Enhanced γ-glutamyl transpeptidase expression and selective loss of CuZn superoxide dismutase in hepatic iron overload

Free Radical Biology and Medicine

Volumn 24, Issue 4, 1998, Pages 545-555

  Brown, Kyle E ^a   Kinter, Michael T ^b,c   Oberley, Terry D ^d   Freeman, Michael L ^e   Frierson, Henry F ^c   Ridnour, Lisa A ^f   Tao, Yan ^f   Oberley, Larry W ^f   Spitz, Douglas R ^g  

^a VETERANS AFFAIRS MEDICAL CENTER   (United States)

^b UNIVERSITY OF VIRGINIA   (United States)

^c UNIVERSITY OF VIRGINIA   (United States)

^d Lab Serv William S Middleton M   (United States)

^e VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^f UNIVERSITY OF IOWA   (United States)

^g WASHINGTON UNIVERSITY   (United States)

Author keywords

4 Hydroxynonenal; CuZn superoxide dismutase; Free radical; Glutathione; Hemochromatosis; Lipid peroxidation

Indexed keywords

4 HYDROXYNONENAL; COLLAGEN; COPPER ZINC SUPEROXIDE DISMUTASE; FREE RADICAL; GAMMA GLUTAMYLTRANSFERASE; GLUTATHIONE; GLUTATHIONE TRANSFERASE; MANGANESE SUPEROXIDE DISMUTASE; MESSENGER RNA;

ANIMAL TISSUE; ANTIOXIDANT ACTIVITY; ARTICLE; COLLAGEN SYNTHESIS; ENZYME ACTIVITY; IMMUNOBLOTTING; IMMUNOHISTOCHEMISTRY; IRON OVERLOAD; LIPID PEROXIDATION; LIVER FIBROSIS; MALE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; RAT;

ALDEHYDES; ANIMALS; CATALASE; GAMMA-GLUTAMYLTRANSFERASE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE; IMMUNOHISTOCHEMISTRY; IRON OVERLOAD; LIPID PEROXIDATION; LIVER DISEASES; MALE; RATS; RATS, SPRAGUE-DAWLEY; RNA, MESSENGER; SUPEROXIDE DISMUTASE;

ANIMALIA;

EID: 0032031941     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(97)00284-0     Document Type: Article

References (54)

