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Volumn 1830, Issue 5, 2013, Pages 3143-3153

Glutathione synthesis

Author keywords

Antioxidant response element; Glutamate cysteine ligase; GSH; GSH synthase; MafG; Nrf2

Indexed keywords

BUTHIONINE SULFOXIMINE; CURCUMIN; CYSTATHIONINE; CYSTEINE; EPIGALLOCATECHIN GALLATE; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; GLUTATHIONE DISULFIDE; GLUTATHIONE SYNTHASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; REACTIVE NITROGEN SPECIES; REACTIVE OXYGEN METABOLITE; S ADENOSYLMETHIONINE; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR MAF; TRANSCRIPTION FACTOR NRF2; TRANSFORMING GROWTH FACTOR BETA; URSODEOXYCHOLIC ACID;

EID: 84875744148     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2012.09.008     Document Type: Review
Times cited : (1571)

References (174)
  • 1
    • 0032421171 scopus 로고    scopus 로고
    • Role of the liver in interorgan homeostasis of glutathione and cyst(e)ine
    • M. Ookhtens, and N. Kaplowitz Role of the liver in interorgan homeostasis of glutathione and cyst(e)ine Semin. Liver Dis. 18 1998 313 329
    • (1998) Semin. Liver Dis. , vol.18 , pp. 313-329
    • Ookhtens, M.1    Kaplowitz, N.2
  • 3
    • 0019948316 scopus 로고
    • The relationship of biliary GSSG efflux and intracellular GSSG content in perfused rat liver
    • T.P.M. Akerboom, M. Bilizer, and H. Sies The relationship of biliary GSSG efflux and intracellular GSSG content in perfused rat liver J. Biol. Chem. 257 1982 4248 4252
    • (1982) J. Biol. Chem. , vol.257 , pp. 4248-4252
    • Akerboom, T.P.M.1    Bilizer, M.2    Sies, H.3
  • 4
  • 5
    • 65049087190 scopus 로고    scopus 로고
    • Glutathione: Overview of its protective roles, measurement, and biosynthesis
    • H.J. Forman, H. Zhang, and A. Rinna Glutathione: overview of its protective roles, measurement, and biosynthesis Mol. Aspects Med. 30 2009 1 12
    • (2009) Mol. Aspects Med. , vol.30 , pp. 1-12
    • Forman, H.J.1    Zhang, H.2    Rinna, A.3
  • 6
    • 0020478933 scopus 로고
    • Status of the mitochondrial pool of glutathione in the isolated hepatocyte
    • M.J. Meredith, and D.J. Reed Status of the mitochondrial pool of glutathione in the isolated hepatocyte J. Biol. Chem. 257 1982 3747 3753
    • (1982) J. Biol. Chem. , vol.257 , pp. 3747-3753
    • Meredith, M.J.1    Reed, D.J.2
  • 7
    • 0026698060 scopus 로고
    • Oxidized redox state of glutathione in the endoplasmic reticulum
    • C. Hwang, A.J. Sinsky, and H.F. Lodish Oxidized redox state of glutathione in the endoplasmic reticulum Science 257 1992 1496 1502
    • (1992) Science , vol.257 , pp. 1496-1502
    • Hwang, C.1    Sinsky, A.J.2    Lodish, H.F.3
  • 8
    • 65049085305 scopus 로고    scopus 로고
    • Glutathione in liver diseases and hepatotoxicity
    • L. Yuan, and N. Kaplowitz Glutathione in liver diseases and hepatotoxicity Mol. Aspects Med. 30 2009 29 41
    • (2009) Mol. Aspects Med. , vol.30 , pp. 29-41
    • Yuan, L.1    Kaplowitz, N.2
  • 10
    • 0021216714 scopus 로고
    • Hepatic glutathione homeostasis in the rat: Efflux accounts for glutathione turnover
    • B.H. Lauterburg, J.D. Adams, and J.R. Mitchell Hepatic glutathione homeostasis in the rat: efflux accounts for glutathione turnover Hepatology 4 1984 586 590
    • (1984) Hepatology , vol.4 , pp. 586-590
    • Lauterburg, B.H.1    Adams, J.D.2    Mitchell, J.R.3
  • 12
    • 0025312043 scopus 로고
    • Glutathione regulates activation-dependent DNA synthesis in highly purified normal human T lymphocytes stimulated via the CD2 and CD3 antigens
    • M. Suthanthiran, M.E. Anderson, V.K. Sharma, and A. Meister Glutathione regulates activation-dependent DNA synthesis in highly purified normal human T lymphocytes stimulated via the CD2 and CD3 antigens Proc. Natl. Acad. Sci. U. S. A. 87 1990 3343 3347
    • (1990) Proc. Natl. Acad. Sci. U. S. A. , vol.87 , pp. 3343-3347
    • Suthanthiran, M.1    Anderson, M.E.2    Sharma, V.K.3    Meister, A.4
  • 13
    • 65049089113 scopus 로고    scopus 로고
    • Regulation of glutathione synthesis
    • S.C. Lu Regulation of glutathione synthesis Mol. Aspects Med. 30 2009 42 59
    • (2009) Mol. Aspects Med. , vol.30 , pp. 42-59
    • Lu, S.C.1
  • 14
    • 65049087578 scopus 로고    scopus 로고
    • Role of nuclear glutathione as a key regulator of cell proliferation
    • F.V. Pallardó, J. Markovic, J.L. García, and J. Viña Role of nuclear glutathione as a key regulator of cell proliferation Mol. Aspects Med. 30 2009 77 85
    • (2009) Mol. Aspects Med. , vol.30 , pp. 77-85
    • Pallardó, F.V.1    Markovic, J.2    García, J.L.3    Viña, J.4
  • 15
    • 74149085153 scopus 로고    scopus 로고
    • Oxidative stress and glutathione in TGF-β-mediated fibrogenesis
    • R.M. Liu, and K.A. Gaston Pravia Oxidative stress and glutathione in TGF-β-mediated fibrogenesis Free Radic. Biol. Med. 2010 1 15
    • (2010) Free Radic. Biol. Med. , pp. 1-15
    • Liu, R.M.1    Gaston Pravia, K.A.2
  • 19
    • 0000311848 scopus 로고
    • Glutathione
    • I.M. Arias, W.B. Jakoby, H. Popper, D. Schachter, D.A. Shafritz, Second edition Raven Press New York
    • A. Meister Glutathione I.M. Arias, W.B. Jakoby, H. Popper, D. Schachter, D.A. Shafritz, The Liver: Biology and Pathobiology Second edition 1988 Raven Press New York 401 417
    • (1988) The Liver: Biology and Pathobiology , pp. 401-417
    • Meister, A.1
  • 20
    • 0022967677 scopus 로고
    • Elevation of intracellular glutathione content associated with mitogenic stimulation of quiescent fibroblasts
    • J.P. Shaw, and I. Chou Elevation of intracellular glutathione content associated with mitogenic stimulation of quiescent fibroblasts J. Cell. Physiol. 129 1986 193 198
    • (1986) J. Cell. Physiol. , vol.129 , pp. 193-198
    • Shaw, J.P.1    Chou, I.2
  • 21
    • 0024426194 scopus 로고
    • Cell cycle progression of glutathione-depleted human peripheral blood mononuclear cells is inhibited at S phase
    • J.P. Messina, and D.A. Lawrence Cell cycle progression of glutathione-depleted human peripheral blood mononuclear cells is inhibited at S phase J. Immunol. 143 1989 1974 1981
    • (1989) J. Immunol. , vol.143 , pp. 1974-1981
    • Messina, J.P.1    Lawrence, D.A.2
  • 22
    • 0024850422 scopus 로고
    • Lymphocyte proliferation in glutathione-depleted lymphocytes: Direct relationship between glutathione availability and the proliferative response
    • D.L. Hamilos, P. Zelarney, and J.J. Mascali Lymphocyte proliferation in glutathione-depleted lymphocytes: direct relationship between glutathione availability and the proliferative response Immunopharmacology 18 1989 223 235
    • (1989) Immunopharmacology , vol.18 , pp. 223-235
    • Hamilos, D.L.1    Zelarney, P.2    Mascali, J.J.3
  • 23
    • 0028318891 scopus 로고
    • Thiol-mediated redox regulation of lymphocyte proliferation. Possible involvement of adult T cell leukemia-derived factor and glutathione in transferrin receptor expression
    • S. Iwata, T. Hori, N. Sato, Y. Ueda-Taniguchi, T. Yamabe, H. Nakamura, H. Masutani, and J. Yodoi Thiol-mediated redox regulation of lymphocyte proliferation. Possible involvement of adult T cell leukemia-derived factor and glutathione in transferrin receptor expression J. Immunol. 152 1994 5633 5642
    • (1994) J. Immunol. , vol.152 , pp. 5633-5642
    • Iwata, S.1    Hori, T.2    Sato, N.3    Ueda-Taniguchi, Y.4    Yamabe, T.5    Nakamura, H.6    Masutani, H.7    Yodoi, J.8
  • 24
    • 0029004836 scopus 로고
    • De novo synthesis of glutathione is required for both entry into and progression through the cell cycle
    • M. Poot, H. Teubert, P.S. Rabinovitch, and T.J. Kavanagh De novo synthesis of glutathione is required for both entry into and progression through the cell cycle J. Cell. Physiol. 163 1995 555 560
    • (1995) J. Cell. Physiol. , vol.163 , pp. 555-560
    • Poot, M.1    Teubert, H.2    Rabinovitch, P.S.3    Kavanagh, T.J.4
  • 25
    • 0027052233 scopus 로고
    • Loss of suppression of GSH synthesis under low cell density in primary cultures of rat hepatocytes
    • S.C. Lu, and J. Ge Loss of suppression of GSH synthesis under low cell density in primary cultures of rat hepatocytes Am. J. Physiol. 263 1992 C1181 C1189
    • (1992) Am. J. Physiol. , vol.263
    • Lu, S.C.1    Ge, J.2
  • 26
    • 0035227318 scopus 로고    scopus 로고
    • Mechanism and significance of increased glutathione level in human hepatocellular carcinoma and liver regeneration
    • 10.1096/fj.00-0445fje
    • Z.Z. Huang, C.J. Chen, Z.H. Zeng, H.P. Yang, J. Oh, L.X. Chen, and S.C. Lu Mechanism and significance of increased glutathione level in human hepatocellular carcinoma and liver regeneration FASEB J. 2000 10.1096/fj.00-0445fje
    • (2000) FASEB J.
