Glutathione depletion exacerbates methylenedianiline toxicity to biliary epithelial cells and hepatocytes in rats

Toxicological Sciences

Volumn 74, Issue 2, 2003, Pages 447-456

  Kanz, Mary F ^a   Dugas, Tammy R ^b   Liu, Hanlin ^a   Santa Cruz, Vicente ^a,c  

^a University of Texas Medical Branch School of Medicine   (United States)

^b LOUISIANA STATE UNIVERSITY HEALTH SCIENCES CENTER   (United States)

^c CHEVRON PHILLIPS CHEMICAL COMPANY LP   (United States)

Author keywords

Apoptosis; Bromoheptane; Buthionine sulfoximine; CoASH CoASSG; Glutathione depletion; GSH GSSG; Methylenedianiline; Oncosis

Indexed keywords

1 NAPHTHYL ISOTHIOCYANATE; 4,4' METHYLENEDIANILINE; BUTHIONINE SULFOXIMINE; COENZYME A; DISULFIDE; GLUTATHIONE; GLUTATHIONE DISULFIDE; GLUTATHIONE TRANSFERASE; HEPTANE; THIOBARBITURIC ACID REACTIVE SUBSTANCE; THIOL;

AMINO ACID DEFICIENCY; ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; APOPTOSIS; BILIARY TRACT INFLAMMATION; CELL STRUCTURE; CLINICAL PROTOCOL; COMMON BILE DUCT; CONTROLLED STUDY; CYTOTOXICITY; DISEASE EXACERBATION; EDEMA; ENZYME ACTIVITY; ENZYME LOCALIZATION; HEPATIC ARTERY; HEPATOBILIARY SYSTEM; LIVER CELL; LIVER CELL DAMAGE; LIVER INJURY; LIVER TOXICITY; MALE; NONHUMAN; PORTAL VEIN; RAT; REVIEW;

ALLERGENS; ANILINE COMPOUNDS; ANIMALS; APOPTOSIS; BILE DUCTS; BUTHIONINE SULFOXIMINE; COENZYME A; DNA FRAGMENTATION; EPITHELIAL CELLS; GLUTATHIONE; HEPATOCYTES; HYDROCARBONS, BROMINATED; MALE; RATS; RATS, SPRAGUE-DAWLEY; THIOBARBITURIC ACID REACTIVE SUBSTANCES;

ANIMALIA;

EID: 0043092131     PISSN: 10966080     EISSN: None     Source Type: Journal    
DOI: 10.1093/toxsci/kfg125     Document Type: Review

References (57)

