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Volumn 237, Issue 10, 2012, Pages 1163-1172

Oxidative stress contributes to liver damage in a murine model of alpha-1-antitrypsin deficiency

Author keywords

Alpha 1 antitrypsin deficiency; Gene array; Oxidative stress; PiZ mice; Redox regulation

Indexed keywords

CARBONYL REDUCTASE; CARBONYL REDUCTASE 3; GLUTATHIONE TRANSFERASE ALPHA; GLUTATHIONE TRANSFERASE M3; MALONALDEHYDE; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; 8 HYDROXYDEOXYGUANOSINE; ALPHA 1 ANTITRYPSIN; CYCLOSPORIN A;

EID: 84868262757     PISSN: 15353702     EISSN: 15353699     Source Type: Journal    
DOI: 10.1258/ebm.2012.012106     Document Type: Article
Times cited : (45)

References (47)
  • 1
    • 0024423930 scopus 로고
    • Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins
    • 8951-6896
    • Huber R, Carrell RW. Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins. Biochemistry 1989;28:8951-6896
    • (1989) Biochemistry , vol.28
    • Huber, R.1    Carrell, R.W.2
  • 2
    • 0029859978 scopus 로고    scopus 로고
    • Molecular pathogenesis of liver disease in alpha1-antitrypsin deficiency
    • Teckman JH, Qu D, Perlmutter DH. Molecular pathogenesis of liver disease in alpha1-antitrypsin deficiency. Hepatology 1996;24:1504-1516
    • (1996) Hepatology , vol.24 , pp. 1504-1516
    • Teckman, J.H.1    Qu, D.2    Perlmutter, D.H.3
  • 4
    • 24144496018 scopus 로고    scopus 로고
    • Alpha-1-antitrypsin deficiency: A new paradigm for hepatocellular carcinoma in genetic liver disease
    • Rudnick DA, Perlmutter DH. Alpha-1-antitrypsin deficiency: a new paradigm for hepatocellular carcinoma in genetic liver disease. Hepatology 2005;42:514-521
    • (2005) Hepatology , vol.42 , pp. 514-521
    • Rudnick, D.A.1    Perlmutter, D.H.2
  • 6
    • 1842532017 scopus 로고    scopus 로고
    • Analyses of hepatocellular proliferation in a mouse model of alpha-1-antitrypsin deficiency
    • Rudnick DA, Liao Y, An JK, Muglia LJ, Perlmutter DH, Teckman JH. Analyses of hepatocellular proliferation in a mouse model of alpha-1-antitrypsin deficiency. Hepatology 2004;39:1048-1055
    • (2004) Hepatology , vol.39 , pp. 1048-1055
    • Rudnick, D.A.1    Liao, Y.2    An, J.K.3    Muglia, L.J.4    Perlmutter, D.H.5    Teckman, J.H.6
  • 11
    • 28244499949 scopus 로고    scopus 로고
    • Accumulation of mutant alpha1-antitrypsin Z in the endoplasmic reticulum activates caspases-4 and -12, NFkappaB, and BAP31 but not the unfolded protein response
    • Hidvegi T, Schmidt BZ, Hale P, Perlmutter DH. Accumulation of mutant alpha1-antitrypsin Z in the endoplasmic reticulum activates caspases-4 and -12, NFkappaB, and BAP31 but not the unfolded protein response. J Biol Chem 2005;280:39002-39015
    • (2005) J Biol Chem , vol.280 , pp. 39002-39015
    • Hidvegi, T.1    Schmidt, B.Z.2    Hale, P.3    Perlmutter, D.H.4
  • 12
    • 34948871658 scopus 로고    scopus 로고
    • Regulator of G Signaling 16 is a marker for the distinct endoplasmic reticulum stress state associated with aggregated mutant alpha1-antitrypsin Z in the classical form of alpha1-antitrypsin deficiency
    • Hidvegi T, Mirnics K, Hale P, Ewing M, Beckett C, Perlmutter DH. Regulator of G Signaling 16 is a marker for the distinct endoplasmic reticulum stress state associated with aggregated mutant alpha1-antitrypsin Z in the classical form of alpha1-antitrypsin deficiency. J Biol Chem 2007;282:27769-27780