    • Huang, Z.Z.1    Chen, C.J.2    Zeng, Z.H.3    Yang, H.P.4    Oh, J.5    Chen, L.X.6    Lu, S.C.7
  • 27
    • 0031961850 scopus 로고    scopus 로고
    • Changes in glutathione homeostasis during liver regeneration in the rat
    • Z.Z. Huang, H. Li, J. Cai, J. Kuhlenkamp, N. Kaplowitz, and S.C. Lu Changes in glutathione homeostasis during liver regeneration in the rat Hepatology 27 1998 147 153
    • (1998) Hepatology , vol.27 , pp. 147-153
    • Huang, Z.Z.1    Li, H.2    Cai, J.3    Kuhlenkamp, J.4    Kaplowitz, N.5    Lu, S.C.6
  • 29
    • 36849069901 scopus 로고    scopus 로고
    • Effects of hepatocyte growth factor on glutathione synthesis, growth, and apoptosis is cell density-dependent
    • H.P. Yang, N. Magilnick, M. Xia, and S.C. Lu Effects of hepatocyte growth factor on glutathione synthesis, growth, and apoptosis is cell density-dependent Exp. Cell Res. 314 2008 398 412
    • (2008) Exp. Cell Res. , vol.314 , pp. 398-412
    • Yang, H.P.1    Magilnick, N.2    Xia, M.3    Lu, S.C.4
  • 30
    • 0019749063 scopus 로고
    • Regulation of ribonucleotide reductase
    • A. Holmgren Regulation of ribonucleotide reductase Curr. Top. Cell. Regul. 19 1981 47 76
    • (1981) Curr. Top. Cell. Regul. , vol.19 , pp. 47-76
    • Holmgren, A.1
  • 33
    • 22344438075 scopus 로고    scopus 로고
    • Dying a thousand deaths: Redundant pathways from different organelles to apoptosis and necrosis
    • J.J. Lemasters Dying a thousand deaths: redundant pathways from different organelles to apoptosis and necrosis Gastroenterology 129 2005 351 360
    • (2005) Gastroenterology , vol.129 , pp. 351-360
    • Lemasters, J.J.1
  • 34
    • 0033088957 scopus 로고    scopus 로고
    • The role of glutathione in the regulation of apoptosis
    • A.G. Hall The role of glutathione in the regulation of apoptosis Eur. J. Clin. Invest. 29 1999 238 245
    • (1999) Eur. J. Clin. Invest. , vol.29 , pp. 238-245
    • Hall, A.G.1
  • 35
    • 0036095124 scopus 로고    scopus 로고
    • Caspase-3-dependent cleavage of the glutamate-L-cysteine ligase catalytic subunit during apoptotic cell death
    • C.C. Franklin, C.M. Krejsa, R.H. Pierce, C.C. White, N. Fausto, and T.J. Kavanagh Caspase-3-dependent cleavage of the glutamate-L-cysteine ligase catalytic subunit during apoptotic cell death Am. J. Pathol. 160 2002 1887 1894
    • (2002) Am. J. Pathol. , vol.160 , pp. 1887-1894
    • Franklin, C.C.1    Krejsa, C.M.2    Pierce, R.H.3    White, C.C.4    Fausto, N.5    Kavanagh, T.J.6
  • 37
    • 0025091990 scopus 로고
    • Amino acid sequence of rat kidney g-glutamylcysteine synthetase
    • N. Yan, and A. Meister Amino acid sequence of rat kidney g-glutamylcysteine synthetase J. Biol. Chem. 265 1990 1588 1593
    • (1990) J. Biol. Chem. , vol.265 , pp. 1588-1593
    • Yan, N.1    Meister, A.2
  • 38
    • 0027227925 scopus 로고
    • Amino acid sequence and function of the light subunit of rat kidney γ-glutamylcysteine synthetase
    • C. Huang, M.E. Anderson, and A. Meister Amino acid sequence and function of the light subunit of rat kidney γ-glutamylcysteine synthetase J. Biol. Chem. 268 1993 20578 20583
    • (1993) J. Biol. Chem. , vol.268 , pp. 20578-20583
    • Huang, C.1    Anderson, M.E.2    Meister, A.3
  • 39
    • 0026689502 scopus 로고
    • Cloning and nucleotide sequence of a full-length cDNA for human liver γ-glutamylcysteine synthetase
    • J.J. Gipp, C. Chang, and R.T. Mulcahy Cloning and nucleotide sequence of a full-length cDNA for human liver γ-glutamylcysteine synthetase Biochem. Biophys. Res. Commun. 185 1992 29 35
    • (1992) Biochem. Biophys. Res. Commun. , vol.185 , pp. 29-35
    • Gipp, J.J.1    Chang, C.2    Mulcahy, R.T.3
  • 40
    • 0028959153 scopus 로고
    • Cloning and sequence of the cDNA for the light subunit of human liver γ-glutamylcysteine synthetase and relative mRNA levels for heavy and light subunits in human normal tissues
    • J.J. Gipp, H.H. Bailey, and R.T. Mulcahy Cloning and sequence of the cDNA for the light subunit of human liver γ-glutamylcysteine synthetase and relative mRNA levels for heavy and light subunits in human normal tissues Biochem. Biophys. Res. Commun. 206 1995 584 589
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 584-589
    • Gipp, J.J.1    Bailey, H.H.2    Mulcahy, R.T.3
  • 42
    • 0021149767 scopus 로고
    • Reversible dissociation of γ-glutamylcysteine synthetase into two subunits
    • G.F. Seelig, R.P. Simondsen, and A. Meister Reversible dissociation of γ-glutamylcysteine synthetase into two subunits J. Biol. Chem. 259 1984 9345 9347
    • (1984) J. Biol. Chem. , vol.259 , pp. 9345-9347
    • Seelig, G.F.1    Simondsen, R.P.2    Meister, A.3
  • 43
    • 0027171195 scopus 로고
    • Catalytic and regulatory properties of the heavy subunit of rat kidney γ-glutamylcysteine synthetase
    • C. Huang, L. Chang, M.E. Anderson, and A. Meister Catalytic and regulatory properties of the heavy subunit of rat kidney γ- glutamylcysteine synthetase J. Biol. Chem. 268 1993 19675 19680
    • (1993) J. Biol. Chem. , vol.268 , pp. 19675-19680
    • Huang, C.1    Chang, L.2    Anderson, M.E.3    Meister, A.4
  • 44
    • 0037147240 scopus 로고    scopus 로고
    • Initial characterization of the glutamate-cysteine ligase modifier subunit Gclm (-/-) knockout mouse: Novel model system for a severely compromised oxidative stress response
    • Y. Yang, M.Z. Dieter, Y. Chen, H.G. Shertzer, D.W. Nebert, and T.P. Dalton Initial characterization of the glutamate-cysteine ligase modifier subunit Gclm (-/-) knockout mouse: novel model system for a severely compromised oxidative stress response J. Biol. Chem. 277 2002 49446 49452
    • (2002) J. Biol. Chem. , vol.277 , pp. 49446-49452
    • Yang, Y.1    Dieter, M.Z.2    Chen, Y.3    Shertzer, H.G.4    Nebert, D.W.5    Dalton, T.P.6
  • 45
    • 65049090510 scopus 로고    scopus 로고
    • Structure, function, and post-translational regulation of the catalytic and modifier subunits of glutamate-cysteine ligase
    • C.C. Franklin, D.S. Backos, I. Mohar, C.C. White, H.J. Forman, and T.J. Kavanagh Structure, function, and post-translational regulation of the catalytic and modifier subunits of glutamate-cysteine ligase Mol. Aspects Med. 2009 86 98
    • (2009) Mol. Aspects Med. , pp. 86-98
    • Franklin, C.C.1    Backos, D.S.2    Mohar, I.3    White, C.C.4    Forman, H.J.5    Kavanagh, T.J.6
  • 46
    • 0016635533 scopus 로고
    • Regulation of γ-glutamylcysteine synthetase by nonallosteric feedback inhibition by glutathione
    • P.G. Richman, and A. Meister Regulation of γ-glutamylcysteine synthetase by nonallosteric feedback inhibition by glutathione J. Biol. Chem. 250 1975 1422 1426
    • (1975) J. Biol. Chem. , vol.250 , pp. 1422-1426
    • Richman, P.G.1    Meister, A.2
  • 47
    • 0022638764 scopus 로고
    • Role of membrane transport in metabolism and function of glutathione in mammals
    • S. Bannai, and N. Tateishi Role of membrane transport in metabolism and function of glutathione in mammals J. Membr. Biol. 89 1986 1 8
    • (1986) J. Membr. Biol. , vol.89 , pp. 1-8
    • Bannai, S.1    Tateishi, N.2
  • 48
    • 0018801016 scopus 로고
    • Glutathione synthetase. Purification from rat kidney and mapping of the substrate binding sites
    • L. Oppenheimer, V.P. Wellner, O.W. Griffith, and A. Meister Glutathione synthetase. Purification from rat kidney and mapping of the substrate binding sites J. Biol. Chem. 254 1979 5184 5190
    • (1979) J. Biol. Chem. , vol.254 , pp. 5184-5190
    • Oppenheimer, L.1    Wellner, V.P.2    Griffith, O.W.3    Meister, A.4
  • 49
    • 0030747207 scopus 로고    scopus 로고
    • Glutathione synthetase is dispensable for growth under both normal and oxidative stress conditions in the yeast Saccharomyces cerevisiae due to an accumulation of the dipeptide γ-glutamylcysteine
    • C.M. Grant, F.H. MacIver, and I.W. Dawes Glutathione synthetase is dispensable for growth under both normal and oxidative stress conditions in the yeast Saccharomyces cerevisiae due to an accumulation of the dipeptide γ-glutamylcysteine Mol. Biol. Cell 8 1997 1699 1707
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1699-1707
    • Grant, C.M.1    Maciver, F.H.2    Dawes, I.W.3
  • 50
    • 0031846919 scopus 로고    scopus 로고
    • Surgical trauma decreases glutathione synthetic capacity in human skeletal muscle tissue
    • J.L. Luo, F. Hammarqvist, K. Andersson, and J. Wernerman Surgical trauma decreases glutathione synthetic capacity in human skeletal muscle tissue Am. J. Physiol. 275 1998 E359 E365
    • (1998) Am. J. Physiol. , vol.275
    • Luo, J.L.1    Hammarqvist, F.2    Andersson, K.3    Wernerman, J.4
  • 51
    • 0034618471 scopus 로고    scopus 로고
    • Inducers of γ-glutamylcysteine synthetase and their effects on glutathione synthetase expression
    • Z.Z. Huang, H.P. Yang, C.J. Chen, Z.H. Zeng, and S.C. Lu Inducers of γ-glutamylcysteine synthetase and their effects on glutathione synthetase expression Biochim. Biophys. Acta 1493 2000 48 55
    • (2000) Biochim. Biophys. Acta , vol.1493 , pp. 48-55
    • Huang, Z.Z.1    Yang, H.P.2    Chen, C.J.3    Zeng, Z.H.4    Lu, S.C.5
  • 52
    • 0020325093 scopus 로고
    • Amino acid transport in isolated rat hepatocytes
    • M.S. Kilberg Amino acid transport in isolated rat hepatocytes J. Membr. Biol. 69 1982 1 12
    • (1982) J. Membr. Biol. , vol.69 , pp. 1-12
    • Kilberg, M.S.1
  • 53
    • 0021341544 scopus 로고
    • Transport of cystine in isolated rat hepatocytes in primary culture
    • A. Takada, and S. Bannai Transport of cystine in isolated rat hepatocytes in primary culture J. Biol. Chem. 259 1984 2441 2445
    • (1984) J. Biol. Chem. , vol.259 , pp. 2441-2445
    • Takada, A.1    Bannai, S.2
  • 54
    • 0008502328 scopus 로고
    • The conversion of methionine to cystine: Experiments with radioactive sulfur
    • H. Tarver, and C.L.A. Schmidt The conversion of methionine to cystine: experiments with radioactive sulfur J. Biol. Chem. 130 1939 67 80
    • (1939) J. Biol. Chem. , vol.130 , pp. 67-80
    • Tarver, H.1    Schmidt, C.L.A.2
  • 55
    • 84875705375 scopus 로고    scopus 로고
    • S-adenosylmethionine in liver health, injury and cancer
    • (in press)
    • S.C. Lu, J.M. Mato, S-adenosylmethionine in liver health, injury and cancer. Physiol. Rev. (in press).