1. Bacon B. R., Brown K. E. Iron metabolism and disorders of iron overload. Kaplowitz N. Liver and biliary diseases. 1996;349-362 Williams and Wilkins, Baltimore.
2. Feder J. N., Gnirke A., Tsuchihashi Z., Ruddy D. A., Basava A., Dormishian F., Domingo R., Ellis M. C., Fullan A., Hinton L. M., Jones N. L., Kimmel B. E., Kronmal G. S., Lauer P., Lee V. K., Loeb D. B., Mapa F. A., McClelland E., Meyer N. C., Mintier G. A., Moeller N., Moore T., Morikang E., Prass C. E., Quintana L., Starnes S. M., Schatzman R. C., Brunke K., Drayna D. T., Risch N. J., Bacon B. R., Wolff R. K. A novel MHC class I-like gene is mutated in patients with hereditary hemochromatosis. Nat. Genet. 13:1996;399-408.
3. Niederau C., Fischer R., Sonnenberg A., Stremmel W., Trampisch H. J., Strohmeyer G. Survival and causes of death in cirrhotic and noncirrhotic patients with primary hemochromatosis. N. Engl. J. Med. 313:1985;1256-1262.
4. Kilpe V. E., Krakauer H., Wren R. E. An analysis of liver transplant experience from 37 transplant centers as reported to Medicare. Transplantation. 56:1993;554-561.
5. Bacon B. R., Britton R. S. The pathology of iron overload a free radical-mediated process? Hepatology. 11:1990;127-137.
6. Park C., Bacon B. R., Brittenham G. M., Tavill A. S. Pathology of dietary carbonyl iron overload in rats. Lab. Invest. 57:1987;555-563.
7. Bacon B. R., Park C. H., Brittenham G. M., O'Neill R., Tavill A. S. Hepatic mitochondrial oxidative metabolism in rats with chronic dietary iron overload. Hepatology. 5:1985;789-797.
8. Bacon B. R., Healey J. F., Brittenham G. M., Park C. H., Nunnari J., Tavill A. S., Bonkovsky H. L. Hepatic microsomal metabolism in rats with chronic dietary iron overload. Gastroenterology. 90:1986;1844-1853.
9. Myers B. M., Prendergast F. G., Holman R., Kuntz S. M., LaRusso N. F. Alterations in the structure, physicochemical properties and pH of hepatocyte lysosomes in experimental iron overload. J. Clin. Invest. 88:1991;1207-1215.
10. Esterbauer H., Schaur R. J., Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic. Biol. Med. 11:1991;81-128.
11. Witz G. Biological interactions of α,β-unsaturated aldehydes. Free Radic. Biol. Med. 7:1989;333-349.
12. Hoff H. F., O'Neil J., Chisolm G. M., Cole T. B., Quehenberger O., Esterbauer H., Juergens G. Modification of low density lipoprotein with 4-hydroxynonenal induces uptake by macrophages. Arteriosclerosis. 9:1989;538-549.
13. Kamimura S., Gaal K., Britton R. S., Bacon B. R., Triadafilopoulos G., Tsukamoto H. Increased 4-hydroxynonenal levels in experimental alcoholic liver disease Association of lipid peroxidation with liver fibrosis . Hepatology. 16:1992;448-453.
14. Parola M., Pinzani M., Casini A., Albano E., Poli G., Gentilini A., Gentilini P., Dianzani M. U. Stimulation of lipid peroxidation or 4-hydroxynonenal treatment increases procollagen α1(I) gene expression in human liver fat storing cells. Biochem. Biophys. Res. Commun. 194:1993;1044-1050.
15. Friedman S. L. The cellular basis of hepatic fibrosis. N. Engl. J. Med. 328:1993;1828-1835.
16. Esterbauer H., Zollner H., Lang J. Metabolism of the lipid peroxidation product 4-hydroxynonenal by isolated hepatocytes and by liver cytosolic fractions. Biochem. J. 228:1985;363-373.
17. Grune T., Siems W. G., Schneider W. Accumulation of aldehydic lipid peroxidation products during postanoxic reoxygenation of isolated rat hepatocytes. Free Radic. Biol. Med. 15:1993;125-132.
18. Poli G., Dianzani M. U., Cheeseman K. H., Slater T. F., Lang J., Esterbauer H. Separation and characterization of the aldehydic products of lipid peroxidation stimulated by carbon tetrachloride or ADP-iron in isolated rat hepatocytes and rat liver microsomes. Biochem. J. 227:1985;629-638.
19. Lowry O., Rosebrough N., Farr A., Randall R. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193:1951;265-275.
20. Jamall I. S., Finelli V. N., Que Hee S. S. A simple method to determine nanogram levels of 4-hydroxyproline in biological tissues. Anal. Biochem. 112:1981;70-75.
21. Peters D. M., Ruwart M. J., Henley K. S. The measurement of hydroxyproline in rat liver (Abstract). Hepatology. 6:1986;782.
22. Kinter M., Sullivan S., Roberts R. J., Spitz D. R. Trace quantitation of 4-hydroxy-2-nonenal in biological samples as its oxime-bis-tert.-butyldimethylsilyl derivative using 3-hydroxynonanal as an internal standard. J. Chromatogr. Biomed. Appl. 578:1992;9-16.
23. Anderson M. Tissue glutathione. Greenwald R. Methods for oxygen radical research. 1985;317-323 CRC Press, Boca Raton.
24. Meister A., Tate S. S., Griffith O. W. γ-Glutamyl transpeptidase. Jackoby W. B. Methods in enzymology. 1981;237-253 Academic Press, New York.
25. Simons P., Vander Jagt D. Purification of glutathione S-transferases from human liver by glutathione-affinity chromatography. Anal. Biochem. 82:1977;334-341.
26. Spitz D. R., Oberley L. W. An assay for superoxide dismutase activity in mammalian tissue homogenates. Anal. Biochem. 179:1989;8-18.
27. 2 by catalase. J. Biol. Chem. 195:1952;133-140.
28. Aebi H. Catalase in vitro. Packer L. Methods in enzymology. 1984;121-126 Academic Press, New York.
