Effects of triethyl lead administration on the expression of glutathione S-transferase isoenzymes and quinone reductase in rat kidney and liver

Toxicology

Volumn 117, Issue 1, 1997, Pages 61-71

  Daggett, Daniel A ^a,b   Nuwaysir, Emile F ^a   Nelson, Shelli A ^b   Wright, Lynda S ^b,c   Kornguth, Steven E ^b,c   Siegel, Frank L ^a,b,c  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b UNIVERSITY OF WISCONSIN MADISON   (United States)

^c UNIVERSITY OF WISCONSIN SCHOOL OF MEDICINE AND PUBLIC HEALTH   (United States)

Author keywords

Glutathione S transferase; NAD(P)H:quinone oxidoreductase; Triethyl lead effects

Indexed keywords

GLUTATHIONE TRANSFERASE; ISOENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); TRIETHYLLEAD;

ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DETOXIFICATION; ENZYME ACTIVITY; KIDNEY; LIVER; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; RAT; TISSUE SPECIFICITY;

ANIMALS; GLUTATHIONE TRANSFERASE; INJECTIONS, INTRAPERITONEAL; ISOENZYMES; KIDNEY; LEAD; LIVER; NAD(P)H DEHYDROGENASE (QUINONE); ORGANOMETALLIC COMPOUNDS; RATS; RATS, INBRED F344;

ANIMALIA;

EID: 0031566988     PISSN: 0300483X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-483X(96)03555-X     Document Type: Article

References (41)