    • Physiol. Rev.
    • Lu, S.C.1    Mato, J.M.2
  • 56
    • 0025362827 scopus 로고
    • Methionine metabolism in mammals
    • J.D. Finkelstein Methionine metabolism in mammals J. Nutr. Biochem. 1 1990 228 237
    • (1990) J. Nutr. Biochem. , vol.1 , pp. 228-237
    • Finkelstein, J.D.1
  • 57
    • 0028229212 scopus 로고
    • Up-regulation of γ-glutamylcysteine synthetase activity in melphalan-resistant human multiple myeloma cells expressing increased glutathione levels
    • R.T. Mulcahy, H.H. Bailey, and J.J. Gipp Up-regulation of γ-glutamylcysteine synthetase activity in melphalan-resistant human multiple myeloma cells expressing increased glutathione levels Cancer Chemother. Pharmacol. 34 1994 67 71
    • (1994) Cancer Chemother. Pharmacol. , vol.34 , pp. 67-71
    • Mulcahy, R.T.1    Bailey, H.H.2    Gipp, J.J.3
  • 58
    • 0028171395 scopus 로고
    • Transcriptional up-regulation of g-glutamylcysteine synthetase gene expression in melphalan-resistant human prostate carcinoma cells
    • R.T. Mulcahy, S. Untawale, and J.J. Gipp Transcriptional up-regulation of g-glutamylcysteine synthetase gene expression in melphalan-resistant human prostate carcinoma cells Mol. Pharmacol. 46 1994 909 914
    • (1994) Mol. Pharmacol. , vol.46 , pp. 909-914
    • Mulcahy, R.T.1    Untawale, S.2    Gipp, J.J.3
  • 59
    • 0028865359 scopus 로고
    • Transfection of complementary DNAs for the heavy and light subunits of human γ-glutamylcysteine synthetase results in an elevation of intracellular glutathione and resistance to melphalan
    • R.T. Mulcahy, H.H. Bailey, and J.J. Gipp Transfection of complementary DNAs for the heavy and light subunits of human γ-glutamylcysteine synthetase results in an elevation of intracellular glutathione and resistance to melphalan Cancer Res. 55 1995 4771 4775
    • (1995) Cancer Res. , vol.55 , pp. 4771-4775
    • Mulcahy, R.T.1    Bailey, H.H.2    Gipp, J.J.3
  • 60
    • 0026594392 scopus 로고
    • High resistance to cisplatin in human ovarian cancer cell lines is associated with marked increase of glutathione synthesis
    • A.K. Godwin, A. Meister, P.J. O'Dwyer, C.S. Huang, T.C. Hamilton, and M.E. Anderson High resistance to cisplatin in human ovarian cancer cell lines is associated with marked increase of glutathione synthesis Proc. Natl. Acad. Sci. U. S. A. 89 1992 3070 3074
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 3070-3074
    • Godwin, A.K.1    Meister, A.2    O'Dwyer, P.J.3    Huang, C.S.4    Hamilton, T.C.5    Anderson, M.E.6
  • 61
    • 0026703404 scopus 로고
    • Enhancement of γ-glutamylcysteine synthetase mRNA in rat kidney by methyl mercury
    • J.S. Woods, H.A. Davis, and R.P. Baer Enhancement of γ- glutamylcysteine synthetase mRNA in rat kidney by methyl mercury Arch. Biochem. Biophys. 296 1992 350 353
    • (1992) Arch. Biochem. Biophys. , vol.296 , pp. 350-353
    • Woods, J.S.1    Davis, H.A.2    Baer, R.P.3
  • 62
    • 0028075841 scopus 로고
    • Quinone-induced oxidative stress elevates glutathione and induces γ-glutamylcysteine synthetase activity in rat lung epithelial L2 cells
    • M.M. Shi, A. Kugelman, T. Iwamoto, L. Tian, and H.J. Forman Quinone-induced oxidative stress elevates glutathione and induces γ-glutamylcysteine synthetase activity in rat lung epithelial L2 cells J. Biol. Chem. 269 1994 26512 26517
    • (1994) J. Biol. Chem. , vol.269 , pp. 26512-26517
    • Shi, M.M.1    Kugelman, A.2    Iwamoto, T.3    Tian, L.4    Forman, H.J.5
  • 63
    • 0032553308 scopus 로고    scopus 로고
    • Expression of multidrug resistance protein/GS-X pump and γ-glutamylcysteine synthetase genes is regulated by oxidative stress
    • Y. Yamane, M. Furuichi, R. Song, N.T. Van, R.T. Mulcahy, T. Ishikawa, and M.T. Kuo Expression of multidrug resistance protein/GS-X pump and γ-glutamylcysteine synthetase genes is regulated by oxidative stress J. Biol. Chem. 273 1998 31075 31085
    • (1998) J. Biol. Chem. , vol.273 , pp. 31075-31085
    • Yamane, Y.1    Furuichi, M.2    Song, R.3    Van, N.T.4    Mulcahy, R.T.5    Ishikawa, T.6    Kuo, M.T.7
  • 64
    • 0026674198 scopus 로고
    • Insulin and glucocorticoid dependence of hepatic γ-glutamylcysteine synthetase and GSH synthesis in the rat: Studies in cultured hepatocytes and in vivo
    • S.C. Lu, J. Ge, J. Kuhlenkamp, and N. Kaplowitz Insulin and glucocorticoid dependence of hepatic γ-glutamylcysteine synthetase and GSH synthesis in the rat: studies in cultured hepatocytes and in vivo J. Clin. Invest. 90 1992 524 532
    • (1992) J. Clin. Invest. , vol.90 , pp. 524-532
    • Lu, S.C.1    Ge, J.2    Kuhlenkamp, J.3    Kaplowitz, N.4
  • 65
    • 0029127718 scopus 로고
    • Hormonal and cell density regulation of hepatic γ-glutamylcysteine synthetase gene expression
    • J. Cai, W.M. Sun, and S.C. Lu Hormonal and cell density regulation of hepatic γ-glutamylcysteine synthetase gene expression Mol. Pharmacol. 48 1995 212 218
    • (1995) Mol. Pharmacol. , vol.48 , pp. 212-218
    • Cai, J.1    Sun, W.M.2    Lu, S.C.3
  • 66
    • 0030884938 scopus 로고    scopus 로고
    • Differential regulation of γ-glutamylcysteine synthetase heavy and light subunit gene expression
    • J. Cai, Z.Z. Huang, and S.C. Lu Differential regulation of γ-glutamylcysteine synthetase heavy and light subunit gene expression Biochem. J. 326 1997 167 172
    • (1997) Biochem. J. , vol.326 , pp. 167-172
    • Cai, J.1    Huang, Z.Z.2    Lu, S.C.3
  • 67
    • 0028797103 scopus 로고
    • Weakened cellular scavenging activity against oxidative stress in diabetes mellitus: Regulation of glutathione synthesis and efflux
    • K. Yoshida, J. Hirokawa, S. Tagami, Y. Kawakami, Y. Urata, and T. Kondo Weakened cellular scavenging activity against oxidative stress in diabetes mellitus: regulation of glutathione synthesis and efflux Diabetologia 38 1995 201 210
    • (1995) Diabetologia , vol.38 , pp. 201-210
    • Yoshida, K.1    Hirokawa, J.2    Tagami, S.3    Kawakami, Y.4    Urata, Y.5    Kondo, T.6
  • 68
    • 4644276707 scopus 로고    scopus 로고
    • Insulin signaling regulates γ-glutamylcysteine ligase catalytic subunit expression in primary cultured rat hepatocytes
    • S.K. Kim, K.J. Woodcroft, S.S. Khodadadeh, and R.F. Novak Insulin signaling regulates γ-glutamylcysteine ligase catalytic subunit expression in primary cultured rat hepatocytes J. Pharmacol. Exp. Ther. 311 2004 99 108
    • (2004) J. Pharmacol. Exp. Ther. , vol.311 , pp. 99-108
    • Kim, S.K.1    Woodcroft, K.J.2    Khodadadeh, S.S.3    Novak, R.F.4
  • 69
    • 0042831502 scopus 로고    scopus 로고
    • Regulation of glutathione in cardiac myocytes
    • S. Li, X. Li, and G.J. Rozanski Regulation of glutathione in cardiac myocytes J. Mol. Cell. Cardiol. 35 2003 1145 1152
    • (2003) J. Mol. Cell. Cardiol. , vol.35 , pp. 1145-1152
    • Li, S.1    Li, X.2    Rozanski, G.J.3
  • 70
    • 56049102574 scopus 로고    scopus 로고
    • Insulin stimulation of γ-glutamylcysteine ligase catalytic subunit expression increases endothelial GSH during oxidative stress: Influence of low glucose
    • J.W. Langston, M.L. Circu, and T.Y. Aw Insulin stimulation of γ-glutamylcysteine ligase catalytic subunit expression increases endothelial GSH during oxidative stress: influence of low glucose Free Radic. Biol. Med. 45 2008 1591 1599
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 1591-1599
    • Langston, J.W.1    Circu, M.L.2    Aw, T.Y.3
  • 71
    • 0031280268 scopus 로고    scopus 로고
    • Transforming growth factor-beta1 is a potent inhibitor of glutathione synthesis in the lung epithelial cell line A549: Transcriptional effect on the GSH rate-limiting enzyme gamma- glutamylcysteine synthetase
    • K. Arsalane, C.M. Dubois, T. Muanza, R. Begin, F. Boudreau, C. Asselin, and A.M. Cantin Transforming growth factor-beta1 is a potent inhibitor of glutathione synthesis in the lung epithelial cell line A549: transcriptional effect on the GSH rate-limiting enzyme gamma- glutamylcysteine synthetase Am. J. Respir. Cell Mol. Biol. 17 1997 599 607
    • (1997) Am. J. Respir. Cell Mol. Biol. , vol.17 , pp. 599-607
    • Arsalane, K.1    Dubois, C.M.2    Muanza, T.3    Begin, R.4    Boudreau, F.5    Asselin, C.6    Cantin, A.M.7
  • 72
    • 0037077204 scopus 로고    scopus 로고
    • Molecular mechanism of transforming growth factor (TGF)-β2-induced glutathione depletion in alveolar epithelial cells
    • H. Jardine, W. MacNee, K. Donaldson, and I. Rahman Molecular mechanism of transforming growth factor (TGF)-β2-induced glutathione depletion in alveolar epithelial cells J. Biol. Chem. 277 2002 21158 21166
    • (2002) J. Biol. Chem. , vol.277 , pp. 21158-21166
    • Jardine, H.1    Macnee, W.2    Donaldson, K.3    Rahman, I.4
  • 73
    • 42449089421 scopus 로고    scopus 로고
    • Epigallocatechin-3-gallate inhibits growth of activated hepatic stellate cells by enhancing the capacity of glutathione synthesis
    • Y. Fu, Y.J. Zhou, S.C. Lu, and A.P. Chen Epigallocatechin-3-gallate inhibits growth of activated hepatic stellate cells by enhancing the capacity of glutathione synthesis Mol. Pharmacol. 73 2008 1465 1473
