Localization by in situ hybridization of γ-glutamylcysteine synthetase mRNA expression in rat kidney following acute methylmercury treatment

Toxicology and Applied Pharmacology

Volumn 141, Issue 1, 1996, Pages 59-67

  Li, Shunan ^b   Thompson, Sally A ^b   Kavanagh, Terrance J ^b   Woods, James S ^a,b  

^a BATTELLE MEMORIAL INSTITUTE   (United States)

^b UNIVERSITY OF WASHINGTON   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; MESSENGER RNA; METHYLMERCURY;

ADAPTATION; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DOSE RESPONSE; GENE EXPRESSION; IN SITU HYBRIDIZATION; INTRAPERITONEAL DRUG ADMINISTRATION; KIDNEY; KIDNEY CORTEX; MALE; NEPHROTOXICITY; NONHUMAN; RAT;

ANIMALIA; TRIXIS;

EID: 2442736665     PISSN: 0041008X     EISSN: None     Source Type: Journal    
DOI: 10.1006/taap.1996.0260     Document Type: Article

References (33)

1. Abate, C., Patel, L., Rausher, F. J., and Curran, T. (1990). Redox regulation of Fos and Jun DNA-binding activity in vitro. Science 249, 1157-1161.
2. Bergelson, S., Pinkus, R., and Daniel, V. (1994). Intracellular glutathione levels regulate Fos/Jun induction and activation of glutathione S-transferase gene expression. Cancer Res. 54, 36-40.
3. Biber, T. U. L., Mylle, M., Baines, A. D., Gottschalk, C. W., Oliver, J. R., and MacDowell, M. C. (1968). A study in micropuncture and microdissection of acute renal damage in rats. Am. J. Med. 44, 664-705.
4. Clapp, W. L., and Tisher, C. C. (1989). Gross anatomy and development of the kidney. In Renal Pathology with Clinical and Functional Correlations (C. C. Tisher, and B. M. Brenner, Eds.), Chap. 54, Vol. 1, pp. 67-89. Lippincott, Philadelphia.
5. Cotgreave, I. A., Moldeus, P., and Orrenius, S. (1988). Host biochemical defense mechanisms against prooxidants. Annu. Rev. Pharmacol. Toxicol. 28, 189-217.
6. Davis, M. A., Wallig, M. A., Eaton, D. E., Borroz, K. I., and Jeffery, E. H. (1993). Differential effect of cyanohydroxybutene on glutathione synthesis in liver and pancreas of male rats. Toxicol. Appl. Pharmacol. 123, 257-264.
7. Fowler, B. A. (1972). Ultrastructural evidence for nephropathy induced by long term exposure to small amounts of methyl mercury. Science 175, 780-781.
8. Goyer, R. A., and Cherian, M. G. (1995). Renal effects of metals. In Metal Toxicology (R. A. Goyer, C. D. Klaassen, and M. P. Waalkes, Eds.), Chap. 25, pp. 389-412. Academic Press, San Diego.
9. Griztka, T. L., and Trump, B. F. (1968). Renal tubular lesions caused by mercuric chloride. Electron microscopic observations: degeneration of the pars recta. Am. J. Pathol. 52, 1225-1277.
10. Gurd, F. R. N., and Wilcox, P. E. (1956). Complex formation between metallic cations and proteins, peptides and amino acids. Adv. Protein Chem. 11, 311-427.
11. Hamel, D. M., White, C., and Eaton, D. L. (1992). Determination of γ-glutamylcysteine synthetase and glutathione synthetase activity by HPLC. Toxicol. Methods 1, 273-288.
12. Kriz, W., and Kaissling, B. (1992). Structural organization of the mammalian kidney. In The Kidney: Physiology and Pathophysiology (D. W. Seldin and G. Giebisch, Eds.). 2nd ed., Chap. 23, Vol. 1, pp. 707-777. Raven Press, New York.
13. Li, Y., and Jaiswal, K. (1994). Human antioxidant-response-element-mediated regulation of type 1 NAD(P)H:quinone oxidoreductase gene expression. Effect of sulfhydryl modifying agents. Eur. J. Biochem. 226, 31-39.
14. 2 production and lipid peroxidation in vitro in rat kidney mitochondria. Biochem. Pharmacol. 42, S181-S187.