1. Ahotupa, M., Hartiala, K. and Aitio, A. (1979). Effects of tetraethyl lead on the activities of drug metabolizing enzymes in different tissues of the rat. Acta Pharmacol. Toxicol. 44, 359-363.
2. Alin, P., Jenssin, H., Cederlund, E., Jornvall, H. and Mannervik, B. (1989). Single step purification and h.p.l.c. analysis of glutathione S-transferase 8-8 in rat tissues. Biochem. J. 261, 531-539.
3. Beck. B.D. (1992). An update on exposure and effects of lead. Fundam. Appl. Toxicol. 18, 1-16.
4. Benson, A.M., Hunkeler, M.J. and Talalay, P. (1980). Increase of NAD(P)H:quinone reductase by dietary antioxidants: possible role in protection against carcinogenesis and toxicity. Proc. Natl. Acad. Sci. USA 77, 5216-5220.
5. Bergelson, S., Pinkus, R. and Daniel, V. (1994). Induction of AP-1 (Fos/Jun) by chemical agents mediates activation of glutathione S-transferase and quinone reductase gene expression. Oncogene 9, 565-571.
6. Bolanowska, W. (1968) Distribution and excretion of triethyl-lead in rats. Br. J. Ind. Med. 25, 203-208.
7. Bradford, M.M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
8. Chomczynski, P. and Sacchi, N. (1987). Single-step method of RNA isolation by acid guanidinium thiocyanate-phenolchloroform extraction. Anal. Biochem. 162, 156-159.
9. Daniel, V. (1993). Glutathione S-transferases: gene structure and regulation of expression. Crit. Rev. Biochem. Mol. Biol. 28, 173-207.
10. Di Ilio, C., Aceto, A., Columbano, A., Ledda-Columbano, G.M. and Federici, G. (1989). Induction of rat liver glutathione transferase subunit 7 by lead nitrate. Cancer Lett. 46, 167-171.
11. Dierickx, P.J. (1994). The influence of picolines on glutathione transferase activity and subunit composition in human liver derived Hep G2 cells. Biochem. Pharmacol. 48, 1976-1978.
12. Favreau, L.V. and Pickett, C.B. (1991). Transcriptional regulation of the rat NAD(P)H:quinone reductase gene. Identification of regulatory elements controlling basal level expression and inducible expression by planar aromatic compounds and phenolic antioxidants. J. Biol. Chem. 266, 4556-4561.
13. Gallagher, E.P., Buetler, T.M., Stapelton, P.L., Wang, C., Stahl, D.L. and Eaton. D.L. (1995). The effects of diquat and clofibrate on mRNA expression and catalytic activities of hepatic xenobiotic metabolizing and antioxidant enzymes in rat liver. Toxicol. Appl. Pharmacol. 134, 81-91.
14. Goldstein, G. and Ar, D. (1983). Lead activates calmodulin sensitive processes. Life Sci. 33. 1001-1006.
15. Goyer, R.A. (1971). Lead and the kidney. Curr. Top. Pathol. 55, 147-176.
16. Habig, W.H. and Jakoby, W.B. (1981). Glutathione S-transferases (rat and human). Methods Enzymol. 77, 218-231.
17. Hayes, J.D. (1988). Selective elution of rodent glutathione S-transferases and glyoxylase I from the S-hexylglutathione-Sepharose affinity matrix. Biochem. J. 255, 913-922.
18. Hayes, J.D. and Pulford, D.J. (1995). The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit. Rev. Biochem. Mol. Biol. 30, 445-600.
19. Imagawa, M., Osada, S., Okuda, A. and Muramatsu, M. (1991). Silencer binding proteins function on multiple cis-elements in the glutathione transferase P gene. Nucleic Acids Res. 19, 5-10.
20. Johnson, J.A., Neal, T.L., Collins, J.H. and Siegel, F.L. (1990). Characterization of methylation of rat liver cytosolic glutathione S-transferases by using reverse-phase h.p.l.c. and chromatofocusing. Biochem. J. 270, 483-489.
21. Lee. S.J. and Boyer, T.D. (1993). The effect of hepatic regeneration on the expression of the glutathione S-transferases. Biochem. J. 293, 137-142.
22. Li, Y. and Jaiswal, A.K. (1992). Regulation of human NAD(P)H:quinone oxidoreductase gene. Role of AP1 binding site contained within human antioxidant response element. J. Biol. Chem. 267, 15097-15104.
23. Mannervik, B. and Danielson, U.H. (1988). Glutathine transferases: structure and catalytic activity. CRC Crit. Rev. Biochem. 23, 283-337.
24. Markovac, J. and Goldstein, G.W. (1988). Picomolar concentrations of lead stimulate brain protein kinase C. Nature. 334, 71-73.
25. McLellan, L.I. and Hayes, J.D. (1989). Differential regulation of murine glutathione S-transferases by xenobiotics. In: J.D. Hayes, C.B. Pickett, and T.J. Mantle (Eds.), Glutathione S-Transferases and Drug Resistance, Taylor and Francis, New York, pp. 196-211.
26. Moser, R., Oberley, T.D., Daggett, D.A., Friedman, A.L., Johnson, J.A. and Siegel, F.L. (1995). Effects of lead on developing rat kidney. L Glutathione S-transferase isoenzymes. Toxicol. Appl. Pharmacol. 131, 85-93.
27. Oberley, T.D., Friedman, A.L., Moser, R. and Siegel, F.L. (1995). Effects of lead administration on developing rat kidney. II. Functional, morphologic and immunohistochemical studies. Toxicol. Appl. Pharmacol. 131, 94-107.
28. Ostlund Farrants, A.K., Meyer, D.J., Coles, B., Southan, C., Aitken, A., Johnson, P.J. and Ketterer, B. (1987). The separation of glutathione S-transferase subunits by using reverse-phase high-pressure liquid chromatography. Biochem. J. 245, 423-428.
29. Pinkus, R., Bergelson, S. and Daniel, V. (1993). Phenobarbital induction of AP-1 binding activity mediates activation of glutathione S-transferase and quinone reductase gene expression. Biochem. J. 290, 637-650.
30. Planas-Bohne, F. and Elizalde. M. (1992). Activity of glutathione S-transferase in rat liver and kidneys after administration of lead or cadmium. Arch. Toxicol. 66, 365-367.
31. Prochaska. H.J. and Fernandes, C.L. (1993). Elevation of phase II enzymes by anticarcinogenic enzyme inducers:markers for a chemoprotected state? Carcinogenesis 14, 2441-2445.
32. Roomi, M.W., Columbando. A., Ledda-Columbano, G.M. and Sarama, D.S.R. (1987). Induction of the placental form of glutathione S-transferase by lead nitrate administration in rat liver. Toxicol. Pathol. 15, 202-205.
33. Rushmore, T.H. and Pickett, C.B. (1989). Regulation of glutathione S-transferase Ya subunit gene expression by planar aromatic compounds. In: J.D. Hayes, C.B. Pickett, and T.J. Mantle (Eds). Glutathione S-transferases and Drug Resistance. Taylor and Francis, New York, pp. 157-164.
34. Rushmore, T.H. and Pickett, C.B. (1993). Glutathione S-transferases, structure, regulation, and therapeutic implications. J. Biol. Chem. 268, 11475-11478.
35. Segura-Aguilar, J., Kaiser, R. and Lind, C. (1992). Separation and characterization of isoenzymes of DT-diaphorase from rat liver cytosol. Biochim. Biophys. Acta 1120, 33-42.
36. Simons, P.C. and VanderJagt, D.L. (1981). Purification of glutathione S-transferases by glutathione-affinity chromatography. Methods Enzymol. 77, 235-237.
37. Spencer, S.R., Xue, L., Klenz, E.M. and Talalay, P. (1991). The potency of inducers of NAD(P)H:(quinone acceptor) oxidoreductase parallels the efficacy as substrates for glutathione transferases. Biochem. J. 273, 711-717.
38. Stone, E.M., Rothblum, K.N., Alevy, M.C., Kuo, T.M. and Schwartz, R.J. (1985). Complete sequence of the chicken glyceraldehyde-3-phosphate dehydrogenase gene. Proc. Nat. Acad. Sci. 82, 1628-1632.
39. Suzuki, T., Morimura, S., Diccianni, M.B., Yamada, R., Hochi, M., Yuki, A., Nomura, K., Kitagawa, T., Imagawa, M. and Muramatsu, M. (1996) Activation of glutathione S-transferase P gene by lead requires glutathione transferase P enhancer. J. Biol. Chem. 271, 1626-1632.
40. Waxman, D.J., Sundesth, S.S., Srivastava, P.K. and Lapenson, D.P. (1992). Gene-specific oligonucleotide probes for alpha, mu, pi and microsomal rat glutathione S-transferases: analysis of liver transferase expression and its modulation by hepatic enzyme inducers and platinum anticancer drugs. Cancer Res. 52, 5797-5802.
41. Westwick, J.K., Weitzel, C., Minden, A., Karin, M. and Brenner, D.A. (1994). Tumor necrosis factor alpha stimulates AP-1 activity through prolonged activation of the c-Jun kinase. J. Biol. Chem. 269, 26936-26401.