    • (2008) Mol. Pharmacol. , vol.73 , pp. 1465-1473
    • Fu, Y.1    Zhou, Y.J.2    Lu, S.C.3    Chen, A.P.4
  • 74
    • 0028181398 scopus 로고
    • Increase in γ-glutamylcysteine synthetase activity as a mechanism for butylated hydroxyanisole-mediated elevation of hepatic glutathione
    • D.L. Eaton, and D.M. Hamel Increase in γ-glutamylcysteine synthetase activity as a mechanism for butylated hydroxyanisole-mediated elevation of hepatic glutathione Toxicol. Appl. Pharmacol. 126 1994 145 149
    • (1994) Toxicol. Appl. Pharmacol. , vol.126 , pp. 145-149
    • Eaton, D.L.1    Hamel, D.M.2
  • 75
    • 0028181392 scopus 로고
    • Modulation of γ-glutamylcysteine synthetase large subunit mRNA expression by butylated hydroxianisole
    • K.I. Borroz, T.M. Buetler, and D.L. Eaton Modulation of γ-glutamylcysteine synthetase large subunit mRNA expression by butylated hydroxianisole Toxicol. Appl. Pharmacol. 126 1994 150 155
    • (1994) Toxicol. Appl. Pharmacol. , vol.126 , pp. 150-155
    • Borroz, K.I.1    Buetler, T.M.2    Eaton, D.L.3
  • 76
    • 0027945198 scopus 로고
    • Regulation of [Ah] gene battery enzymes and glutathione levels by 5,10-dihyroindeno[1,2-b]indole in mouse hepatoma cell lines
    • R.M. Liu, V. Vasiliou, H. Zhu, J.L. Duh, M.W. Tabor, A. Puga, D.W. Nebert, M. Sainsbury, and H.G. Shertzer Regulation of [Ah] gene battery enzymes and glutathione levels by 5,10-dihyroindeno[1,2-b]indole in mouse hepatoma cell lines Carcinogenesis 15 1994 2347 2352
    • (1994) Carcinogenesis , vol.15 , pp. 2347-2352
    • Liu, R.M.1    Vasiliou, V.2    Zhu, H.3    Duh, J.L.4    Tabor, M.W.5    Puga, A.6    Nebert, D.W.7    Sainsbury, M.8    Shertzer, H.G.9
  • 77
    • 0030075365 scopus 로고    scopus 로고
    • Differential enhancement of γ-glutamyl transpeptidase and γ-glutamylcysteine synthetase by tert-butylhydroquinone in rat lung epithelial L2 cells
    • R.M. Liu, H. Hu, T.W. Robison, and H.J. Forman Differential enhancement of γ-glutamyl transpeptidase and γ-glutamylcysteine synthetase by tert-butylhydroquinone in rat lung epithelial L2 cells Am. J. Respir. Cell Mol. Biol. 14 1996 186 191
    • (1996) Am. J. Respir. Cell Mol. Biol. , vol.14 , pp. 186-191
    • Liu, R.M.1    Hu, H.2    Robison, T.W.3    Forman, H.J.4
  • 78
    • 0030956247 scopus 로고    scopus 로고
    • Constitutive and β-naphthoflavone-induced expression of the human γ-glutamylcysteine synthetase heavy subunit gene is regulated by a distal antioxidant response element/TRE sequence
    • R.T. Mulcahy, M.A. Wartman, H.H. Bailey, and J.J. Gipp Constitutive and β-naphthoflavone-induced expression of the human γ-glutamylcysteine synthetase heavy subunit gene is regulated by a distal antioxidant response element/TRE sequence J. Biol. Chem. 272 1997 7445 7454
    • (1997) J. Biol. Chem. , vol.272 , pp. 7445-7454
    • Mulcahy, R.T.1    Wartman, M.A.2    Bailey, H.H.3    Gipp, J.J.4
  • 79
    • 0027170787 scopus 로고
    • γ-Glutamylcysteine synthetase and active transport of glutathione S-conjugate are responsive to heat shock in K562 erythroid cells
    • T. Kondo, K. Yoshida, Y. Urata, S. Goto, S. Gasa, and N. Taniguchi γ-Glutamylcysteine synthetase and active transport of glutathione S-conjugate are responsive to heat shock in K562 erythroid cells J. Biol. Chem. 268 1993 20366 20372
    • (1993) J. Biol. Chem. , vol.268 , pp. 20366-20372
    • Kondo, T.1    Yoshida, K.2    Urata, Y.3    Goto, S.4    Gasa, S.5    Taniguchi, N.6
  • 80
    • 33745667587 scopus 로고    scopus 로고
    • Increased glutathione synthesis through an ARE-Nrf2-dependent pathway by zinc in the RPE: Implication for protection against oxidative stress
    • K.N. Ha, Y. Chen, J. Cai, and P. Sternberg Jr. Increased glutathione synthesis through an ARE-Nrf2-dependent pathway by zinc in the RPE: implication for protection against oxidative stress Invest. Ophthalmol. Vis. Sci. 47 2006 2709 2715
    • (2006) Invest. Ophthalmol. Vis. Sci. , vol.47 , pp. 2709-2715
    • Ha, K.N.1    Chen, Y.2    Cai, J.3    Sternberg Jr., P.4
  • 81
    • 0032878234 scopus 로고    scopus 로고
    • Melatonin induces γ-glutamylcysteine synthetase mediated by activator protein-1 in human vascular endothelial cells
    • Y. Urata, S. Honma, S. Goto, S. Todoroki, T. Iida, S. Cho, K. Honma, and T. Kondo Melatonin induces γ-glutamylcysteine synthetase mediated by activator protein-1 in human vascular endothelial cells Free Radic. Biol. Med. 27 1999 838 847
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 838-847
    • Urata, Y.1    Honma, S.2    Goto, S.3    Todoroki, S.4    Iida, T.5    Cho, S.6    Honma, K.7    Kondo, T.8
  • 82
    • 34250858137 scopus 로고    scopus 로고
    • De novo synthesis of glutathione is a prerequisite for curcumin to inhibit hepatic stellate cell (HSC) activation
    • S. Zheng, F. Yumei, and A. Chen De novo synthesis of glutathione is a prerequisite for curcumin to inhibit hepatic stellate cell (HSC) activation Free Radic. Biol. Med. 43 2007 444 453
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 444-453
    • Zheng, S.1    Yumei, F.2    Chen, A.3
  • 83
    • 15744393896 scopus 로고    scopus 로고
    • Mechanisms of glutamate cysteine ligase (GCL) induction by 4-hydroxynonenal
    • K.E. Iles, and R.M. Liu Mechanisms of glutamate cysteine ligase (GCL) induction by 4-hydroxynonenal Free Radic. Biol. Med. 38 2005 547 556
    • (2005) Free Radic. Biol. Med. , vol.38 , pp. 547-556
    • Iles, K.E.1    Liu, R.M.2
  • 84
    • 33846849624 scopus 로고    scopus 로고
    • Submicromolar concentrations of 4-hydroxynonenal induce glutamate cysteine ligase expression in HBE1 cells
    • H. Zhang, N. Court, and H.J. Forman Submicromolar concentrations of 4-hydroxynonenal induce glutamate cysteine ligase expression in HBE1 cells Redox Rep. 12 2007 101 106
    • (2007) Redox Rep. , vol.12 , pp. 101-106
    • Zhang, H.1    Court, N.2    Forman, H.J.3
  • 85
    • 33744940306 scopus 로고    scopus 로고
    • Induction of adaptive response and enhancement of PC12 cell tolerance by 7-hydroxycholesterol and 15-deoxy-delta(12,14)-prostaglandin J2 through up-regulation of cellular glutathione via different mechanisms
    • Z.H. Chen, Y. Yoshida, Y. Saito, A. Sekine, N. Noguchi, and E. Niki Induction of adaptive response and enhancement of PC12 cell tolerance by 7-hydroxycholesterol and 15-deoxy-delta(12,14)-prostaglandin J2 through up-regulation of cellular glutathione via different mechanisms J. Biol. Chem. 281 2006 14440 14445
    • (2006) J. Biol. Chem. , vol.281 , pp. 14440-14445
    • Chen, Z.H.1    Yoshida, Y.2    Saito, Y.3    Sekine, A.4    Noguchi, N.5    Niki, E.6
  • 86
    • 8544277300 scopus 로고    scopus 로고
    • 15-Deoxy12,14-prostaglandin J2 protects against nitrosative neuronal PC12 cell death through up-regulation of intracellular glutathione synthesis
    • S.Y. Lim, J.H. Jang, S.C. Lu, I. Rahman, and Y.J. Surh 15-Deoxy12,14-prostaglandin J2 protects against nitrosative neuronal PC12 cell death through up-regulation of intracellular glutathione synthesis J. Biol. Chem. 279 2004 46263 46270
    • (2004) J. Biol. Chem. , vol.279 , pp. 46263-46270
    • Lim, S.Y.1    Jang, J.H.2    Lu, S.C.3    Rahman, I.4    Surh, Y.J.5
  • 87
    • 67349186705 scopus 로고    scopus 로고
    • Distinct Nrf1/2-independent mechanisms mediate As 3+-induced glutamate-cysteine ligase subunit gene expression in murine hepatocytes
    • J.A. Thompson, C.C. White, D.P. Cox, J.Y. Chan, T.J. Kavanagh, N. Fausto, and C.C. Franklin Distinct Nrf1/2-independent mechanisms mediate As 3+-induced glutamate-cysteine ligase subunit gene expression in murine hepatocytes Free Radic. Biol. Med. 46 2009 1614 1625
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 1614-1625
    • Thompson, J.A.1    White, C.C.2    Cox, D.P.3    Chan, J.Y.4    Kavanagh, T.J.5    Fausto, N.6    Franklin, C.C.7
  • 88
    • 77953751455 scopus 로고    scopus 로고
    • Ajoene, a stable garlic by-product, has an antioxidant effect through Nrf2-mediated glutamate-cysteine ligase induction in HepG2 cells and primary hepatocytes
    • H.Y. Kay, J. Won Yang, T.H. Kim, D.Y. Lee, B. Kang, J.H. Ryu, R. Jeon, and S.G. Kim Ajoene, a stable garlic by-product, has an antioxidant effect through Nrf2-mediated glutamate-cysteine ligase induction in HepG2 cells and primary hepatocytes J. Nutr. 140 2010 1211 1219
    • (2010) J. Nutr. , vol.140 , pp. 1211-1219
    • Kay, H.Y.1    Won Yang, J.2    Kim, T.H.3    Lee, D.Y.4    Kang, B.5    Ryu, J.H.6    Jeon, R.7    Kim, S.G.8
  • 89
    • 65649150412 scopus 로고    scopus 로고
    • Nitric oxide-mediated protection of endothelial cells from hydrogen peroxide is mediated by intracellular zinc and glutathione
    • M.M. Cortese-Krott, C.V. Suschek, W. Wetzel, K.D. Kröncke, and V. Kolb-Bachofen Nitric oxide-mediated protection of endothelial cells from hydrogen peroxide is mediated by intracellular zinc and glutathione Am. J. Physiol. Cell Physiol. 296 2009 C811 C820
    • (2009) Am. J. Physiol. Cell Physiol. , vol.296
    • Cortese-Krott, M.M.1    Suschek, C.V.2    Wetzel, W.3    Kröncke, K.D.4    Kolb-Bachofen, V.5