    • (2007) J Biol Chem , vol.282 , pp. 27769-27780
    • Hidvegi, T.1    Mirnics, K.2    Hale, P.3    Ewing, M.4    Beckett, C.5    Perlmutter, D.H.6
  • 13
    • 33845626484 scopus 로고    scopus 로고
    • Changes of endoplasmic reticulum chaperone complexes, redox state, and impaired protein disulfide reductase activity in misfolding alpha1-antitrypsin transgenic mice
    • Papp E, Szaraz P, Korcsmaros T, Csermely P. Changes of endoplasmic reticulum chaperone complexes, redox state, and impaired protein disulfide reductase activity in misfolding alpha1-antitrypsin transgenic mice. FASEB J 2006;20:1018-1020
    • (2006) FASEB J , vol.20 , pp. 1018-1020
    • Papp, E.1    Szaraz, P.2    Korcsmaros, T.3    Csermely, P.4
  • 16
  • 18
    • 0036351376 scopus 로고    scopus 로고
    • Role of alpha class glutathione S-transferases as antioxidant enzymes in rodent tissues
    • Yang Y, Sharma R, Zimniak P, Awasthi YC. Role of alpha class glutathione S-transferases as antioxidant enzymes in rodent tissues. Toxicol Appl Pharmacol 2002;182:105-115
    • (2002) Toxicol Appl Pharmacol , vol.182 , pp. 105-115
    • Yang, Y.1    Sharma, R.2    Zimniak, P.3    Awasthi, Y.C.4
  • 19
    • 0033828113 scopus 로고    scopus 로고
    • Glutathione S-transferase polymorphisms and their biological consequences
    • Hayes JD, Strange RC. Glutathione S-transferase polymorphisms and their biological consequences. Pharmacology 2000;61:154-166
    • (2000) Pharmacology , vol.61 , pp. 154-166
    • Hayes, J.D.1    Strange, R.C.2
  • 21
    • 33846945701 scopus 로고    scopus 로고
    • Carbonyl reductases: The complex relationships of mammalian carbonyl- and quinone-reducing enzymes and their role in physiology
    • Oppermann U. Carbonyl reductases: the complex relationships of mammalian carbonyl- and quinone-reducing enzymes and their role in physiology. Annu Rev Pharmacol Toxicol 2007;47:293-322
    • (2007) Annu Rev Pharmacol Toxicol , vol.47 , pp. 293-322
    • Oppermann, U.1
  • 22
    • 0037150281 scopus 로고    scopus 로고
    • Hepatotoxicity and aging: Endogenous antioxidant systems in hepatocytes from 2-, 6-,12-, 18- and 30-month-old rats following a necrogenic dose of thioacetamide
    • Sanz N, Diez-Fernandez C, Andres D, Cascales M. Hepatotoxicity and aging: endogenous antioxidant systems in hepatocytes from 2-, 6-,12-, 18- and 30-month-old rats following a necrogenic dose of thioacetamide. Bba-Mol Basis Dis 2002;1587:12-20
    • (2002) Bba-Mol Basis Dis , vol.1587 , pp. 12-20
    • Sanz, N.1    Diez-Fernandez, C.2    Andres, D.3    Cascales, M.4
  • 23
    • 24644463306 scopus 로고    scopus 로고
    • Enhanced anti-oxidant protection of liver membranes in long-lived rats fed on a coenzyme Q10-supplemented diet
    • Bello RI, Gomez-Diaz C, Buron MI, Alcain FJ, Navas P, Villalba JM. Enhanced anti-oxidant protection of liver membranes in long-lived rats fed on a coenzyme Q10-supplemented diet. Exp Gerontol 2005;40:694-706
    • (2005) Exp Gerontol , vol.40 , pp. 694-706
    • Bello, R.I.1    Gomez-Diaz, C.2    Buron, M.I.3    Alcain, F.J.4    Navas, P.5    Villalba, J.M.6
  • 26
    • 17844403545 scopus 로고    scopus 로고
