. Sohn O.S., Fiala E.S., Upadhyaya P., Chae Y.H., and El-Bayoumy K. Comparative effects of phenylenebis(methylene)selenocyanate isomers on xenobiotic metabolizing enzymes in organs of female CD rats. Carcinogenesis 20 (1999) 615-621
26. Spallholz J.E. On the nature of selenium toxicity and carcinostatic activity. Free Radic. Biol. Med. 17 (1994) 45-64
27. Spallholz J.E., and Hoffman D.J. Selenium toxicity: cause and effects in aquatic birds. Aquat. Toxicol. 57 (2002) 27-37
28. Sun Y., Larry W., Oberley W., and Ying L. A simple method for clinical assay of superoxide dismutase. Clin. Chem. 34 (1988) 497-500
29. Talalay P. Chemoprotection against cancer by induction of phase 2 enzymes. Biofactors 12 (2000) 5-11
30. Thorlacius-Ussing O. Selenium-induced growth retardation: histochemical and endocrinological studies on the anterior pituitaries of selenium treated rats. Dan. Med. Bull. 37 (1990) 347-358
31. Wang H., Zhang J., and Yu H. Elemental selenium at nanosize possesses lower toxicity without compromising the fundamental effect on selenoenzymes: comparison with selenomethionine in mice. Free Radic. Biol. Med. 42 (2007) 1524-1533
32. Xiao H., and Parkin K.L. Induction of phase II enzyme activity by various selenium compounds. Nutr. Cancer 55 (2006) 210-223
33. Zhang J.S., Gao X.Y., Zhang L.D., and Bao Y.P. Biological effects of a nanored elemental selenium. Biofactors 15 (2001) 27-38
34. Zhang J., Svehlikova V., Bao Y., Howie A.F., Beckett G.J., and Williamson G. Synergy between sulforaphane and selenium in the induction of thioredoxin reductase 1 requires both transcriptional and translational modulation. Carcinogenesis 24 (2003) 497-503
35. Zhang J., Wang H., Yan X., and Zhang L. Comparison of short-term toxicity between Nano-Se and selenite in mice. Life Sci. 76 (2005) 1099-1109
36. Zhang J., Wang X., and Xu T. Elemental selenium at nanosize (Nano-Se) as a potential chemopreventive agent with reduced risk of selenium toxicity: comparison with Se-methylselenocysteine in mice. Toxicol. Sci. 101 (2007) 22-31