1. Anders, M. W. (1978). Inhibition and enhancement of microsomal drug metabolism by diethyl maleate. Biochem. Pharmacol. 27, 1098-1101.
2. Anders, M. W., and Dekant, W. (1998). Glutathione-dependent bioactivation of haloalkenes. Ann. Rev. Pharmacol. Toxicol. 38, 501-537.
3. Baggett, J. M., and Berndt, W. O. (1986). The effect of depletion of nonprotein sulfhydryls by diethyl maleate plus buthionine sulfoximine on renal uptake of mercury in the rat. Toxicol. Appl. Pharmacol. 83, 556-562.
4. Baker, M. J., Cerniglia, G. J., and Zaman, A. (1990). Microtiter plate assay for the measurement of glutathione disulfide in large numbers of biological samples. Anal. Biochem. 190, 360-365.
5. Barnes, M. M., James, S. P., and Wood, P. B. (1959). The formation of mercapturic acids. 1. Formation of mercapturic acid and the levels of glutathione in tissues. Biochem. J. 71, 680-689.
6. Burk, R. F., and Correia, M. A. (1979). Stimulation of rat hepatic microsomal heme oxygenase by diethyl maleate. Res. Commun. Chem. Pathol. Pharmacol. 24, 205-207.
7. Cocker, J., Gristwood, W., and Wilson, H. K. (1986). Assessment of occupational exposure to 4,4′-diaminodiphenylmethane (methylene dianiline) by gas chromatography-mass spectrometry analysis of urine. Br. J. Ind. Med. 43, 620-625.
8. Corrales, F., Ochoa, P., Rivas, C., Martin-Lomas, M., Mato, J. M., and Pajares, M. A. (1991). Inhibition of glutathione synthesis in the liver leads to S-adenosyl-L-methionine synthetase reduction. Hepatology 14, 528-533.
9. Crane, D., Haussinger, D., and Sies, H. (1982). Rise of coenzyme A-glutathione mixed disulfide during hydroperoxide metabolism in perfused rat liver. Eur. J. Biochem. 127, 575-578.
10. Dahm, L. J., and Roth, R. A. (1991). Protection against α-naphthylisothiocyanate-induced liver injury by decreased hepatic non-protein sulfhydryl content. Biochem. Pharmacol. 42, 1181-1188.
11. Dhakshinamoorthy, S., Long, D. J. II, and Jaiswal, A. K. (2000). Antioxidant regulation of genes encoding enzymes that detoxify xenobiotics and carcinogens. Curr. Top. Cell. Regul. 36, 201-216.
12. Dyer, R. E., and Wilken, D. R. (1972). Rat liver levels of coenzyme A-glutathione and of enzymes in its metabolism. Arch. Biochem. Biophys. 153, 619-626.
13. Eaton, D. L., and Bammler, T. K. (1999). Concise review of the glutathione S-transferases and their significance to toxicology. Toxicol. Sci. 49, 156-164.
14. Esterbauer, H., and Cheeseman, K. H. (1990). Determination of aldehydic lipid peroxidation products: malonaldehyde and 4-hydroxynonenal. Methods Enzymol. 186, 407-421.
15. Farooqui, M. Y. H., and Ahmed, A. E. (1984). Circadian periodicity of tissue glutathione and its relationship with lipid peroxidation in rats. Life Sci. 34, 2413-2418.
16. Gerard-Monnier, D., Fougeat, S., and Chaudiere, J. (1992). Glutathione and cysteine depletion in rats and mice following acute intoxication with diethylmaleate. Biochem. Pharmacol. 43, 451-456.
17. Grasl-Kraupp, B., Ruttkay-Nedecky, B., Koudelka, H., Bukowska, K., Bursch, W., and Schulte-Hermann, R. (1995). In situ detection of fragmented DNA (TUNEL assay) fails to discriminate among apoptosis, necrosis, and autolytic cell death: A cautionary note. Hepatology 21, 1465-1468.
18. Griffith, O. W. (1981). Depletion of glutathione by inhibition of biosynthesis. Methods Enzymol. 77, 59-63.
19. Habig, W. H., Pabst, M. J., and Jakoby, W. B. (1974). Glutathione S-transferases: The first enzymatic step in mercapturic acid formation. J. Biol. Chem. 249, 7130-7139.
20. International Agency for Research on Cancer (IARC). (1986). IARC Monographs on the Evaluation of Carcinogenic Risk of Chemicals to Humans, Vol. 39, Chemicals Used in Plastics and Elastomers, pp. 347-365. Lyon, France.
21. Jaeschke, H., and Wendel, A. (1985). Diurnal fluctuation and pharmacological alteration of mouse organ glutathione content. Biochem. Pharmacol. 34, 1029-1033.