  • 90
    • 77950617143 scopus 로고    scopus 로고
    • Induction of avian musculoaponeurotic fibrosarcoma proteins by toxic bile acid inhibits expression of GSH synthetic enzymes and contributes to cholestatic liver injury in mice
    • H.P. Yang, K. Ko, M. Xia, T.W.H. Li, P. Oh, J. Li, and S.C. Lu Induction of avian musculoaponeurotic fibrosarcoma proteins by toxic bile acid inhibits expression of GSH synthetic enzymes and contributes to cholestatic liver injury in mice Hepatology 51 2010 1291 1301
    • (2010) Hepatology , vol.51 , pp. 1291-1301
    • Yang, H.P.1    Ko, K.2    Xia, M.3    Li, T.W.H.4    Oh, P.5    Li, J.6    Lu, S.C.7
  • 91
    • 0028914295 scopus 로고
    • Identification of a putative antioxidant response element in the 5′-flanking region of the human γ-glutamylcysteine synthetase heavy subunit gene
    • R.T. Mulcahy, and J.J. Gipp Identification of a putative antioxidant response element in the 5′-flanking region of the human γ-glutamylcysteine synthetase heavy subunit gene Biochem. Biophys. Res. Commun. 209 1995 227 233
    • (1995) Biochem. Biophys. Res. Commun. , vol.209 , pp. 227-233
    • Mulcahy, R.T.1    Gipp, J.J.2
  • 92
    • 0030670301 scopus 로고    scopus 로고
    • Regulation of human γ-glutamylcysteine synthetase: Co-ordinate induction of the catalytic and regulatory subunits in HepG2 cells
    • D.C. Galloway, D.G. Blake, A.G. Shepherd, and L.I. McLellan Regulation of human γ-glutamylcysteine synthetase: co-ordinate induction of the catalytic and regulatory subunits in HepG2 cells Biochem. J. 328 1997 99 104
    • (1997) Biochem. J. , vol.328 , pp. 99-104
    • Galloway, D.C.1    Blake, D.G.2    Shepherd, A.G.3    McLellan, L.I.4
  • 93
    • 2642671110 scopus 로고    scopus 로고
    • An electrophile responsive element (EpRE) regulates β-naphthoflavone induction of the human γ-glutamylcsteine synthetase regulatory subunit gene
    • H.R. Moinova, and R.T. Mulcahy An electrophile responsive element (EpRE) regulates β-naphthoflavone induction of the human γ-glutamylcsteine synthetase regulatory subunit gene J. Biol. Chem. 273 1998 14683 14689
    • (1998) J. Biol. Chem. , vol.273 , pp. 14683-14689
    • Moinova, H.R.1    Mulcahy, R.T.2
  • 94
    • 0034710173 scopus 로고    scopus 로고
    • Cloning and characterization of the proximal promoter region of the mouse glutamate-L-cysteine ligase regulatory subunit gene
    • F.N. Hudson, and T.J. Kavanagh Cloning and characterization of the proximal promoter region of the mouse glutamate-L-cysteine ligase regulatory subunit gene Biochim. Biophys. Acta 1492 2000 447 451
    • (2000) Biochim. Biophys. Acta , vol.1492 , pp. 447-451
    • Hudson, F.N.1    Kavanagh, T.J.2
  • 95
    • 0035879035 scopus 로고    scopus 로고
    • Cloning and characterization of the 5′-flanking region of the rat glutamate-cysteine ligase catalytic subunit
    • H.P. Yang, Z.Z. Huang, J.H. Wang, X.P. Ou, and S.C. Lu Cloning and characterization of the 5′-flanking region of the rat glutamate-cysteine ligase catalytic subunit Biochem. J. 357 2001 447 455
    • (2001) Biochem. J. , vol.357 , pp. 447-455
    • Yang, H.P.1    Huang, Z.Z.2    Wang, J.H.3    Ou, X.P.4    Lu, S.C.5
  • 97
    • 27444447043 scopus 로고    scopus 로고
    • Tumor necrosis alpha induces coordinated activation of rat GSH synthetic enzymes via NFκB and AP-1
    • H.P. Yang, N. Magilnick, X.P. Ou, and S.C. Lu Tumor necrosis alpha induces coordinated activation of rat GSH synthetic enzymes via NFκB and AP-1 Biochem. J. 391 2005 399 408
    • (2005) Biochem. J. , vol.391 , pp. 399-408
    • Yang, H.P.1    Magilnick, N.2    Ou, X.P.3    Lu, S.C.4
  • 98
    • 0030828703 scopus 로고    scopus 로고
    • Tumor necrosis factor increases hepatocellular glutathione by transcriptional regulation of the heavy subunit chain of γ- glutamylcysteine synthetase
    • A. Morales, C. García-Ruiz, M. Miranda, M. Marí, A. Colell, E. Ardite, and J.C. Fernández- Checa Tumor necrosis factor increases hepatocellular glutathione by transcriptional regulation of the heavy subunit chain of γ-glutamylcysteine synthetase J. Biol. Chem. 272 1997 30371 30379
    • (1997) J. Biol. Chem. , vol.272 , pp. 30371-30379
    • Morales, A.1    García-Ruiz, C.2    Miranda, M.3    Marí, M.4    Colell, A.5    Ardite, E.6    Fernández- Checa, J.C.7
  • 99
    • 0032079268 scopus 로고    scopus 로고
    • Transcriptional regulation of the heavy subunit chain of γ-glutamylcysteine synthetase by ionizing radiation
    • A. Morales, M. Miranda, A. Sanchez-Reyes, A. Colell, A. Biete, and J.C. Fernández-Checa Transcriptional regulation of the heavy subunit chain of γ-glutamylcysteine synthetase by ionizing radiation FEBS Lett. 427 1998 15 20
    • (1998) FEBS Lett. , vol.427 , pp. 15-20
    • Morales, A.1    Miranda, M.2    Sanchez-Reyes, A.3    Colell, A.4    Biete, A.5    Fernández-Checa, J.C.6
  • 100
    • 0030605012 scopus 로고    scopus 로고
    • Induction of γ-glutamylcysteine synthetase by cigarette smoke is associated with AP-1 in human alveolar epithelial cells
    • I. Rahman, C.A. Smith, M.F. Lawson, D.J. Harrison, and W. MacNee Induction of γ-glutamylcysteine synthetase by cigarette smoke is associated with AP-1 in human alveolar epithelial cells FEBS Lett. 396 1996 21 25
    • (1996) FEBS Lett. , vol.396 , pp. 21-25
    • Rahman, I.1    Smith, C.A.2    Lawson, M.F.3    Harrison, D.J.4    Macnee, W.5
  • 101
    • 0032079350 scopus 로고    scopus 로고
    • Characterization of γ-glutamylcysteine synthetase-heavy subunit promoter: A critical role for AP-1
    • C.A. Smith Rahman, F. Antonicelli, and W. MacNee Characterization of γ-glutamylcysteine synthetase-heavy subunit promoter: a critical role for AP-1 FEBS Lett. 427 1998 129 133
    • (1998) FEBS Lett. , vol.427 , pp. 129-133
    • Smith Rahman, C.A.1    Antonicelli, F.2    Macnee, W.3
  • 102
    • 0030973242 scopus 로고    scopus 로고
    • Alteration of transcriptional and post-transcriptional expression of gamma-glutamylcysteine synthetase by diethyl maleate
    • K.R. Sekhar, M. Long, J. Long, Z.Q. Xu, M.L. Summar, and M.L. Freeman Alteration of transcriptional and post-transcriptional expression of gamma-glutamylcysteine synthetase by diethyl maleate Radiat. Res. 147 1997 592 597
    • (1997) Radiat. Res. , vol.147 , pp. 592-597
    • Sekhar, K.R.1    Long, M.2    Long, J.3    Xu, Z.Q.4    Summar, M.L.5    Freeman, M.L.6
  • 104
    • 0033584867 scopus 로고    scopus 로고
    • Regulation of γ-glutamylcysteine synthetase subunit gene expression by the transcription factor Nrf2
    • A.C. Wild, H.R. Moinova, and R.T. Mulcahy Regulation of γ-glutamylcysteine synthetase subunit gene expression by the transcription factor Nrf2 J. Biol. Chem. 274 1999 33627 33636
    • (1999) J. Biol. Chem. , vol.274 , pp. 33627-33636
    • Wild, A.C.1    Moinova, H.R.2    Mulcahy, R.T.3
  • 105
    • 0037163092 scopus 로고    scopus 로고
    • Identification of a variant antioxidant response element in the promoter of the human glutamate-cysteine ligase modifier subunit gene
    • A.M. Erickson, Z. Nevarea, J.J. Gipp, and R.T. Mulcahy Identification of a variant antioxidant response element in the promoter of the human glutamate-cysteine ligase modifier subunit gene J. Biol. Chem. 277 2002 30730 30737
    • (2002) J. Biol. Chem. , vol.277 , pp. 30730-30737
    • Erickson, A.M.1    Nevarea, Z.2    Gipp, J.J.3    Mulcahy, R.T.4
  • 106
    • 80053583532 scopus 로고    scopus 로고
    • Activation of promoter activity of the catalytic subunit of γ-glutamylcysteine ligase (GCL) in brain endothelial cells by insulin requires antioxidant response element 4 and altered glycemic status: Implication for GCL expression and GSH synthesis
    • J.W. Langston, W. Li, L. Harrison, and T.Y. Aw Activation of promoter activity of the catalytic subunit of γ-glutamylcysteine ligase (GCL) in brain endothelial cells by insulin requires antioxidant response element 4 and altered glycemic status: implication for GCL expression and GSH synthesis Free Radic. Biol. Med. 51 2011 1749 1757
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 1749-1757
    • Langston, J.W.1    Li, W.2    Harrison, L.3    Aw, T.Y.4
  • 107
    • 0039726828 scopus 로고    scopus 로고
    • The CNC basic leucine zipper factor, Nrf1, is essential for cell survival in response to oxidative stress-inducing agents
    • M. Kwong, Y.W. Kan, and J.Y. Chan The CNC basic leucine zipper factor, Nrf1, is essential for cell survival in response to oxidative stress-inducing agents J. Biol. Chem. 274 1999 37491 37498
    • (1999) J. Biol. Chem. , vol.274 , pp. 37491-37498
    • Kwong, M.1    Kan, Y.W.2    Chan, J.Y.3
  • 108
    • 1942520367 scopus 로고    scopus 로고
    • Nrf2 signaling in coordinated activation of antioxidant gene expression. Review
    • A.K. Jaiswal Nrf2 signaling in coordinated activation of antioxidant gene expression. Review Free Radic. Biol. Med. 36 2004 1199 1207
    • (2004) Free Radic. Biol. Med. , vol.36 , pp. 1199-1207
    • Jaiswal, A.K.1
  • 109
    • 0034672595 scopus 로고    scopus 로고