29. Lawrence R., Burk R. Glutathione peroxidase activity in selenium-deficient rat liver. Biochem. Biophys. Res. Commun. 71:1976;952-958.
30. Oberley L. W., McCormick M. L., Sierra E., Kasemset-St. Clair D. Manganese superoxide dismutase in normal and transformed human embryonic lung fibroblasts. Free Radic. Biol. Med. 6:1989;379-384.
31. Hanigan M. H., Pitot H. C. Isolation of γ-glutamyl transpeptidase-positive hepatocytes during the early stages of hepatocarcinogenesis in the rat. Carcinogenesis. 3:1982;1349-1354.
32. Oberley T. D., Oberley L. W., Slattery A. F., Lauchner L. J., Elwell J. H. Immunohistochemical localization of antioxidant enzymes in adult Syrian hamster tissues and during kidney development. Am. J. Pathol. 137:1990;199-214.
33. Rutenburg A. M., Kim H., Fischbein J. W., Hanker J. S., Wasserkrug H. L., Seligman A. M. Histochemical and ultrastructural demonstration of γ-glutamyl transpeptidase activity. J. Histochem. Cytochem. 17:1969;517-526.
34. Sierra-Rivera E., Meredith M. J., Summar M. L., Smith M. D., Vorhees G. J., Stoffel C. M., Freeman M. L. Genes regulating glutathione concentrations in X-ray-transformed rat embryo fibroblasts Changes in γ-glutamylcysteine synthase and γ-glutamyl transpeptidase expression . Carcinogenesis. 15:1994;1301-1307.
35. Brown K. E., Poulos J. E., Li L., Soweid A. M., Ramm G. A., O'Neill R., Britton R. S., Bacon B. R. The effect of vitamin E supplementation on hepatic fibrogenesis in chronic dietary iron overload. Am. J. Physio. 272:1997;G116-G123.
36. Iancu T. C., Ward R. J., Peters T. J. Ultrastructural observations in the carbonyl iron-fed rat, an animal model for hemochromatosis. Virch. Arch. B Cell Pathol. 53:1987;208-217.
37. Grune T., Siems W., Kowalewski J., Zollner H., Esterbauer H. Identification of metabolic pathways of the lipid peroxidation product 4-hydroxynonenal by enterocytes of rat small intestine. Biochem. Int. 25:1991;963-971.
38. Ishikawa T., Esterbauer H., Sies H. Role of cardiac glutathione transferase and of the glutathione S-conjugate export system in biotranformation of 4-hydroxynonenal in the heart. J. Biol. Chem. 261:1986;1576-1581.
39. Spitz D. R., Sullivan S. J., Malcolm R. R., Roberts R. J. Glutathione-dependent metabolism and detoxification of 4-hydroxy-2-nonenal. Free Radic. Biol. Med. 11:1991;415-423.
40. Bilzer M., Krauth-Siege R. L., Schirmer R. H., Akerboom T. P., Sies H., Schulz G. E. Interaction of a glutathione S-conjugate with glutathione reductase. Eur. J. Biochem. 138:1984;373-378.
41. Meister A. On the cycles of glutathione metabolism and transport. Curr. Topics Cell. Regul. 18:1981;21-58.
42. Siems W. G., Grune T., Zollner H., Esterbauer H. Formation and metabolism of the lipid peroxidation product 4-hydroxynonenal in liver and small intestine. Poli G., Albano E., Dianzani M. Free radicals From basic science to medicine . 1993;89-101 Birkhaeuser Verlag, Basel.
43. Petras T., Siems W. G., Grune T. 4-Hydroxynonenal is degraded to mercapturic acid conjugate in rat kidney. Free Radic. Biol. Med. 19:1995;685-688.
44. Rajpert-De Meyts E.; Shi, M.; Chang M., Robinson T. W., Groffen J., Heisterkamp N., Forman H. J. Transfection with γ-glutamyl transpeptidase enhances recovery from glutathione depletion using extracellular glutathione. Toxicol. Appl. Pharmacol. 114:1992;56-62.
45. 2-induced injury by 2,3-dimethoxy-1,4-naphthoquinone. Free Radic. Biol. Med. 15:1993;57-67.
46. Deneke S. M., Fanburg B. L. Regulation of cellular glutathione. Am. J. Physiol. 257:1989;L163-L173.
47. Kugelman A., Choy H. A., Liu R., Shi M. M., Gozal E., Forman H. J. γ-Glutamyl transpeptidase is increased by oxidative stress in rat alveolar L2 epithelial cells. Am. J. Respir. Cell Mol. Biol. 11:1994;586-592.
48. Ogino T., Kawabata T., Awai M. Stimulation of glutathione synthesis in iron-loaded mice. Biochim. Biophys. Acta. 1006:1989;131-135.
49. Khan M. F., Srivastava S. K., Singhal S. S., Chaubey M., Awasthi S., Petersen D. R., Ansari G. A. S., Awasthi Y. C. Iron-induced lipid peroxidation in rat liver is accompanied by preferential induction of glutathione S-transferase 8-8 isozyme. Toxicol. Appl. Pharmacol. 131:1995;63-72.
50. Fletcher L. M., Roberts F. D., Irving M. G., Powell L. W., Halliday J. W. Effects of iron-loading on free radical scavenging enzymes and lipid peroxidation in rat liver. Gastroenterology. 97:1989;1011-1018.
51. Hodgson E. K., Fridovich I. The interaction of bovine erythrocyte superoxide dismutase with hydrogen peroxide Inactivation of the enzyme . Biochemistry. 14:1975;5294-5299.
52. Szweda L. I., Stadtman E. R. Iron-catalyzed oxidative modification of glucose-6-phosphate dehydrogenase from Leuconostoc mesenteroides: Structural and functional changes. J. Biol. Chem. 267:1992;3096-3100.
53. Szweda L. I., Uchida K., Tsai L., Stadtman E. R. Inactivation of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal Selective modification of an active-site lysine . J. Biol. Chem. 268:1993;3342-3347.
54. Grune T., Reinhecker T., Joshi M., Davies K. J. A. Proteolysis in cultured liver epithelial cells during oxidative stress. J. Biol. Chem. 270:1995;2344-2351.