Post-transcriptional defects of antioxidant selenoenzymes cause oxidative stress under methylmercury exposure

Journal of Biological Chemistry

Volumn 286, Issue 8, 2011, Pages 6641-6649

  Usuki, Fusako ^a   Yamashita, Akio ^b,c   Fujimura, Masatake ^a  

^a NATIONAL INSTITUTE FOR MINAMATA DISEASE   (Japan)

^b YOKOHAMA CITY UNIVERSITY   (Japan)

^c JAPAN SCIENCE AND TECHNOLOGY AGENCY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIOXIDANT ENZYME; CELL LINES; CELLULAR MECHANISMS; CELLULAR REDOX; EBSELEN; ENVIRONMENTAL PROBLEMS; EXON-EXON JUNCTION; GLUTATHIONE PEROXIDASE; HUMAN HEALTH; METHYLMERCURY; MOLECULAR MECHANISM; POST-TRANSCRIPTIONAL; PREMATURE TERMINATION CODON; RECODING; SELENIUM DEFICIENCY; SELENOCYSTEINE; SELENOENZYMES; THIOREDOXIN REDUCTASE; THIOREDOXINS; UP-REGULATION;

CELL CULTURE; CLARIFICATION; MERCURY COMPOUNDS; NUCLEIC ACIDS; PLANTS (BOTANY); PLATINUM COMPOUNDS; SELENIUM; SELENIUM COMPOUNDS;

OXIDATIVE STRESS;

EBSELEN; GLUTATHIONE PEROXIDASE 1; MESSENGER RNA; METHYLMERCURY; SELENOCYSTEINE; THIOREDOXIN REDUCTASE 1; TROLOX C;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ANTIOXIDANT ACTIVITY; ARTICLE; CELL LINE; CELL PROTECTION; CONTROLLED STUDY; CYTOTOXICITY; ENZYME ACTIVITY; EXON; GENETIC TRANSCRIPTION; MERCURIALISM; NONHUMAN; NONSENSE MEDIATED MRNA DECAY; OXIDATION REDUCTION STATE; OXIDATIVE STRESS; PRIORITY JOURNAL; RAT; RNA DEGRADATION; SELENIUM DEFICIENCY; STOP CODON; UPREGULATION;

ANIMALS; ANTIOXIDANTS; AZOLES; CELL LINE; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GLUTATHIONE PEROXIDASE; HUMANS; METHYLMERCURY COMPOUNDS; ORGANOSELENIUM COMPOUNDS; OXIDATIVE STRESS; RATS; RNA STABILITY; RNA, MESSENGER; SELENIUM; SELENOPROTEINS; THIOREDOXIN REDUCTASE 1;

EID: 79953208992     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M110.168872     Document Type: Article

References (40)