    • Impaired expression of glutathione synthetic enzyme genes in mice with targeted deletion of the Nrf2 basic-leucine zipper protein
    • J.Y. Chan, and M. Kwong Impaired expression of glutathione synthetic enzyme genes in mice with targeted deletion of the Nrf2 basic-leucine zipper protein Biochim. Biophys. Acta 1517 2000 19 26
    • (2000) Biochim. Biophys. Acta , vol.1517 , pp. 19-26
    • Chan, J.Y.1    Kwong, M.2
  • 110
    • 33847050801 scopus 로고    scopus 로고
    • Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway
    • T.W. Kensler, N. Wakabayashi, and S. Biswal Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway Annu. Rev. Pharmacol. Toxicol. 47 2007 89 116
    • (2007) Annu. Rev. Pharmacol. Toxicol. , vol.47 , pp. 89-116
    • Kensler, T.W.1    Wakabayashi, N.2    Biswal, S.3
  • 111
    • 79955442831 scopus 로고    scopus 로고
    • KPNA6 (Importin α7)-mediated nuclear import of Keap1 represses the Nrf2-dependent antioxidant response
    • Z. Sun, T. Wu, F. Zhao, A. Lau, C.M. Birch, and D.D. Zhang KPNA6 (Importin α7)-mediated nuclear import of Keap1 represses the Nrf2-dependent antioxidant response Mol. Cell. Biol. 31 2011 1800 1811
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 1800-1811
    • Sun, Z.1    Wu, T.2    Zhao, F.3    Lau, A.4    Birch, C.M.5    Zhang, D.D.6
  • 112
    • 50849126791 scopus 로고    scopus 로고
    • Heterodimerization with small Maf proteins enhances nuclear retention of Nrf2 via masking the NESzip motif
    • W. Li, S. Yu, T. Liu, J.H. Kim, V. Blank, H. Li, and A.N.T. Kong Heterodimerization with small Maf proteins enhances nuclear retention of Nrf2 via masking the NESzip motif Biochim. Biophys. Acta 1783 2008 1847 1856
    • (2008) Biochim. Biophys. Acta , vol.1783 , pp. 1847-1856
    • Li, W.1    Yu, S.2    Liu, T.3    Kim, J.H.4    Blank, V.5    Li, H.6    Kong, A.N.T.7
  • 113
    • 33745807575 scopus 로고    scopus 로고
    • Nrf1 is targeted to the endoplasmic reticulum membrane by an N-terminal transmembrane domain
    • W. Wang, and J.Y. Chan Nrf1 is targeted to the endoplasmic reticulum membrane by an N-terminal transmembrane domain J. Biol. Chem. 281 2006 19676 19687
    • (2006) J. Biol. Chem. , vol.281 , pp. 19676-19687
    • Wang, W.1    Chan, J.Y.2
  • 114
    • 0038382987 scopus 로고    scopus 로고
    • Nrf1 is critical for redox balance and survival of liver cells during development
    • L. Chen, M. Kwong, R. Lu, D. Ginzinger, C. Lee, L. Leung, and J.Y. Chan Nrf1 is critical for redox balance and survival of liver cells during development Mol. Cell. Biol. 23 2003 4673 4686
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 4673-4686
    • Chen, L.1    Kwong, M.2    Lu, R.3    Ginzinger, D.4    Lee, C.5    Leung, L.6    Chan, J.Y.7
  • 115
    • 0035836698 scopus 로고    scopus 로고
    • An important function of Nrf2 in combating oxidative stress: Detoxification of acetaminophen
    • K. Chan, X.D. Han, and Y.W. Kan An important function of Nrf2 in combating oxidative stress: detoxification of acetaminophen Proc. Natl. Acad. Sci. U. S. A. 98 2001 4611 4616
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 4611-4616
    • Chan, K.1    Han, X.D.2    Kan, Y.W.3
  • 116
    • 0035951489 scopus 로고    scopus 로고
    • TCF11/Nrf1 overexpression increases the intracellular glutathione level and can transactivate the gamma-glutamylcysteine synthetase (GCS) heavy subunit promoter
    • M.C.W. Myhrstad, C. Husberg, P. Murphy, O. Nordström, R. Blomhoff, J. Moskaug, and A.B. Kolstø TCF11/Nrf1 overexpression increases the intracellular glutathione level and can transactivate the gamma-glutamylcysteine synthetase (GCS) heavy subunit promoter Biochim. Biophys. Acta 1517 2001 212 219
    • (2001) Biochim. Biophys. Acta , vol.1517 , pp. 212-219
    • Myhrstad, M.C.W.1    Husberg, C.2    Murphy, P.3    Nordström, O.4    Blomhoff, R.5    Moskaug, J.6    Kolstø, A.B.7
  • 117
    • 67749090960 scopus 로고    scopus 로고
    • Identification and characterization of a Nrf2-mediated ARE upstream of the rat glutamate cysteine ligase catalytic subunit gene
    • M. Li, J.F. Chiu, A. Kelsen, S.C. Lu, and N.K. Fukagawa Identification and characterization of a Nrf2-mediated ARE upstream of the rat glutamate cysteine ligase catalytic subunit gene J. Cell. Biochem. 107 2009 944 954
    • (2009) J. Cell. Biochem. , vol.107 , pp. 944-954
    • Li, M.1    Chiu, J.F.2    Kelsen, A.3    Lu, S.C.4    Fukagawa, N.K.5
  • 118
    • 21944452087 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 regulate rat glutamate-cysteine ligase catalytic subunit transcription indirectly via AP-1 and NFκB
    • H.P. Yang, N. Magilnick, C. Lee, D. Kalmaz, X.P. Ou, J.Y. Chan, and S.C. Lu Nrf1 and Nrf2 regulate rat glutamate-cysteine ligase catalytic subunit transcription indirectly via AP-1 and NFκB Mol. Cell. Biol. 25 2005 5933 5946
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 5933-5946
    • Yang, H.P.1    Magilnick, N.2    Lee, C.3    Kalmaz, D.4    Ou, X.P.5    Chan, J.Y.6    Lu, S.C.7
  • 119
  • 121
    • 84855421010 scopus 로고    scopus 로고
    • The anthocyanin cyanidin-3-O-β-glucoside, a flavonoid, increases hepatic glutathione synthesis and protects hepatocytes against reactive oxygen species during hyperglycemia: Involvement of a cAMP-PKA-dependent signaling pathway
    • W. Zhu, Q. Jia, Y. Wang, Y. Zhang, and M. Xia The anthocyanin cyanidin-3-O-β-glucoside, a flavonoid, increases hepatic glutathione synthesis and protects hepatocytes against reactive oxygen species during hyperglycemia: Involvement of a cAMP-PKA-dependent signaling pathway Free Radic. Biol. Med. 52 2012 314 327
    • (2012) Free Radic. Biol. Med. , vol.52 , pp. 314-327
    • Zhu, W.1    Jia, Q.2    Wang, Y.3    Zhang, Y.4    Xia, M.5
  • 122
    • 0031735363 scopus 로고    scopus 로고
    • γ-Glutamylcysteine synthetase: MRNA stabilization and independent subunit transcription by 4-hydroxy-2-nonenal
    • R.M. Liu, L. Gao, J. Choi, and H.J. Forman γ-Glutamylcysteine synthetase: mRNA stabilization and independent subunit transcription by 4-hydroxy-2-nonenal Am. J. Physiol. 275 1998 L861 L869
    • (1998) Am. J. Physiol. , vol.275
    • Liu, R.M.1    Gao, L.2    Choi, J.3    Forman, H.J.4
  • 123
    • 0025738538 scopus 로고
    • Hormone-mediated down-regulation of hepatic GSH synthesis in the rat
    • S.C. Lu, J. Kuhlenkamp, C. Garcia-Ruiz, and N. Kaplowitz Hormone-mediated down-regulation of hepatic GSH synthesis in the rat J. Clin. Invest. 88 1991 260 269
    • (1991) J. Clin. Invest. , vol.88 , pp. 260-269
    • Lu, S.C.1    Kuhlenkamp, J.2    Garcia-Ruiz, C.3    Kaplowitz, N.4
  • 124
    • 0024203875 scopus 로고
    • α-Adrenergic modulation of glutathione metabolism in isolated rat hepatocytes
    • J.M. Estrela, F. Gil, J.M. Vila, and J. Vina α-Adrenergic modulation of glutathione metabolism in isolated rat hepatocytes Am. J. Physiol. 255 1988 E801 E805
    • (1988) Am. J. Physiol. , vol.255
    • Estrela, J.M.1    Gil, F.2    Vila, J.M.3    Vina, J.4
  • 126
    • 0026069813 scopus 로고
    • Effects of vasopressor hormones and modulators of protein kinase C on glutathione efflux from perfused rat liver
    • D.S. Raiford, A.M. Sciuto, and M.C. Mitchell Effects of vasopressor hormones and modulators of protein kinase C on glutathione efflux from perfused rat liver Am. J. Physiol. 24 1991 G578 G584
    • (1991) Am. J. Physiol. , vol.24
    • Raiford, D.S.1    Sciuto, A.M.2    Mitchell, M.C.3
  • 127
    • 0025203434 scopus 로고
    • On the metallothionein, glutathione and cysteine relationship in rat liver
    • J. Hidalgo, J.S. Garvey, and A. Armario On the metallothionein, glutathione and cysteine relationship in rat liver J. Pharmacol. Exp. Ther. 255 1990 554 564
    • (1990) J. Pharmacol. Exp. Ther. , vol.255 , pp. 554-564
    • Hidalgo, J.1    Garvey, J.S.2    Armario, A.3
  • 128
    • 0029848066 scopus 로고    scopus 로고
    • Regulation of γ-glutamylcysteine synthetase by protein phosphorylation
    • W.M. Sun, Z.Z. Huang, and S.C. Lu Regulation of γ-glutamylcysteine synthetase by protein phosphorylation Biochem. J. 320 1996 321 328
    • (1996) Biochem. J. , vol.320 , pp. 321-328
    • Sun, W.M.1    Huang, Z.Z.2    Lu, S.C.3
  • 129
    • 0020036267 scopus 로고
    • Toxic doses of acetaminophen suppress hepatic glutathione synthesis in rats
    • B.H. Lauterburg, and J.R. Mitchell Toxic doses of acetaminophen suppress hepatic glutathione synthesis in rats Hepatology 2 1982 8 12
    • (1982) Hepatology , vol.2 , pp. 8-12
    • Lauterburg, B.H.1    Mitchell, J.R.2
  • 130
    • 85061109401 scopus 로고    scopus 로고
    • TGFβ1-induced suppression of glutathione antioxidant defenses in hepatocytes: Caspase-dependent posttranslational and caspase-independent transcriptional regulatory mechanisms
    • 10.1096/fj.02-0867fje
    • C.C. Franklin, M.E. Rosenfled-Franklin, C. White, T.J. Kavanagh, and N. Fausto TGFβ1-induced suppression of glutathione antioxidant defenses in hepatocytes: caspase-dependent posttranslational and caspase-independent transcriptional regulatory mechanisms FASEB J. 2003 10.1096/fj.02-0867fje
    • (2003) FASEB J.
