Compartmental inhibition of hepatic glutathione reductase activities by 1,3-bis(2-chloroethyl)-N-nitrosourea (BCNU) in Sprague-Dawley and Fischer-344 rats

Toxicology Letters

Volumn 147, Issue 3, 2004, Pages 219-228

  Jopperi Davis, Katrina S ^a   Park, Min Soo ^a,b   Rogers, Lynette K ^a   Backes Jr , Carl H ^a   Lim, In Kyoung ^c   Smith, Charles V ^a  

^a THE RESEARCH INSTITUTE AT NATIONWIDE CHILDREN S HOSPITAL   (United States)

^b Yonsei University College of Medicine   (South Korea)

^c Ajou University School of Medicine   (South Korea)

Author keywords

1,3 Bis(2 chloroethyl) N nitrosourea (BCNU); Fischer 344 rats; Glutathione peroxidase; Glutathione reductase; O 6 Alkylguanine DNA alkyltransferase (AGT, MGMT); Sprague Dawley rats

Indexed keywords

6 O ALKYLGUANINE DNA ALKYLTRANSFERASE INHIBITOR; CARMUSTINE; GLUTATHIONE REDUCTASE; LIVER ENZYME; REACTIVE OXYGEN METABOLITE;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CELL DEATH; CENTRIFUGATION; CONTROLLED STUDY; CYTOSOL; ENZYME ACTIVITY; ENZYME INHIBITION; LIVER; LIVER HOMOGENATE; LIVER INJURY; LIVER NECROSIS; LIVER TOXICITY; MALE; MICROSOME; MITOCHONDRION; NONHUMAN; PRIORITY JOURNAL; RAT; RAT STRAIN; STRAIN DIFFERENCE;

EID: 0842324415     PISSN: 03784274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxlet.2003.10.017     Document Type: Article

References (31)