    • Role of oxidative carbonylation in protein quality control and senescence
    • Nystrom T. Role of oxidative carbonylation in protein quality control and senescence. EMBO J 2005;24:1311-1317
    • (2005) EMBO J , vol.24 , pp. 1311-1317
    • Nystrom, T.1
  • 27
    • 26444588758 scopus 로고    scopus 로고
    • Nrf2 activation involves an oxidative-stress independent pathway in tetrafluoroethylcysteine-induced cytotoxicity
    • Ho HK, White CC, Fernandez C, Fausto N, Kavanagh TJ, Nelson SD, Bruschi SA. Nrf2 activation involves an oxidative-stress independent pathway in tetrafluoroethylcysteine-induced cytotoxicity. Toxicol Sci 2005;86:354-364
    • (2005) Toxicol Sci , vol.86 , pp. 354-364
    • Ho, H.K.1    White, C.C.2    Fernandez, C.3    Fausto, N.4    Kavanagh, T.J.5    Nelson, S.D.6    Bruschi, S.A.7
  • 28
    • 0016275313 scopus 로고
    • Glutathione S-transferases. The first enzymatic step in mercapturic acid formation
    • Habig WH, Pabst MJ, Jakoby WB. Glutathione S-transferases. The first enzymatic step in mercapturic acid formation. J Biol Chem 1974;249:7130-7139
    • (1974) J Biol Chem , vol.249 , pp. 7130-7139
    • Habig, W.H.1    Pabst, M.J.2    Jakoby, W.B.3
  • 29
    • 0028262418 scopus 로고
    • Colorimetric and fluorometric assays of glutathione transferase based on 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole
    • Ricci G, Caccuri AM, Lo Bello M, Pastore A, Piemonte F, Federici G. Colorimetric and fluorometric assays of glutathione transferase based on 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole. Anal Biochem 1994;218:463-465
    • (1994) Anal Biochem , vol.218 , pp. 463-465
    • Ricci, G.1    Caccuri, A.M.2    Lo, B.M.3    Pastore, A.4    Piemonte, F.5    Federici, G.6
  • 30
    • 0014481378 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Applications to mammalian blood and other tissues
    • Tietze F. Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal Biochem 1969;27:502-522
    • (1969) Anal Biochem , vol.27 , pp. 502-522
    • Tietze, F.1
  • 31
    • 0019167355 scopus 로고
    • Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine
    • Griffith OW. Determination of glutathione and glutathione disulfide using glutathione reductase and 2-vinylpyridine. Anal Biochem 1980;106:207-212
    • (1980) Anal Biochem , vol.106 , pp. 207-212
    • Griffith, O.W.1
  • 32
    • 3643113551 scopus 로고    scopus 로고
    • Reactions of 1-methyl-2-phenylindole with malondialdehyde and 4-hydroxyalkenals. Analytical applications to a colorimetric assay of lipid peroxidation
    • Gerard-Monnier D, Erdelmeier I, Regnard K, Moze-Henry N, Yadan JC, Chaudiere J. Reactions of 1-methyl-2-phenylindole with malondialdehyde and 4-hydroxyalkenals. Analytical applications to a colorimetric assay of lipid peroxidation. Chem Res Toxicol 1998;11:1176-1183
    • (1998) Chem Res Toxicol , vol.11 , pp. 1176-1183
    • Gerard-Monnier, D.1    Erdelmeier, I.2    Regnard, K.3    Moze-Henry, N.4    Yadan, J.C.5    Chaudiere, J.6
  • 33
    • 23944491356 scopus 로고    scopus 로고
    • Tissue, species, and environmental differences in absolute quantities of murine mRNAs coding for alpha, mu, omega, pi, and theta glutathione S-transferases
