Hyperoxia enhances expression of γ-glutamyl transpeptidase and increases protein S-glutathiolation in rat lung

American Journal of Physiology - Lung Cellular and Molecular Physiology

Volumn 270, Issue 1 14-1, 1996, Pages

  Knickelbein, Roy G ^a   Ingbar, David H ^b   Seres, Tamas ^b   Snow, Kris ^b   Johnston Jr , Richard B ^b   Fayemi, Olutoyin ^b   Gumkowski, Francine ^b   Jamieson, James D ^b   Warshaw, Joseph B ^b  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b NONE

Author keywords

disulfides; immunocytochemistry; messenger ribonucleic acid; oxidation reduction; glutamyl transferase

Indexed keywords

GAMMA GLUTAMYLTRANSFERASE; GLUCOSE 6 PHOSPHATE DEHYDROGENASE; GLUTATHIONE; MESSENGER RNA; PROTEIN S;

ANIMAL EXPERIMENT; ANIMAL MODEL; ANIMAL TISSUE; ARTICLE; CELL DAMAGE; ENZYME ACTIVITY; GENE EXPRESSION; GLUTATHIONE METABOLISM; HYPEROXIA; IMMUNOCYTOCHEMISTRY; NONHUMAN; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; RAT; RESPIRATORY DISTRESS SYNDROME;

EID: 0030058601     PISSN: 10400605     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajplung.1996.270.1.l115     Document Type: Article

References (37)