22. Jean, P. A., and Roth, R. A. (1995). Naphthylisothiocyanate disposition in bile and its relationship to liver glutathione and toxicity. Biochem. Pharmacol. 50, 1469-1474.
23. Jin, K., Chen, J., Nagayama, T., Chen, M., Sinclair, J., Graham, S. H., and Simon, R. P. (1999). In situ detection of neuronal DNA strand breaks using the Klenow fragment of DNA polymerase I reveals different mechanisms of neuron death after global cerebral ischemia. J. Neurochem. 72, 1204-1214.
24. Kanz, M. F., Gunasena, G. H., Kaphalia, L., Hammond, D. K., and Syed, Y. A. (1998). A minimally toxic dose of methylene dianiline injures biliary epithelial cells in rats. Toxicol. Appl. Pharmacol. 150, 414-426.
25. Kanz, M. F., Kaphalia, L., Kaphalia, B. S., Romagnoli, E., and Ansari, G. A. S. (1992). Methylene dianiline: Acute toxicity and effects on biliary function. Toxicol. Appl. Pharmacol. 117, 88-97.
26. Kanz, M. F., Wang, A., and Campbell, G. A. (1995). Infusion of bile from methylene dianiline treated rats into the common bile duct injures biliary epithelial cells of recipient rats. Toxicol. Lett. 78, 165-178.
27. Khan, S., and O'Brien, P. J. (1991). 1-Bromoalkanes as new potent nontoxic glutathione depletors in isolated rat hepatocytes. Biochem. Biophys. Res. Commun. 179, 436-441.
28. Kobayashi, T., Robinson, M. K., Robinson, V., DeRosa, E., Wilmore, D. W., and Jacobs, D. O. (1993). Glutathione depletion alters hepatocellular high-energy phosphate metabolism. J. Surg. Res. 54, 189-195.
29. Kopelman, H., Scheuer, P. J., and Williams, R. (1966). The liver lesion of the Epping jaundice. Q. J. Med. 35, 533-564.
30. Koss, F. W., Mayer, D., and Haindl, H. (1974). Bile acids. Methods Enzymol. Anal. 4, 1886-1888.
31. Kroemer G., Dallaporta, B., and Resche-Rigon, M. (1998). The mitochondrial death/life regulator in apoptosis and necrosis. Annu. Rev. Physiol. 60, 619-642.
32. Lemasters, J. J. (1999). Mechanisms of hepatic toxicity. V. Necrapoptosis and the mitochondrial permeability transition: Shared pathways to necrosis and apoptosis. Am. J. Physiol. Gastrointest. Liver Physiol. 276, G1-G6.
33. Levin, S., Bucci, T. J., Cohen, S. M., Fix, A. S., Hardisty, J. F., LeGrand, E. K., Maronpot, R. R., and Trump, B. F. (1999). The nomenclature of cell death: Recommendations of an ad hoc committee of the Society of Toxicologic Pathologists. Toxicol. Pathol. 27, 484-490.
34. Meredith, M. J., and Reed, D. J. (1983). Depletion in vitro of mitochondrial glutathione in rat hepatocytes and enhancement of lipid peroxidation by adriamycin and 1,3-bis(2-chloroethyl)-1-nitorsourea (BCNU). Biochem. Pharmacol. 32, 1383-1388.
35. Miccadei, S., Kyle, M. E., Gilfor, D., and Farber, J. L. (1988). Toxic consequence of the abrupt depletion of glutathione in cultured rat hepatocytes. Arch. Biochem. Biophys. 265, 311-320.
36. 1 to DNA in the mouse. Toxicol. Appl. Pharmacol. 94, 118-127.
37. Moore, W. M. (1978). Methylenedianiline. In Kirk-Othmer Encyclopedia of Chemical Technology, (H. F. Mark, D. F. Othmer, C. G. Overgerger, and G. T. Seaborg, Eds.), 3rd ed., Vol. 2, pp. 338-348. John Wiley & Sons, New York.
38. Mulder, G. J., and Ouwerkerk-Mahadevan, S. (1997). Modulation of glutathione conjugation in vivo: How to decrease glutathione conjugation in vivo or in intact cellular systems in vitro. Chemico-Biol. Interact. 105, 17-34.
39. +-linked assay for microsomal uridine diphosphate glucuronyltransferase of rat liver and some observations on substrate specificity of the enzyme. Biochem. J. 151, 131-140.
40. Nagai, H., Matsumaru, K., Feng, G., and Kaplowitz, N. (2002). Reduced glutathione depletion causes necrosis and sensitization to tumor necrosis factor-α-induced apoptosis in cultured mouse hepatocytes. Hepatology 36, 55-64.