    • Franklin, C.C.1    Rosenfled-Franklin, M.E.2    White, C.3    Kavanagh, T.J.4    Fausto, N.5
  • 131
    • 40449086667 scopus 로고    scopus 로고
    • Rapid detection, discovery, and identification of posttranslationally myristoylated proteins during apoptosis using a bio-orthogonal azidomyristate analog
    • D.D. Martin, G.L. Vilas, J.A. Prescher, G. Rajaiah, J.R. Falck, C.R. Bertozzi, and L.G. Berthiaume Rapid detection, discovery, and identification of posttranslationally myristoylated proteins during apoptosis using a bio-orthogonal azidomyristate analog FASEB J. 22 2008 797 806
    • (2008) FASEB J. , vol.22 , pp. 797-806
    • Martin, D.D.1    Vilas, G.L.2    Prescher, J.A.3    Rajaiah, G.4    Falck, J.R.5    Bertozzi, C.R.6    Berthiaume, L.G.7
  • 132
    • 78650692177 scopus 로고    scopus 로고
    • Posttranslational modification and regulation of glutamate-cysteine ligase by the α, β-unsaturated aldehyde 4-hydroxy-2-nonenal
    • D.S. Backos, K.S. Fritz, J.R. Roede, D.R. Petersen, and C.C. Franklin Posttranslational modification and regulation of glutamate-cysteine ligase by the α, β-unsaturated aldehyde 4-hydroxy-2-nonenal Free Radic. Biol. Med. 50 2011 14 26
    • (2011) Free Radic. Biol. Med. , vol.50 , pp. 14-26
    • Backos, D.S.1    Fritz, K.S.2    Roede, J.R.3    Petersen, D.R.4    Franklin, C.C.5
  • 133
    • 0032535320 scopus 로고    scopus 로고
    • Inducible expression of the γ-glutamylcysteine synthetase light subunit by t-butylhydroquinone in HepG2 cells is not dependent on an antioxidant-responsive element
    • D.C. Galloway, and L.I. McLellan Inducible expression of the γ-glutamylcysteine synthetase light subunit by t-butylhydroquinone in HepG2 cells is not dependent on an antioxidant-responsive element Biochem. J. 336 1998 535 539
    • (1998) Biochem. J. , vol.336 , pp. 535-539
    • Galloway, D.C.1    McLellan, L.I.2
  • 134
    • 0033546686 scopus 로고    scopus 로고
    • Up-regulation of the human γ-glutamylcysteine synthetase regulatory subunit gene involves binding of Nrf-2 to an electrophile responsive element
    • H.R. Moinova, and R.T. Mulcahy Up-regulation of the human γ-glutamylcysteine synthetase regulatory subunit gene involves binding of Nrf-2 to an electrophile responsive element Biochem. Biophys. Res. Commun. 261 1999 661 668
    • (1999) Biochem. Biophys. Res. Commun. , vol.261 , pp. 661-668
    • Moinova, H.R.1    Mulcahy, R.T.2
  • 135
    • 0033063222 scopus 로고    scopus 로고
    • Effect of ethanol and high fat feeding on hepatic γ-glutamate- cysteine ligase subunit expression in the rat
    • S.C. Lu, Z.Z. Huang, J. Yang, and H. Tsukamoto Effect of ethanol and high fat feeding on hepatic γ-glutamate-cysteine ligase subunit expression in the rat Hepatology 30 1999 209 214
    • (1999) Hepatology , vol.30 , pp. 209-214
    • Lu, S.C.1    Huang, Z.Z.2    Yang, J.3    Tsukamoto, H.4
  • 136
    • 68949114163 scopus 로고    scopus 로고
    • Dysregulation of glutathione synthesis during cholestasis in mice: Molecular mechanisms and therapeutic implications
    • H.P. Yang, K. Ramani, M. Xia, K.S. Ko, T.W.H. Li, P. Oh, J. Li, and S.C. Lu Dysregulation of glutathione synthesis during cholestasis in mice: molecular mechanisms and therapeutic implications Hepatology 49 2009 1982 1991
    • (2009) Hepatology , vol.49 , pp. 1982-1991
    • Yang, H.P.1    Ramani, K.2    Xia, M.3    Ko, K.S.4    Li, T.W.H.5    Oh, P.6    Li, J.7    Lu, S.C.8
  • 139
    • 0034603123 scopus 로고    scopus 로고
    • Molecular emchanism of decreased glutathione content in human immunodeficiency virus type 1 Tat-transgenic mice
    • J. Choi, R.M. Liu, R.K. Kundu, F. Sangiorgi, W. Wu, R. Maxson, and H.J. Forman Molecular emchanism of decreased glutathione content in human immunodeficiency virus type 1 Tat-transgenic mice J. Biol. Chem. 275 2000 3693 3698
    • (2000) J. Biol. Chem. , vol.275 , pp. 3693-3698
    • Choi, J.1    Liu, R.M.2    Kundu, R.K.3    Sangiorgi, F.4    Wu, W.5    Maxson, R.6    Forman, H.J.7
  • 140
    • 0032843217 scopus 로고    scopus 로고
    • Effect of thioacetamide on hepatic γ-glutamylcysteine synthetase subunit expression
    • S.C. Lu, Z.Z. Huang, H. Yang, and H. Tsukamoto Effect of thioacetamide on hepatic γ-glutamylcysteine synthetase subunit expression Toxicol. Appl. Pharmacol. 159 1999 161 168
    • (1999) Toxicol. Appl. Pharmacol. , vol.159 , pp. 161-168
    • Lu, S.C.1    Huang, Z.Z.2    Yang, H.3    Tsukamoto, H.4
  • 141
    • 36348989162 scopus 로고    scopus 로고
    • Mechanism of all-trans retinoic acid effect on tumor-associated myeloid-derived suppressor cells
    • Y. Nefedova, M. Fishman, S. Sherman, X. Wang, A.A. Beg, and D.I. Gabrilovich Mechanism of all-trans retinoic acid effect on tumor-associated myeloid-derived suppressor cells Cancer Res. 67 2007 11021 11028
    • (2007) Cancer Res. , vol.67 , pp. 11021-11028
    • Nefedova, Y.1    Fishman, M.2    Sherman, S.3    Wang, X.4    Beg, A.A.5    Gabrilovich, D.I.6
  • 142
  • 143
    • 0037144436 scopus 로고    scopus 로고
    • Role of AP-1 in the co-ordinate induction of rat glutamate-cysteine ligase and glutathione synthetase by tert-butylhydroquinone
    • H.P. Yang, Y. Zeng, T.D. Lee, T. Yang, X.P. Ou, L.X. Chen, M. Haque, R. Rippe, and S.C. Lu Role of AP-1 in the co-ordinate induction of rat glutamate-cysteine ligase and glutathione synthetase by tert-butylhydroquinone J. Biol. Chem. 277 2002 35232 35239
    • (2002) J. Biol. Chem. , vol.277 , pp. 35232-35239
    • Yang, H.P.1    Zeng, Y.2    Lee, T.D.3    Yang, T.4    Ou, X.P.5    Chen, L.X.6    Haque, M.7    Rippe, R.8    Lu, S.C.9
  • 144
    • 25144440916 scopus 로고    scopus 로고
    • Cloning and characterization of the human glutathione synthetase 5′-flanking region
    • T.D. Lee, H.P. Yang, J. Whang, and S.C. Lu Cloning and characterization of the human glutathione synthetase 5′-flanking region Biochem. J. 390 2005 521 528
    • (2005) Biochem. J. , vol.390 , pp. 521-528
    • Lee, T.D.1    Yang, H.P.2    Whang, J.3    Lu, S.C.4
  • 145
    • 0037172653 scopus 로고    scopus 로고
    • Polymorphism in the 5′-flanking region of human glutamate-cysteine ligase modifier subunit gene is associated with myocardial infarction
    • S. Nakamura, K. Kugiyama, S. Sugiyama, S. Miyamoto, S. Koide, H. Fukushima, O. Honda, M. Yoshimura, and H. Ogawa Polymorphism in the 5′-flanking region of human glutamate-cysteine ligase modifier subunit gene is associated with myocardial infarction Circulation 105 2002 2968 2973
    • (2002) Circulation , vol.105 , pp. 2968-2973
    • Nakamura, S.1    Kugiyama, K.2    Sugiyama, S.3    Miyamoto, S.4    Koide, S.5    Fukushima, H.6    Honda, O.7    Yoshimura, M.8    Ogawa, H.9
  • 146
    • 0141615873 scopus 로고    scopus 로고
    • Polymorphism in glutamate-cysteine ligase modifier subunit gene is associated with impairment of nitric oxide-mediated coronary vasomotor function
    • S. Nakamura, S. Sugiyama, D. Fujioka, K. Kawabata, H. Ogawa, and K. Kugiyama Polymorphism in glutamate-cysteine ligase modifier subunit gene is associated with impairment of nitric oxide-mediated coronary vasomotor function Circulation 108 2003 1425 1427
    • (2003) Circulation , vol.108 , pp. 1425-1427
    • Nakamura, S.1    Sugiyama, S.2    Fujioka, D.3    Kawabata, K.4    Ogawa, H.5    Kugiyama, K.6
  • 148
    • 35548985912 scopus 로고    scopus 로고
    • Activation of nuclear factor (erythroid-2 like) factor 2 by toxic bile acids provokes adaptive defense responses to enhance cell survival at the emergence of oxidative stress
    • K.P. Tan, M. Yang, and S. Ito Activation of nuclear factor (erythroid-2 like) factor 2 by toxic bile acids provokes adaptive defense responses to enhance cell survival at the emergence of oxidative stress Mol. Pharmacol. 72 2007 1380 1390
    • (2007) Mol. Pharmacol. , vol.72 , pp. 1380-1390
    • Tan, K.P.1    Yang, M.2    Ito, S.3
  • 149
    • 0034685897 scopus 로고    scopus 로고
    • Transcriptional regulation of the antioxidant response element
    • T. Nguyen, H.C. Huang, and C.B. Pickett Transcriptional regulation of the antioxidant response element J. Biol. Chem. 275 2000 15466 15473
    • (2000) J. Biol. Chem. , vol.275 , pp. 15466-15473
    • Nguyen, T.1    Huang, H.C.2    Pickett, C.B.3
  • 150
    • 0034704137 scopus 로고    scopus 로고