    • Ruiz-Laguna J, Abril N, Prieto-Alamo MJ, Lopez-Barea J, Pueyo C. Tissue, species, and environmental differences in absolute quantities of murine mRNAs coding for alpha, mu, omega, pi, and theta glutathione S-transferases. Gene Expr 2005;12:165-176
    • (2005) Gene Expr , vol.12 , pp. 165-176
    • Ruiz-Laguna, J.1    Abril, N.2    Prieto-Alamo, M.J.3    Lopez-Barea, J.4    Pueyo, C.5
  • 34
    • 0024337729 scopus 로고
    • Mouse hepatic glutathione transferase isoenzymes and their differential induction by anticarcinogens. Specificities of butylated hydroxyanisole and bisethylxanthogen as inducers of glutathione transferases in male and female CD-1 mice
    • Benson AM, Hunkeler MJ, York JL. Mouse hepatic glutathione transferase isoenzymes and their differential induction by anticarcinogens. Specificities of butylated hydroxyanisole and bisethylxanthogen as inducers of glutathione transferases in male and female CD-1 mice. Biochem J 1989;261:1023-1029
    • (1989) Biochem J , vol.261 , pp. 1023-1029
    • Benson, A.M.1    Hunkeler, M.J.2    York, J.L.3
  • 35
    • 0037106544 scopus 로고    scopus 로고
    • Cloning and expression of a novel Mu class murine glutathione transferase isoenzyme
    • Guo J, Zimniak L, Zimniak P, Orchard JL, Singh SV. Cloning and expression of a novel Mu class murine glutathione transferase isoenzyme. Biochem J 2002;366:817-824
    • (2002) Biochem J , vol.366 , pp. 817-824
    • Guo, J.1    Zimniak, L.2    Zimniak, P.3    Orchard, J.L.4    Singh, S.V.5
  • 36
    • 33644774644 scopus 로고    scopus 로고
    • Identification of the insulin signaling cascade in the regulation of alpha-class glutathione S-transferase expression in primary cultured rat hepatocytes
    • Kim SK, Abdelmegeed MA, Novak RF. Identification of the insulin signaling cascade in the regulation of alpha-class glutathione S-transferase expression in primary cultured rat hepatocytes. J Pharmacol Exp Ther 2006;316:1255-12561
    • (2006) J Pharmacol Exp Ther , vol.316 , pp. 1255-12561
    • Kim, S.K.1    Abdelmegeed, M.A.2    Novak, R.F.3
  • 37
    • 51249104026 scopus 로고    scopus 로고
    • Pro-oxidant shift in glutathione redox state during aging
    • Rebrin I, Sohal RS. Pro-oxidant shift in glutathione redox state during aging. Adv Drug Deliv Rev 2008;60:1545-1552
    • (2008) Adv Drug Deliv Rev , vol.60 , pp. 1545-1552
    • Rebrin, I.1    Sohal, R.S.2
  • 39
    • 78649747024 scopus 로고    scopus 로고
    • The melanoma-associated transmembrane glycoprotein Gpnmb controls trafficking of cellular debris for degradation and is essential for tissue repair
    • Li B, Castano AP, Hudson TE, Nowlin BT, Lin SL, Bonventre JV, Swanson KD, Duffield JS. The melanoma-associated transmembrane glycoprotein Gpnmb controls trafficking of cellular debris for degradation and is essential for tissue repair. Faseb Journal 2010;24:4767-4781
    • (2010) Faseb Journal , vol.24 , pp. 4767-4781
    • Li, B.1    Castano, A.P.2    Hudson, T.E.3    Nowlin, B.T.4    Lin, S.L.5    Bonventre, J.V.6    Swanson, K.D.7    Duffield, J.S.8
  • 40
    • 11244346111 scopus 로고    scopus 로고
    • Quantitative isolation of alphalAT mutant Z protein polymers from human and mouse livers and the effect of heat
    • An JK, Blomenkamp K, Lindblad D, Teckman JH. Quantitative isolation of alphalAT mutant Z protein polymers from human and mouse livers and the effect of heat. Hepatology 2005;41:160-167