41. O'Donovan, D. J., Rogers, L. K., Kelley, D. K., Welty, S. E., Ramsay, P. L., and Smith, C. V. (2002). CoASH and CoASSG levels in lungs of hyperoxic rats as potential biomarkers of intramitochondrial oxidant stresses. Pediatr. Res. 51, 346-353.
42. Ohno, M., Takemura, G., Ohno, A., Misao, J., Hayakawa, Y., Minatoguchi, S., Fujiwara, T., and Fujiwara, H. (1998). "Apoptotic" myocytes in infarct area in rabbit hearts may be oncotic myocytes with DNA fragmentation. Analysis by immunogold electron microscopy combined with in situ nick end-labeling. Circulation 98, 1422-1430.
43. Parola, M., Cheeseman, K. H., Biocca, M. E., Dianzani, M. U., and Slater, T. F. (1990a). Biochemical studies on bile duct epithelial cells isolated from rat liver. J. Hepatol. 10, 341-345.
44. Parola, M., Cheeseman, K. H., Biocca, M. E., Dianzani, M. U., and Slater, T. F. (1990b). Menadione and cumene hydroperoxide induced cytotoxicity in biliary epithelial cells isolated from rat liver. Biochem. Pharmacol. 39, 1727-1734.
45. Pikul, J., Leszczynski, N. D., and Kummerow, F. A. (1983). Elimination of sample autoxidation by butylated hydroxytoluene additions before thiobarbituric acid assay for malonaldehyde in fat from chicken meat. J. Agric. Food Chem. 31, 1338-1342.
46. Rogers, L. K., Valentine, C. J., Szczpyka, M., and Smith, C. V. (2000). Effects of hepatotoxic doses of acetaminophen and furosemide on tissue concentrations of CoASH and CoASSG in vivo. Chem. Res. Toxicol. 13, 873- 882.
47. Seçkin, S., Başaran-Küçükgergin, C., and Uysal, M. (1999). Effect of acute and chronic administration of sodium valproate on lipid peroxidation and antioxidant system in rat liver. Pharmacol. Toxicol. 85, 294-298.
48. Shintani, H., and Nakamura, A. (1989). Analysis of a carcinogen, 4,4′-methylenedianiline, from thermosetting polyurethane during sterilization. J. Anal. Toxicol. 13, 354-357.
49. Siess, E. A., Brocks, D. G., and Wieland, O. H. (1978). Distribution of metabolites between the cytosolic and mitochondrial compartments of hepatocytes isolated from fed rats. Hoppe-Seyler's Z. Physiol. Chem. 359, 785-798.
50. Smith, P. K., Krohn, R. I., Hermanson, G. T., Malia, A. K., Gartner, F. H., Provenzano, M. D., Fujimoto, E. K., Goeke, N. M., Olson, B. J., and Klenk, D. C. (1985). Measurement of protein using bicinchoninic acid. Anal. Biochem. 150, 76-85.
51. Soboll, S., Scholz, R., Freisl, M., Elbers, R., and Heldt, H. W. (1976). Distribution of metabolites between mitochondria and cytosol of perfused liver. In Use of Isolated Liver Cells and Kidney Tubules in Metabolic Studies (J. M. Tager, H.-D. Soling, and J. R. Williamson, Eds.), pp. 29-40. North-Holland, Amsterdam.
52. Tietze, F. (1969). Enzymatic method for quantitative determination of nanogram amounts of total and oxidized glutathione. Anal. Biochem. 27, 502-515.
53. Videla, L. A., Fernandez, V., Ugarte, G., and Valenzuela A. (1980). Effect of acute ethanol intoxication on the content of reduced glutathione of the liver in relation to its lipoperoxidative capacity in the rat. FEBS Lett. 111, 6-10.
54. Vore, M. (1993). Canalicular transport: Discovery of ATP-dependent mechanisms. Toxicol. Appl. Pharmacol. 118, 2-7.
55. Yoshida, T., Oguro, T., Numazawa, S., and Kuroiwa Y. (1987). Effects of phorone (diisopropylidene acetate), a glutathione (GSH) depletor, on hepatic enzymes involved in drug and heme metabolism in rats: Evidence that phorone is a potent inducer of heme oxygenase. Biochem. Biophys. Res. Commun. 145, 502-508.
56. Younes, M., Schlichting, R., and Siegers, C.-P. (1980). Effect of metabolic inhibitors, diethylmaleate and carbon tetrachloride-induced liver damage on glutathione S-transferase activities in rat liver. Pharmacol. Res. Commun. 12, 921-930.
57. Zhang, W., Khanna, P., Chan, L. L., Campbell, G., and Ansari, N. H. (1997). Diabetes-induced apoptosis in rat kidney. Biochem. Mol. Med. 61, 58-62.