Gene transfer of mitochondrially targeted glutathione reductase protects H441 cells from t-butyl hydroperoxide-induced oxidant stresses

American Journal of Respiratory Cell and Molecular Biology

Volumn 20, Issue 2, 1999, Pages 256-263

  O'Donovan, Donough J ^a   Katkin, Julie P ^a   Tamura, Toshiya ^a   Husser, Richard ^a   Xu, Xudong ^a   Smith, Charles V ^a   Welty, Stephen E ^a  

^a BAYLOR COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOVIRIDAE; CRICETINAE; CRICETULUS GRISEUS;

GLUTATHIONE; GLUTATHIONE DISULFIDE; GLUTATHIONE REDUCTASE; LACTATE DEHYDROGENASE; SIGNAL PEPTIDE; TERT BUTYL HYDROPEROXIDE;

ARTICLE; CELL LINE; ENZYME ACTIVATION; ENZYMOLOGY; GENE TRANSFER; GENETICS; HUMAN; METABOLISM; MITOCHONDRION; OXIDATIVE STRESS;

CELL LINE, TRANSFORMED; ENZYME ACTIVATION; GENE TRANSFER TECHNIQUES; GLUTATHIONE; GLUTATHIONE DISULFIDE; GLUTATHIONE REDUCTASE; HUMANS; L-LACTATE DEHYDROGENASE; MITOCHONDRIA; OXIDATIVE STRESS; PROTEIN SORTING SIGNALS; TERT-BUTYLHYDROPEROXIDE;

EID: 0033071047     PISSN: 10441549     EISSN: None     Source Type: Journal    
DOI: 10.1165/ajrcmb.20.2.3367     Document Type: Article

References (50)