    • Small Maf (MafG and MafK) proteins negatively regulate antioxidant response element-mediated expression and antioxidant induction of the NAD(P)H:quinone oxidoreductase 1 gene
    • S. Dhakshinamoorthy, and A.K. Jaiswal Small Maf (MafG and MafK) proteins negatively regulate antioxidant response element-mediated expression and antioxidant induction of the NAD(P)H:quinone oxidoreductase 1 gene J. Biol. Chem. 275 2000 40134 40141
    • (2000) J. Biol. Chem. , vol.275 , pp. 40134-40141
    • Dhakshinamoorthy, S.1    Jaiswal, A.K.2
  • 151
    • 0037043822 scopus 로고    scopus 로고
    • C-Maf negatively regulates ARE-mediated detoxifying enzyme genes expression and anti-oxidant induction
    • S. Dhakshinamoorthy, and A.K. Jaiswal C-Maf negatively regulates ARE-mediated detoxifying enzyme genes expression and anti-oxidant induction Oncogene 21 2002 5301 5312
    • (2002) Oncogene , vol.21 , pp. 5301-5312
    • Dhakshinamoorthy, S.1    Jaiswal, A.K.2
  • 152
    • 0035140229 scopus 로고    scopus 로고
    • Use of ursodeoxycholic acid in liver disease
    • A. Kumar, and R.K. Tandon Use of ursodeoxycholic acid in liver disease J. Gastroenterol. Hepatol. 16 2001 3 14
    • (2001) J. Gastroenterol. Hepatol. , vol.16 , pp. 3-14
    • Kumar, A.1    Tandon, R.K.2
  • 153
    • 0034131309 scopus 로고    scopus 로고
    • Oxidant stress in rat liver after lipopolysaccharide administration: Effect of inducible nitric-oxide synthase inhibition
    • C. Zhang, L.M. Walker, J.A. Hinson, and P.R. Mayeux Oxidant stress in rat liver after lipopolysaccharide administration: effect of inducible nitric-oxide synthase inhibition J. Pharmacol. Exp. Ther. 293 2000 968 972
    • (2000) J. Pharmacol. Exp. Ther. , vol.293 , pp. 968-972
    • Zhang, C.1    Walker, L.M.2    Hinson, J.A.3    Mayeux, P.R.4
  • 154
    • 0036074141 scopus 로고    scopus 로고
    • Lipopolysaccharides in liver injury: Molecular mechanisms of Kupffer cell activation
    • G.L. Su Lipopolysaccharides in liver injury: molecular mechanisms of Kupffer cell activation Am. J. Physiol. Gastrointest. Liver Physiol. 283 2002 G256 G265
    • (2002) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.283
    • Su, G.L.1
  • 155
    • 0001513966 scopus 로고    scopus 로고
    • Obesity increases sensitivity to endotoxin liver injury: Implications for the pathogenesis of steatohepatitis
    • S.Q. Yang, H.Z. Lin, M.D. Lane, M. Clemens, and A.M. Diehl Obesity increases sensitivity to endotoxin liver injury: implications for the pathogenesis of steatohepatitis Proc. Natl. Acad. Sci. U. S. A. 94 1997 2557 2562
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 2557-2562
    • Yang, S.Q.1    Lin, H.Z.2    Lane, M.D.3    Clemens, M.4    Diehl, A.M.5
  • 156
    • 0026749890 scopus 로고
    • Enhanced sinusoidal glutathione efflux during endotoxin-induced oxidant stress in vivo
    • H. Jaeschke Enhanced sinusoidal glutathione efflux during endotoxin-induced oxidant stress in vivo Am. J. Physiol. Gastrointest. Liver Physiol. 263 1992 G60 G68
    • (1992) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.263
    • Jaeschke, H.1
  • 158
    • 0037245316 scopus 로고    scopus 로고
    • Immune cells redox state from mice with endotoxin-induced oxidative stress. Involvement of NF-κB
    • V.M. Victor, and M. De La Fuente Immune cells redox state from mice with endotoxin-induced oxidative stress. Involvement of NF-κB Free Radic. Res. 37 2003 19 27
    • (2003) Free Radic. Res. , vol.37 , pp. 19-27
    • Victor, V.M.1    De La Fuente, M.2
  • 159
    • 0035094614 scopus 로고    scopus 로고
    • Xanthine oxidase activity and blood glutathione redox ration in infants and children with septic shock syndrome
    • I. Németh, and D. Boda Xanthine oxidase activity and blood glutathione redox ration in infants and children with septic shock syndrome Intensive Care Med. 27 2001 216 221
    • (2001) Intensive Care Med. , vol.27 , pp. 216-221
    • Németh, I.1    Boda, D.2
  • 160
    • 37849187228 scopus 로고    scopus 로고
    • Protective effect of glutathione against lipopolysaccharide-induced inflammation and mortality in rats
    • S. Sun, H. Zhang, B. Xue, Y. Wu, J. Wang, Z. Yin, and L. Luo Protective effect of glutathione against lipopolysaccharide-induced inflammation and mortality in rats Inflamm. Res. 55 2006 504 510
    • (2006) Inflamm. Res. , vol.55 , pp. 504-510
    • Sun, S.1    Zhang, H.2    Xue, B.3    Wu, Y.4    Wang, J.5    Yin, Z.6    Luo, L.7
  • 161
    • 80053448632 scopus 로고    scopus 로고
    • Macropinocytosis of extracellular glutathione ameliorates tumor necrosis factor α release in activated macrophages
    • N.S. Gould, E. Min, and B.J. Day Macropinocytosis of extracellular glutathione ameliorates tumor necrosis factor α release in activated macrophages PLoS One 6 2011 e25704
    • (2011) PLoS One , vol.6 , pp. 25704
    • Gould, N.S.1    Min, E.2    Day, B.J.3
  • 165
    • 0035013288 scopus 로고    scopus 로고
    • Current concepts in the pathogenesis of alcoholic liver injury
    • H.C. Tsukamoto, and S.C. Lu Current concepts in the pathogenesis of alcoholic liver injury FASEB J. 15 2001 1335 1349
    • (2001) FASEB J. , vol.15 , pp. 1335-1349
    • Tsukamoto, H.C.1    Lu, S.C.2
  • 167
    • 0024314801 scopus 로고
    • Maintenance of differentiated phenotype of cultured rat hepatic lipocytes by basement membrane matrix
    • S.L. Friedman, F.J. Roll, J. Boyles, D.M. Arenson, and D.M. Bissell Maintenance of differentiated phenotype of cultured rat hepatic lipocytes by basement membrane matrix J. Biol. Chem. 264 1989 10756 10762
    • (1989) J. Biol. Chem. , vol.264 , pp. 10756-10762
    • Friedman, S.L.1    Roll, F.J.2    Boyles, J.3    Arenson, D.M.4    Bissell, D.M.5
  • 168
    • 0027177097 scopus 로고
    • Cellular and molecular aspects of hepatic fibrosis
    • A.D. Burt Cellular and molecular aspects of hepatic fibrosis J. Pathol. 70 1993 105 114
    • (1993) J. Pathol. , vol.70 , pp. 105-114
    • Burt, A.D.1
  • 170
    • 0036281460 scopus 로고    scopus 로고
    • Effects and regulation of connective tissue growth factor on hepatic stellate cells
    • V. Paradis, D. Dargere, F. Bonvoust, M. Vidaud, P. Segarini, and P. Bedossa Effects and regulation of connective tissue growth factor on hepatic stellate cells Lab. Invest. 82 2002 767 774
    • (2002) Lab. Invest. , vol.82 , pp. 767-774
    • Paradis, V.1    Dargere, D.2    Bonvoust, F.3    Vidaud, M.4    Segarini, P.5    Bedossa, P.6
  • 171
    • 0038644530 scopus 로고    scopus 로고
    • Leptin induces increased alpha2(I) collagen gene expression in cultured rat hepatic stellate cells
    • N.K. Saxena, G. Saliba, J.J. Floyd, and F.A. Anania Leptin induces increased alpha2(I) collagen gene expression in cultured rat hepatic stellate cells J. Cell. Biochem. 89 2003 2003 311 320
    • (2003) J. Cell. Biochem. , vol.89 , Issue.2003 , pp. 311-320
    • Saxena, N.K.1    Saliba, G.2    Floyd, J.J.3    Anania, F.A.4
  • 172
    • 1842426610 scopus 로고    scopus 로고
    • Inhibitory effect of soluble PDGF-beta receptor in culture-activated hepatic stellate cells
    • B.E. Kamphorst, D. Stoll, A.M. Gressner, and R. Weiskirchen Inhibitory effect of soluble PDGF-beta receptor in culture-activated hepatic stellate cells Biochem. Biophys. Res. Commun. 317 2004 451 462
    • (2004) Biochem. Biophys. Res. Commun. , vol.317 , pp. 451-462
    • Kamphorst, B.E.1    Stoll, D.2    Gressner, A.M.3    Weiskirchen, R.4
  • 173
    • 0034809414 scopus 로고    scopus 로고
    • Hepatic stellate cell behavior during the resolution of liver injury
    • J.P. Iredale Hepatic stellate cell behavior during the resolution of liver injury Semin. Liver Dis. 21 2001 427 436
    • (2001) Semin. Liver Dis. , vol.21 , pp. 427-436
    • Iredale, J.P.1
  • 174
    • 84867801009 scopus 로고    scopus 로고
    • Mechanism and significance of changes in glutamate-cysteine ligase expression during hepatic fibrogenesis
    • doi:10.1074/jbc.M112.370775 (in press)
    • K. Ramani, M.L. Tomasi, H. Yang, K. Ko, S.C. Lu, Mechanism and significance of changes in glutamate-cysteine ligase expression during hepatic fibrogenesis. J. Biol. Chem. (in press) http://dx.doi.org/10.1074/jbc.M112. 370775.
    • J. Biol. Chem.
    • Ramani, K.1    Tomasi, M.L.2    Yang, H.3    Ko, K.4    Lu, S.C.5


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