1. Blakeman D.P., Ryan T.P., Jolly R.A., Petry T.W. Protein oxidation: examination of potential lipid-independent mechanisms for protein carbonyl formation. J. Biochem. Mol. Toxicol. 12:1998;185-190.
2. 6-(2-chloroethyl)guanine mediates the biological effects of chloroethylnitrosoureas. Environ. Health Perspect. 62:1985;119-126.
3. 6-alkylguanine DNA adducts in glioma-derived human cells resistant to the cytotoxic and cytogenetic effects of 1,3-bis(2-chloroethyl)-1- nitrosourea. Carcinogenesis. 7:1986;879-883.
4. 6-alkylguanine-DNA alkyltransferases. Cancer Res. 60:2000;5464-5469.
5. Fu Y., Cheng W.H., Porres J.M., Ross D.A., Lei X.G. Knockout of cellular glutathione peroxidase gene renders mice susceptible to diquat-induced oxidative stress. Free Radic. Biol. Med. 27:1999;605-611.
6. Gilbert H.F. Thiol/disulfide exchange equilibria and disulfide bond stability. Methods Enzymol. 251:1995;8-28.
7. Gupta S., Husser R.C., Geske R.S., Welty S.E., Smith C.V. Sex differences in diquat-induced hepatic necrosis and DNA fragmentation in Fischer-344 rats. Toxicol. Sci. 54:2000;203-211.
8. Gupta S., Kleiner H.E., Rogers L.K., Lau S.S., Smith C.V. Redox stress and hepatic DNA fragmentation induced by diquat in vivo are not accompanied by increased 8-hydroxydeoxyguanosine contents. Redox Rep. 3:1997;31-39.
9. Jones D.P., Mody V.C. Jr., Carlson J.L., Lynn M.J., Sternberg P. Jr. Redox analysis of human plasma allows separation of pro-oxidant events of aging from decline in antioxidant defenses. Free Radic. Biol. Med. 33:2002;1290-1300.
10. Kehrer J.P. The effect of BCNU (carmustine) on tissue glutathione reductase activity. Toxicol. Lett. 17:1983;63-68.
11. Kehrer J.P., Haschek W., Witschi H. The influence of hyperoxia on the acute toxicity of paraquat and diquat. Drug Chem. Toxicol. 2:1979;397-408.
12. Kehrer J.P., Paraidathathu T. Enhanced oxygen toxicity following treatment with 1,3-bis(2-chloroethyl)-1-nitrosourea. Fundam. Appl. Toxicol. 4:1984;760-767.
13. Lauterburg B.H., Smith C.V., Hughes H., Mitchell J.R. Biliary excretion of glutathione and glutathione disulfide in the rat: regulation and response to oxidative stress. J. Clin. Invest. 73:1984;124-133.
14. Lawrence R.A., Burk R.F. Glutathione peroxidase activity in selenium-deficient rat liver. Biochem. Biophys. Res. Commun. 71:1976;952-958.
15. 6-methylguanine-DNA methyltransferase during diethylnitrosamine-induced carcinogenesis and liver regeneration in Sprague-Dawley male rats. J. Cancer Res. Clin. Oncol. 125:1999;493-499.
16. Lind C., Gerdes R., Hamnell Y., Schuppe-Koistinen I., von Lowenhielm H.B., Holmgren A., Cotgreave I.A. Identification of S-glutathionylated cellular proteins during oxidative stress and constitutive metabolism by affinity purification and proteomic analysis. Arch. Biochem. Biophys. 406:2002;229-240.
17. Maze R., Carney J.P., Kelley M.R., Glassner B.J., Williams D.A., Samson L. Increasing DNA repair methyltransferase levels via bone marrow stem cell transduction rescues mice from the toxic effects of 1,3-bis(2-chloroethyl)-1- nitrosourea, a chemotherapeutic alkylating agent. Proc. Natl. Acad. Sci. U.S.A. 93:1996;206-210.
18. Mitchell J.R., Jollow D.J., Potter W.Z., Gillette J.R., Brodie B.B. Acetaminophen-induced hepatic necrosis. IV. Protective role of glutathione. J. Pharmacol. Exp. Ther. 187:1973;211-217.
19. Rikans L.E., Ardinska V., Hornbrook K.R. Age-associated increase in ferritin content of male rat liver: implication for diquat-mediated oxidative injury. Arch. Biochem. Biophys. 344:1997;85-93.
20. Rogers L.K., Gupta S., Welty S.E., Hansen T.N., Smith C.V. Nuclear and nucleolar glutathione reductase, peroxidase, and transferase activities in livers of male and female Fischer-344 rats. Toxicol. Sci. 69:2002;279-285.
21. Rogers L.K., Smith C.V. Coenzyme A and coenzyme A-glutathione disulfide measurements by HPLC. Curr. Protocols Toxicol. Suppl. 15:2003;6.9.1-6.9.8.
22. Rogers L.K., Valentine C.J., Szczypka M., Smith C.V. Effects of hepatotoxic doses of acetaminophen and furosemide on tissue concentrations of CoASH and CoASSG in vivo. Chem. Res. Toxicol. 13:2000;873-882.
23. Smith C.V. Effect of BCNU pretreatment on diquat-induced oxidant stress and hepatotoxicity. Biochem. Biophys. Res. Commun. 144:1987a;415-421.
24. Smith C.V. Evidence for the participation of lipid peroxidation and iron in diquat-induced hepatic necrosis in vivo. Mol. Pharmacol. 32:1987b;417-422.
25. Smith C.V. Correlations and apparent contradictions in assessment of oxidant stress status in vivo. Free Radic. Biol. Med. 10:1991;217-224.
26. Smith, C.V., 1992. Free radical mechanisms of tissue injury. In: Moslen, M.T., Smith, C.V. (Eds.), Free Radical Mechanisms of Tissue Injury. CRC Press, Boca Raton, pp. 1-22.
27. Smith, C.V., Hughes, H., Lauterburg, B.H., Mitchell, J.R., 1983. Chemical nature of reactive metabolites determines their biological interactions with glutathione. In: Larsson, A., Orrenius, S., Holmgren, A., Mannervik, B. (Eds.), Functions of Glutathione: Biochemical, Physiological, Toxicological, and Clinical Aspects. Raven Press, New York, pp. 125-138.
28. Smith C.V., Hughes H., Lauterburg B.H., Mitchell J.R. Oxidant stress and hepatic necrosis in rats treated with diquat. J. Pharmacol. Exp. Ther. 235:1985;172-177.
29. Smith, C.V., Welty, S.E., 1999. Molecular mechanisms of oxygen-induced lung injury. In: Bland, R.D., Coalson, J.J. (Eds.), Chronic Lung Disease of Early Infancy. Marcel Dekker, New York, pp. 749-777.
30. Tamura T., McMicken H.W., Smith C.V., Hansen T.N. Mitochondrial targeting of glutathione reductase requires a leader sequence. Biochem. Biophys. Res. Commun. 222:1996;659-663.
31. 1-deoxyguanosyl]-ethane in DNA treated with N,N′-bis(2-chloroethyl)-N-nitrosourea. Cancer Res. 42:1982;3102-3105.