1. Deneke, S. M., and B. I., Fanburg. 1980. Normobaric oxygen toxicity of the lung. N. Engl. J. Med. 303:76-86.
2. Frank, L., and D. Massaro. 1980. Oxygen toxicity. Am. J. Med. 69:117-126.
3. Frank, L. 1985. Effects of oxygen on the newborn. Fed. Proc. 44:2328-2334.
4. Freeman, B. A., and J. D. Crapo. 1981. Hyperoxia increases oxygen radical production in rat lungs and lung mitochondria. J. Biol. Chem. 256:10986-10992.
5. Yusa, T., J. D. Crapo, and B. A. Freeman. 1984. Hyperoxia enhances lung and liver nuclear superoxide generation. Biochem. Biophys. Acta 798:167-174.
6. Halliwell, B. 1996. Free radicals, proteins and DNA: Oxidative damage versus redox regulation. Biochem. Soc. Trans. 24:1023-1027.
7. McCord, J. M., and I. Fridovich. 1978. The biology and pathology of oxygen radicals. Ann. Int. Med. 89:122-127.
8. Fridovich, I. 1978. The biology of oxygen radicals. Science 201:875-880.
9. Vilar-Rojas, C., A. M. Guzman-Grenfell, and J. J. Hicks. 1996. Participation of oxygen free radicals in the oxido-reduction of proteins. Arch. Med. Res. 27:1-6.
10. Bongarzone, E. R., J. M. Pasquini, and E. F. Soto. 1995. Oxidative damage to proteins and lipids of CNS myelin produced by in vitro generated reactive oxygen species. J. Neurosci. Res. 41:213-221.
11. Gerard-Monnier, D., and J. Chaudiere. 1996. Metabolism and antioxidant function of glutathione. Pathol. Biol. (Paris) 44:77-85.
12. Reed, D. J. 1990. Glutathione: toxicological implications. Ann. Rev. Pharmacol. Tox. 30:603-631.
13. Babson, J. R., N. S. Abell, and D. J. Reed. 1981. Protective role of the glutathione redox cycle against adriamycin-mediated toxicity in isolated hepatocytes. Biochem. Pharmacol. 30:2299-2304.
14. Reed, D. J., G. A. Pascoe, and K. Olafsdottir. 1987. Some aspects of cell defense mechanisms of glutathione and vitamin E during cell injury. Arch. Tox. Supp. 11:34-38.
15. Reed, D. J., and M. W. Fariss. 1984. Glutathione depletion and susceptibility. Pharm. Rev. 36:S25-S33.
16. Tonoki, H. 1994. Establishment of Chinese hamster ovary cell lines with reduced expression of glutathione reductase after antisense-oriented gene transfection and assessment of the sensitivity to oxidant injury. Hokkaido J. Med. Sci. 69:1261-1274.
17. Kehrer, J. P., and T. Paraidathathu. 1984. Enhanced oxygen toxicity following treatment with 1,3-bis(2-chloroethyl)-1-nitrosourea. Fund. Appl. Toxi col. 4:760-767.
18. Loos, H., W. D. Roos, M. J. Meredith, and D. J. Reed. 1983. Depletion in vitro of mitochondrial glutathione in rat hepatocytes and enhancement of lipid peroxidation by adriamycin and 1,3-bis(2-chloroethyl)-1-nitrosourea. Biochem. Pharmacol. 32:1383-1388.
19. Cholin, S., H. Tonoki, T. N. Hansen, and F. D. Ledley. 1993. Expression of recombinant human glutathione reductase in eukaryotic cells after DNA-mediated gene transfer. Biochem. Med. Metab. Biol. 49:108-113.
20. Tamura, T., H. W. McMicken, C. V. Smith, and T. N. Hansen. 1996. Mitochondrial targeting of glutathione reductase requires a leader sequence. Biochem. Biophys. Res. Commun. 222:659-663.
21. Tamura, T., H. W. McMicken, C. V. Smith, and T. N. Hansen. 1997. Over-expression of human glutathione reductase in Chinese hamster ovary cells protects cells from oxidant injury. Pediatr. Res. 39:A248. (Abstr.)
22. Tamura, T., H. W. McMicken, C. V. Smith, and T. N. Hansen. 1997. Gene structure for mouse glutathione reductase, including a putative mitochondrial targeting signal. Biochem. Biophys. Res. Commun. 237:419-422.
23. Smith, C. V., T. N. Hansen, N. E. Martin, H. W. McMicken, and S. J. Elliott. 1993. Oxidant stress responses in premature infants during exposure to hyperoxia. Pediatr. Res. 34:360-365.
24. Bett, A. J., W. Haddara, L. Prevec, and F. L. Graham. 1994. An efficient and flexible system for construction of adenovirus vectors with insertions or deletions in early regions 1 and 3. Proc. Natl. Acad. Sci. USA 91:8802-8806.
25. Bergmeyer, H. U. 1974. Methods in Enzymatic Analysis. Academic Press, New York.
26. Tietze, F. 1969. Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal. Biochem. 27:502-522.
27. Bradford, 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.
28. Awasthi, S., A. Gyurasics, S. A. Knight, S. E. Welty, and C. V. Smith. 1998. Protein oxidation biomarkers in hyperoxic lung injury: effects of U-74389. Toxicol. Lett. 95:47-61.