1. Anderson, M. E., and A. Meister. Transport and direct utilization of γ-glutamylcyst(e)ine for glutathione synthesis. Proc. Natl. Acad. Sci. USA 80: 707-711, 1983.
2. Baik, J. H., N. Chikhi, F. Bulle, G. Giuili, G. Guellaen, and S. Siegrist. Repetitive 5-azacytidine treatments of Fao cells induce a stable and strong expression of γ-glutamyl transpeptidase. J. Cell. Physiol. 153: 408-416, 1992.
3. Baik, J. H., S. Siegrist, G. Giuili, O. Lahuna, F. Bulle, and G. Guellaen. Tissue and developmental stage specific methylation in the two kidney promoters of the rat γ-glutamyl transpeptidase gene. Biochem. J. 287: 691-694, 1992.
4. Bilzer, M., and B. H. Lauterburg. Glutathione metabolism in activated human neutrophils: stimulation of glutathione synthesis and consumption of glutathione by reactive oxygen species. Eur. J. Clin. Invest. 21: 316-322, 1991.
5. Cameron, R., J. Kellen, A. Kolin, A. Malkin, and E. Farber. γ-Glutamyl transferase in putative premalignant liver cell populations during hepatocarcinogenesis. Cancer Res. 38: 823-829, 1978.
6. Castle, J. D., R. S. Cameron, P. L. Patterson, and A. K. Ma. Identification of high molecular weight antigens structurally related to gamma-glutamyl transferase in epithelial tissues. J. Membr. Biol. 87: 13-26, 1985.
7. Chirgwin, J. M., A. E. Przbyla, R. J. MacDonald, and W. J. Rutter. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18: 5294-5299, 1979.
8. Del Corso, A., M. Cappiello, and U. Mura. Thiol dependent oxidation of enzymes: the last chance against oxidative stress. Int. J. Biochem. 26: 745-750, 1994.
9. Deneke, S. M., and B. L. Fanburg. Regulation of cellular glutathione. Am. J. Physiol. 257 (Lung Cell. Mol. Physiol. 1): L163-L173, 1989.
10. Dickerson, J. E., Jr., and F. L. Marjorie. A new mixed disulfide species in human cataractous and aged lenses. Biochem. Biophys. Acta 1157: 141-146, 1993.
11. Dinsdale, D., J. A. Green, M. M. Manson, and M. J. Lee. The ultrastructural immunolocalization of γ-glutamyl transpeptidase in rat lung: correlation with the histochemical demonstration of enzyme activity. Histochem. J. 24: 144-152, 1992.
12. Forbush, B. Assay of Na,K-ATPase in plasma membrane preparations: increasing the permeability of membrane vesicles using sodium dodecyl sulfate buffered with bovine serum albumin. Anal. Biochem. 128: 159-163, 1983.
13. Forman, H. J., and D. C. Skelton. Protection of alveolar macrophages from hyperoxia by γ-glutamyl transpeptidase. Am. J. Physiol. 259 (Lung Cell. Mol. Physiol. 3): L102-L107, 1990.
14. Grisham, M. B., and J. M. McCord. Chemistry and cytotoxicity of reactive oxygen metabolites. In: Physiology of Oxygen Radicals. Bethesda, MD: Am. Physiol. Soc., 1986, p. 1-18.
15. Ingbar, D. H., K. Hepler, R. Dowin, E. Jacobsen, J. M. Dunitz, L. Nici, and J. D. Jamieson. γ-Glutamyl transpeptidase is a polarized alveolar epithelial membrane protein. Am. J. Physiol. 269 (Lung Cell. Mol. Physiol. 13): L261-L271, 1995.
16. Keeling, P. L., L. L. Smith, and W. N. Aldridge. The formation of mixed disulfides in rat lung following paraquat administration. Correlation with changes in intermediary metabolism. Biochem. Biophys. Acta 716: 249-257, 1982.
17. Kimura, R. E., G. E. Thulin, D. Wender, and J. B. Warshaw. Decreased oxidative metabolism in neonatal rat lung exposed to hyperoxia. J. Appl. Physiol. 55: 1501-1505, 1983.
18. Kugelman, A., H. A. Choy, R. Liu, M. M. Shi, E. Gozal, and H. J. Forman. γ-Glutamyl transpeptidase is increased by oxidative stress in rat alveolar L2 epithelial cells. Am. J. Respir. Cell Mol. Biol. 11: 586-592, 1994.
19. Kurauchi, O., O. Lahuna, M. Darbouy, M. Aggerbeck, M. N. Chobert, and Y. Laperche. Organization of the 5′ end of the rat γ-glutamyl transpeptidase gene: structure of a promoter active in the kidney. Biochemistry 30: 1618-1623, 1991.
20. Lauterburg, B. H., C. V. Smith, H. Hughes, and J. R. Mitchell. Biliary excretion of glutathione and glutathione disulfide in the rat. Regulation and response to oxidative stress. J. Clin. Invest. 73: 124-133, 1984.
21. Loeb, G. A., D. C. Skelton, and H. J. Forman. Dependence of mixed disulfide formation in alveolar macrophages upon production of oxidized glutathione; effect of selenium depletion. Biochem. Pharmacol. 38: 3119-3121, 1989.
22. Löhr, G. W., and H. D. Waller. Glucose-6-phosphate dehydrogenase. In: Methods of Enzymatic Analysis. New York: Academic, 1974, vol. 2, p. 636-643.
23. Martensson, J.,A. Jain, W. Frayer, and A. Meister. Glutathione metabolism in the lung: inhibition of its synthesis leads to lamellar body and mitochondrial defects Proc. Natl. Acad. Sci. USA 86: 5296-5300, 1989.
24. Meredith, M. J. Analysis of protein-glutathione mixed disulfides by high performance liquid chromatography. Anal. Biochem. 131: 504-509, 1983.
25. Murphy, M. E., and J. P. Kehrer. Oxidation state of tissue thiol groups and content of protein carbonyl groups in chickens with inherited muscular dystrophy. Biochem. J. 260: 359-364, 1989.
26. Nici, L., R. Dowin, M. Gilmore-Herbert, J. D. Jamieson, and D. H. Ingbar. Upregulation of rat lung Na-K-ATPase during hyperoxic injury. Am. J. Physiol. 261 (Lung Cell. Mol. Physiol. 5): L307-L314, 1991.
27. Northway, W. H., Jr. An introduction to bronchopulmonary dysplasia. Clin. Perinatol 19: 489-495, 1992.
28. Omar, B., J. McCord, and J. Downey. Ischaemia-reperfusion. In: Oxidative Stress: Oxidants and Antioxidants. London: Academic, 1991, p. 493-527.
29. +-ATPase expression. J. Clin. Invest. 87: 821-830, 1991.
30. Ravichandran, V., T. Seres, T. Moriguchi, J. A. Thomas, and R. B. Johnston, Jr. S-Thiolation of glyceraldehyde-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocartes. J. Biol. Chem. 236: 25010-25015, 1994.
31. Reed, D. J., J. R. Babson, P. W. Beatty, A. E. Brodie, W. W. Ellis, and D. W. Potter. High-performance liquid chromatography analysis of nanomole levels of glutathione, glutathione disulfide, and related thiols and disulfides. Anal. Biochem. 106: 55-62, 1980.
32. Rosalki, S. B., and R. Rau. Serum γ-glutamyl transpeptidase activity in alcoholism. Clin. Chim. Acta 39: 41-47, 1972.
33. Rushmore, T. H., M. R. Morton, and C. B. Pickett. The antioxidant responsive element. Activation by oxidative stress and identification of the DNA consensus sequence required for functional activity J. Biol. Chem. 266: 11632-11639, 1991.
34. Sies, H. Oxidative stress: from basic research to clinical application. Am. J. Med. 91: 31S-38S, 1991.
35. Smith, G. D., J. L. Ding, and T. J. Peters. A sensitive fluorimetric assay for γ-glutamyl transferase. Anal. Biochem. 100: 136-139, 1979.
36. Stein, H. J., M. M. J. Oosthuizen, R. A. Hinder, and H. Lamprechts. Oxygen free radicals and glutathione in hepatic ischemia/reperfusion injury. J. Surg. Res. 50: 398-402, 1991.
37. Warshaw, J. B., C. W. Wilson III, K. Saito, and R. A. Prough. The responses of glutathione and antioxidant enzymes to hyperoxia in developing lung. Pediatr. Res. 19: 819-823, 1985.