15. 2 formation and oxidative stress in vivo and in vitro in rat kidney mitochondria. Biochem. Pharmacol. 45, 2017-2024.
16. Machlin, L. J., and Bendich, A. (1987). Free radical tissue damage: Protective role of antioxidant nutrients. FASEB J. 1, 441-445.
17. Meister, A. (1994). Glutathione, ascorbate, and cellular protection. Cancer Res. 54, 1969S-1975S.
18. Mulcahy, R. T., and Gipp, J. J. (1995). Identification of a putative antioxidant response element in the 5′-flanking region of the human γ-glutamylcysteine synthetase heavy subunit gene. Biochem. Biophys. Res. Commun. 209, 227-233.
19. Reed, D. J. (1990). Glutathione: Toxicological implications. Annu. Rev. Pharmacol. Toxicol. 30, 603-631.
20. Rushmore, T. H., Morton, M. R., and Pickett, C. B. (1991). The antioxidant response element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activation. J. Biol. Chem. 266, 11632-11639.
21. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989). Molecular Cloning. A Laboratory Manual, 2nd ed., Chapter 11, pp. 11.31-11.33, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
22. 2+ of cultured rabbit renal tubular cells. Biochim. Biophys. Acta 931, 130-142.
23. Smith, P. K., Krohn, R. I., Hermanson, G. T., Mallia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, G. K., Goere, N. M., Olson, B. J., and Klenk, D. C. (1985). Measurement of protein using bicinchoninic acid. Anal. Biochem. 150, 76-85.
24. Subrahmanyan, C. S., Cassidy, B., Busch, H., and Rothblum, L. I. (1982). Nucleotide sequence of the region between the 18S rRNA sequence and the 28S rRNA of rat ribosomal DNA. Nucleic Acids Res. 10, 3667-3680.
25. Trenga, C. A., Kunkel, D. D., Eaton, D. L., and Costa, L. G. (1991). Effect of styrene oxide on rat brain glutathione. Neurotoxicology 12, 165-178.
26. Trump, B. F., Berezesky, I. K., Smith, M. W., Phelps, P. C., and Elliget, K. A. (1989). The relationship between cellular ion deregulation and acute and chronic toxicity. Toxicol. Appl. Pharmacol. 97, 6-22.
27. Woods, J. S., Bowers, M. A., and Davis, H. A. (1991). Urinary porphyrin profiles as biomarkers of trace metal exposure and toxicity: Studies on urinary porphyrin excretion patterns in rats during prolonged exposure to methyl mercury. Toxicol. Appl. Pharmacol. 110, 464-476.
28. Woods, J. S., Calas, C. A., Aicher, L. D., Robinson, B. H., and Mailer, C. (1990a). Stimulation of porphyrinogen oxidation by mercuric ion. I. Evidence of free radical formation in the presence of thiols and hydrogen peroxide. Mol. Pharmacol. 38, 253-260.
29. Woods, J. S., Calas, C. A., and Aicher, L. D. (1990b). Stimulation of porphyrinogen oxidation by mercuric ion. II. Promotion of oxidation from the interaction of mercuric ion, glutathione, and mitochondria-generated hydrogen peroxide. Mol. Pharmacol. 38, 261-266.
30. Woods, J. S., Davis, H. A., and Bear, R. P. (1992). Enhancement of γ-glutamylcysteine synthetase mRNA in rat kidney by methylmercury. Arch. Biochem. Biophys. 296, 350-353.
31. Woods, J. S., and Ellis, M. E. (1995). Up-regulation of glutathione synthesis in rat kidney by methyl mercury. Relationship to mercury-induced oxidative tress. Biochem. Pharmacol. 50, 1719-1724.
32. Yan, C., Bentley, J. K., Sonnenburg, W. K., and Beavo, J. A. (1994). Differential expression of the 61 kDa and 63 kDa calmodulin-dependent phosphodiesterases in the mouse brain. J. Neurosci. 14, 973-984.
33. Yan, N., and Meister, A. (1990). Amino acid sequence of rat kidney γ-glutamylcysteine synthetase. J. Biol. Chem. 265, 1588-1593.