29. Benzick, A. E., S. L. Reddy, S. Gupta, L. K. Rogers, and C. V. Smith. 1994. Diquat-and acetaminophen-induced alterations of biliary efflux of iron in rats. Biochem. Pharmacol. 47:2079-2085.
30. Stadtman, E. R., and B. S. Berlett. 1997. Reactive oxygen-mediated protein oxidation in aging and disease. Chem. Res. Toxicol. 10:485-494.
31. Balla, G., G. M. Vereellotti, J. W. Eaton, and H. S. Jacob. 1990. Iron loading of endothelial cells augments oxidant damage. J. Lab. Clin. Med. 116:546-554.
32. Dean, R. T., S. Fu, R. Stocker, and M. J. Davies. 1997. Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 324:1-18.
33. Park, Y., S. Kanekal, and J. P. Kehrer. 1991. Oxidative changes in hypoxic rat heart tissue. Am. J. Physiol. 260:111395-111405.
34. Gilbert, H. F. 1990. Molecular and cellular aspects of thiol-disulfide exchange. Adv. Enzymol. 63:69-172.
35. Rokutan, K., J. A. Thomas, and H. Sies. 1989. Specific S-thiolation of a 30-kDa cytosolic protein from rat liver under oxidative stress. FEBS 22:233-239.
36. Schuppe, I., P. Moldeus, and I. A. Cotgreave. 1992. Protein-specific S-thiolation in human endothelial cells during oxidative stress. Biochem. Pharmacol. 44:1757-1764.
37. Gupta, S., L. K. Rogers, and C. V. Smith. 1994. Biliary excretion of lysosomal enzymes, iron, and oxidized protein in Fischer-344 and Sprague-Dawley rats and the effects of diquat and acetaminophen. Toxicol. Appl. Pharmacol. 125:42-50.
38. Smith, C. V., D. P. Jones, T. M. Guenthner, L. H. Lash, and B. H. Lauterburg. 1996. Compartmentation of glutathione: implications for the study of toxicity and disease. Toxicol. Appl. Pharmacol. 140:1-12.
39. Palmeira, C. M., and K. B. Wallace. 1997. Benzoquinone inhibits the voltage-dependent induction of the mitochondrial permeability transition caused hy redox-cycling naphthoquinones. Toxicol. Appl. Pharmacol. 143: 338-347.
40. Costantini, P., B. V. Chernyak, V. Petronilli, and P. Bernardi. 1996. Modulation of the mitochondrial permeability transition pore by pyridine nucleotides and dithiol oxidation at two separate sites. J. Biol. Chem. 271:6746-6751.
41. Petronilli, V., P. Costantini, L. Scorrano, R. Colonna, S. Passamonti, and P. Bernardi. 1994. The voltage sensor of the mitochondrial permeability transition pore is tuned by the oxidation-reduction state of vicinal thiols: increase of the gating potential by oxidants and its reversal by reducing agents. J. Biol. Chem. 269:16638-16642.
42. Yang, J., X. Liu, K. Bhalla, C. N. Kim, A. M. Ibrado, J. Cai, T. I. Peng, D. P. Jones, and X. Wang. 1997. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science 275:1129-1132.
43. Nieminen, A. L., A. M. Byrne, B. Herman, and J. J. Lemasters. 1997. Mitochondrial permeability transition in hepatocytes induced by 1-BuOOH: NAD(P)H and reactive oxygen species. Am. J. Physiol. 272:C1286-C1294.
44. Lauterburg, B. H., C. V. Smith, H. Hughes, and J. R. Mitchell. 1984. Biliary excretion of glutathione and glutathione disulfide in the rat; regulation and response to oxidative stress. J. Clin. Invest. 73:124-133.
45. Olafsdottir, K., and D. J. Reed. 1988. Retention of oxidized glutathione by isolated rat liver mitochondria during hydroperoxide treatment. Biochem. Biophys. Acta 964:377-382.
46. Fernandez-Checa, J. C., N. Kaplowitz, C. Garcia-Ruiz, A. Colell, M. Miranda, M. Mari, E. Ardite, and A. Morales. 1997. GSH transport in mitochondria: defense against TNF-induced oxidative stress and alcohol-induced defect. Am. J. Physiol. 273:G7-G17.
47. Garcia-Ruiz, C., A. Colell, A. Morales, N. Kaplowitz, and J. C. Fernandez-Checa. 1995. Role of oxidative stress generated from the mitochondrial electron transport chain and mitochondrial glutathione status in loss of mitochondrial function and activation of transcription factor nuclear factor-kappa B: studies with isolated mitochondria and rat hepatocytes. Mol. Pharmacol. 48:825-834.
48. Hirano, T., N. Kaplowitz, H. Tsukamoto, S. Kamimura, and J. C. Fernandez-Checa. 1992. Hepatic mitochondrial glutathione depletion and progression of experimental alcoholic liver disease in rats. Hepatology 16:1423-1427.
49. Dong, J. Y., D. Wang, F. W. Van Ginkel, D. W. Pascual, and R. A. Frizzell. 1996. Systemic analysis of repeated gene delivery into animal lungs with recombinant adenovirus vector. Hum. Gene Ther. 7:329-333.
50. Flint, S. J. 1982. Expression of adenoviral genetic information in productively infected cells. Biochem. Biophys. Acta 651:175-208.