1. Hamada, R., and Osame, M. (1996) Toxicology of Metals (Chang, L. W., ed) pp. 337-351, CRC Press, London
2. Bakir, F., Damluji, S. F., Amin-Zaki, L., Murtadha, M., Khalidi, A., al-Rawi, N. Y., Tikriti, S., Dahahir, H. I., Clarkson, T. W., Smith, J. C., and Doherty, R. A. (1973) Science 181, 230-241
3. Davis, L. E., Kornfeld, M., Mooney, H. S., Fiedler, K. J., Haaland, K. Y., Orrison, W. W., Cernichiari, E., and Clarkson, T. W. (1994) Ann. Neurol. 35, 680-688
4. Deleted in proof
5. Park, S. T., Lim, K. T., Chung, Y. T., and Kim, S. U. (1996) Neurotoxicology 17, 37-45
6. Yee, S., and Choi, B. H. (1996) Neurotoxicology 17, 17-26
7. Usuki, F., and Ishiura, S. (1998) NeuroReport 9, 2291-2296
8. Usuki, F., Takahashi, N., Sasagawa, N., and Ishiura, S. (2000) Biochem. Biophys. Res. Commun. 267, 739-743
9. Usuki, F., Fujita, E., and Sasagawa, N. (2008) Neurotoxicology 29, 22-30
10. Shanker, G., and Aschner, M. (2003) Brain Res. Mol. Brain Res. 110, 85-91
11. Yee, S., and Choi, B. H. (1994) Exp. Mol. Pathol. 60, 188-196
12. Usuki, F., Yasutake, A., Umehara, F., Tokunaga, H., Matsumoto, M., Eto, K., Ishiura, S., and Higuchi, I. (2001) Neurosci. Lett. 304, 199-203
13. Usuki, F., Yasutake, A., Umehara, F., and Higuchi, I. (2004) Acta Neuropathol. 108, 1-9
14. Sugiura, Y., Tamai, Y., and Tanaka, H. (1978) Bioinorg. Chem. 9, 167-180
15. Ganther, H. E., Goudie, C., Sunde, M. L., Kopecky, M. J., Wagner, P., Oh, S-H., and Hoekstra, W. G. (1972) Science 175, 1122-1124
16. Nobunaga, T., Satoh, H., and Suzuki, T. (1979) Toxicol. Appl. Pharmacol. 47, 79-88
17. Satoh, H., Yasuda, N., and Shimai, S. (1985) Toxicol. Lett. 25, 199-203
18. Imura, N. (1986) Dev. Toxicol. Environ. Sci. 12, 115-123
19. Nishikido, N., Furuyashiki, K., Naganuma, A., Suzuki, T., and Imura, N. (1987) Toxicol. Appl. Pharmacol. 88, 322-328
20. Watanabe, C., Yin, K., Kasanuma, Y., and Satoh, H. (1999) Neurotoxicol. Teratol. 21, 83-88
21. Hirota, Y., Yamaguchi, S., Shimojoh, N., and Sano, K. (1980) Toxicol. App. Pharmacol. 53, 174-176
22. Usuki, F., Yasutake, A., Matsumoto, M., and Higuchi, I. (2001) J. Health Science 47, 162-167
23. Farina, M., Soares, F. A., Zeni, G., Souza, D. O., and Rocha, J. B. (2004) Toxicol. Lett. 146, 227-235
24. Carvalho, C. M., Chew, E. H., Hashemy, S. I., Lu, J., and Holmgren, A. (2008) J. Biol. Chem. 283, 11913-11923
25. Hatfield, D. L., and Gladyshev, V. N. (2002) Mol. Cell. Biol. 22, 3565-3576
26. Yamashita, A., Kashima, I., and Ohno, S. (2005) Biochim. Biophys. Acta 1754, 305-315
27. Usuki, F., Yamashita, A., Kashima, I., Higuchi, I., Osame, M., and Ohno, S. (2006) Mol. Ther. 14, 351-360
28. Yamashita, A., Izumi, N., Kashima, I., Ohnishi, T., Saari, B., Katsuhata, Y., Muramatsu, R., Morita, T., Iwamatsu, A., Hachiya, T., Kurata, R., Hirano, H., Anderson, P., and Ohno, S. (2009) Genes Dev. 23, 1091-1105
29. Ohnishi, T., Yamashita, A., Kashima, I., Schell, T., Anders, K. R., Grimson, A., Hachiya, T., Hentze, M. W., Anderson, P., and Ohno, S. (2003) Mol. Cell 12, 1187-1200
30. Moriarty, P. M., Reddy, C. C., and Maquat, L. E. (1998) Mol. Cell. Biol. 18, 2932-2939
31. Kashima, I., Yamashita, A., Izumi, N., Kataoka, N., Morishita, R., Hoshino, S., Ohno, M., Dreyfuss, G., and Ohno, S. (2006) Genes Dev. 20, 355-367
32. Nagy, E., and Maquat, L. E. (1998) Trends Biochem. Sci. 23, 198-199
33. Lu, J., Zhong, L., Lönn, M. E., Burk, R. F., Hill, K. E., and Holmgren, A. (2009) FASEB J. 23, 2394-2402
34. Mustacich, D., and Powis, G. (2000) Biochem. J. 346, 1-8
35. Kumar, S., Björnstedt, M., and Holmgren, A. (1992) Eur. J. Biochem. 207, 435-439
36. Björnstedt, M., Hamberg, M., Kumar, S., Xue, J., and Holmgren, A. (1995) J. Biol. Chem. 270, 11761-11764
37. Björnstedt, M., Xue, J., Huang, W., Akesson, B., and Holmgren, A. (1994) J. Biol. Chem. 269, 29382-29384
38. Sies, H. (1993) Free Rad. Biol. Med. 14, 313-323
39. Zhao, R., Masayasu, H., and Holmgren, A. (2002) Proc. Natl. Acad. Sci. U.S.A. 99, 8579-8584
40. Zhao, R., and Holmgren, A. (2002) J. Biol. Chem. 277, 39456-39462