    • (2005) Hepatology , vol.41 , pp. 160-167
    • An, J.K.1    Blomenkamp, K.2    Lindblad, D.3    Teckman, J.H.4
  • 41
    • 42149184731 scopus 로고    scopus 로고
    • Role of sulphated polysaccharides from Sargassum wightii in Cyclosporine A-induced oxidative liver injury in rats
    • Josephine A, Nithya K, Amudha G, Veena CK, Preetha SP, Varalakshmi P. Role of sulphated polysaccharides from Sargassum wightii in Cyclosporine A-induced oxidative liver injury in rats. BMC Pharmacol 2008;8:4
    • (2008) BMC Pharmacol , vol.8 , pp. 4
    • Josephine, A.1    Nithya, K.2    Amudha, G.3    Veena, C.K.4    Preetha, S.P.5    Varalakshmi, P.6
  • 42
    • 34547456557 scopus 로고    scopus 로고
    • Age-associated perturbations in glutathione synthesis in mouse liver
    • Toroser D, Sohal RS. Age-associated perturbations in glutathione synthesis in mouse liver. Biochem J 2007;405:583-589
    • (2007) Biochem J , vol.405 , pp. 583-589
    • Toroser, D.1    Sohal, R.S.2
  • 43
    • 77953798742 scopus 로고    scopus 로고
    • Energy restriction does not compensate for the reduced expression of hepatic drug-processing genes in mice with aging
    • Zhang YK, Saupe KW, Klaassen CD. Energy restriction does not compensate for the reduced expression of hepatic drug-processing genes in mice with aging. Drug Metab Dispos 2010;38:1122-1131
    • (2010) Drug Metab Dispos , vol.38 , pp. 1122-1131
    • Zhang, Y.K.1    Saupe, K.W.2    Klaassen, C.D.3
  • 44
    • 0037101768 scopus 로고    scopus 로고
    • Loss of the Nrf2 transcription factor causes a marked reduction in constitutive and inducible expression of the glutathione S-transferase Gsta1, Gsta2, Gstm1, Gstm2, Gstm3 and Gstm4 genes in the livers of male and female mice
    • Chanas SA, Jiang Q, McMahon M, McWalter GK, McLellan LI, Elcombe CR, Henderson CJ, Wolf CR, Moffat GJ, Itoh K, Yamamoto M, Hayes JD. Loss of the Nrf2 transcription factor causes a marked reduction in constitutive and inducible expression of the glutathione S-transferase Gsta1, Gsta2, Gstm1, Gstm2, Gstm3 and Gstm4 genes in the livers of male and female mice. Biochem J 2002;365:405-416
    • (2002) Biochem J , vol.365 , pp. 405-416
    • Chanas, S.A.1    Jiang, Q.2    McMahon, M.3    McWalter, G.K.4    McLellan, L.I.5    Elcombe, C.R.6    Henderson, C.J.7    Wolf, C.R.8    Moffat, G.J.9    Itoh, K.10    Yamamoto, M.11    Hayes, J.D.12
  • 45
    • 77957288996 scopus 로고    scopus 로고
    • Regulation of human carbonyl reductase 3 (CBR3; SDR21C2) expression by Nrf2 in cultured cancer cells
    • Ebert B, Kisiela M, Malatkova P, El-Hawari Y, Maser E. Regulation of human carbonyl reductase 3 (CBR3; SDR21C2) expression by Nrf2 in cultured cancer cells. Biochemistry 2010;49:8499-8511
    • (2010) Biochemistry , vol.49 , pp. 8499-8511
    • Ebert, B.1    Kisiela, M.2    Malatkova, P.3    El-Hawari, Y.4    Maser, E.5
  • 46
    • 77953012548 scopus 로고    scopus 로고
    • Stress-activated cap'n'collar transcription factors in aging and human disease
    • Sykiotis GP, Bohmann D. Stress-activated cap'n'collar transcription factors in aging and human disease. Sci Signal 2010;3:re3
    • (2010) Sci Signal , vol.3
    • Sykiotis, G.P.1    Bohmann, D.2


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