This work is licensed under the Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.
Franklin C.C., Backos D.S., Mohar I., White C.C., Forman H.J., Kavanagh T.J.: Structure, function, and post-translational regulation of the catalytic and modifier subunits of glutamate cysteine ligase. Mol. Aspects Med., 2009; 30: 86-98FranklinC.C.BackosD.S.MoharI.WhiteC.C.FormanH.J.KavanaghT.J.Structure, function, and post-translational regulation of the catalytic and modifier subunits of glutamate cysteine ligaseMol. Aspects Med200930869810.1016/j.mam.2008.08.009Search in Google Scholar
Bilska A., Kryczyk A., Włodek L.: The different aspects of the biological role of glutathione. Postępy Hig. Med. Dośw., 2007; 61: 438-453BilskaA.KryczykA.WłodekL.The different aspects of the biological role of glutathionePostępy Hig. Med. Dośw200761438453Search in Google Scholar
Ferguson G., Bridge W.: Glutamate cysteine ligase and the age-related decline in cellular glutathione: The therapeutic potential of γ-glutamylcysteine. Arch. Biochem. Biophys., 2016; 593: 12-23FergusonG.BridgeW.Glutamate cysteine ligase and the age-related decline in cellular glutathione: The therapeutic potential of γ-glutamylcysteineArch. Biochem. Biophys2016593122310.1016/j.abb.2016.01.017Search in Google Scholar
Lu S.C.: Glutathione synthesis. Biochim. Biophys. Acta, 2013; 1830: 3143-3153LuS.C.Glutathione synthesisBiochim. Biophys. Acta201318303143315310.1016/j.bbagen.2012.09.008Search in Google Scholar
Li S., Li X., Rozanski G.J.: Regulation of glutathione in cardiac myocytes. J. Mol. Cell. Cardiol., 2003; 35: 1145-1152LiS.LiX.RozanskiG.J.Regulation of glutathione in cardiac myocytesJ. Mol. Cell. Cardiol2003351145115210.1016/S0022-2828(03)00230-XSearch in Google Scholar
Pompella A., Corti A., Paolicchi A., Giommarelli C., Zunino F.: γ-glutamyltransferase, redox regulation and cancer drug resistance. Curr. Opin. Pharmacol., 2007; 7: 360-366PompellaA.CortiA.PaolicchiA.GiommarelliC.ZuninoF.γ-glutamyltransferase, redox regulation and cancer drug resistanceCurr. Opin. Pharmacol2007736036610.1016/j.coph.2007.04.004Search in Google Scholar
Meister A.: On the discovery of glutathione. Trends. Biochem. Sci., 1988; 13: 185-188MeisterA.On the discovery of glutathioneTrends. Biochem. Sci19881318518810.1016/0968-0004(88)90148-XSearch in Google Scholar
Zarka M.H., Bridge W.J.: Oral administration of γ-glutamylcysteine increases intracellular glutathione levels above homeostasis in a randomised human trial pilot study. Redox Biol., 2017; 11: 631-636ZarkaM.H.BridgeW.J.Oral administration of γ-glutamylcysteine increases intracellular glutathione levels above homeostasis in a randomised human trial pilot studyRedox Biol20171163163610.1016/j.redox.2017.01.014528448928131081Search in Google Scholar
Franco R., Schoneveld O.J., Pappa A., Panayiotidis M.I.: The central role of glutathione in the pathophysiology of human diseases. Arch. Physiol. Biochem., 2007; 113: 234-258FrancoR.SchoneveldO.J.PappaA.PanayiotidisM.I.The central role of glutathione in the pathophysiology of human diseasesArch. Physiol. Biochem200711323425810.1080/1381345070166119818158646Search in Google Scholar
Forman H.J., Zhang H., Rinna A.: Glutathione: Overview of its protective roles, measurement, and biosynthesis. Mol. Aspects Med., 2009; 30: 1-12FormanH.J.ZhangH.RinnaA.Glutathione: Overview of its protective roles, measurement, and biosynthesisMol. Aspects Med20093011210.1016/j.mam.2008.08.006269607518796312Search in Google Scholar
Yang Y., Chen Y., Johansson E., Schneider S.N., Shertzer H.G., Nebert D.W., Dalton T.P.: Interaction between the catalytic and modifier subunits of glutamate-cysteine ligase. Biochem. Pharmacol., 2007; 74: 372-381YangY.ChenY.JohanssonE.SchneiderS.N.ShertzerH.G.NebertD.W.DaltonT.P.Interaction between the catalytic and modifier subunits of glutamate-cysteine ligaseBiochem. Pharmacol20077437238110.1016/j.bcp.2007.02.00317517378Search in Google Scholar
Shi Z.Z., Osei-Frimpong J., Kala G., Kala S.V., Barrios R.J., Habib G.M., Lukin D.J., Danney C.M., Matzuk M.M., Lieberman M.W.: Glutathione synthesis is essential for mouse development but not for cell growth in culture. Proc. Natl. Acad. Sci. USA, 2000; 97: 5101-5106ShiZ.Z.Osei-FrimpongJ.KalaG.KalaS.V.BarriosR.J.HabibG.M.LukinD.J.DanneyC.M.MatzukM.M.LiebermanM.W.Glutathione synthesis is essential for mouse development but not for cell growth in cultureProc. Natl. Acad. Sci. USA2000975101510610.1073/pnas.97.10.51012578810805773Search in Google Scholar
Yang Y., Dieter M.Z., Chen Y., Shertzer H.G., Nebert D.W., Dalton T.P.: 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., 2002; 277: 49446-49452YangY.DieterM.Z.ChenY.ShertzerH.G.NebertD.W.DaltonT.P.Initial characterization of the glutamate-cysteine ligase modifier subunit Gclm(-/-) knockout mouseNovel model system for a severely compromised oxidative stress response. J. Biol. Chem2002277494464945210.1074/jbc.M20937220012384496Search in Google Scholar
Mulcahy R.T., Bailey H.H., Gipp J.J.: Up-regulation of γ-glutamylcysteine synthetase activity in melphalan-resistant human multiple myeloma cells expressing increased glutathione levels. Cancer Chemother. Pharmacol., 1994; 34: 67-71MulcahyR.T.BaileyH.H.GippJ.J.Up-regulation of γ-glutamylcysteine synthetase activity in melphalan-resistant human multiple myeloma cells expressing increased glutathione levelsCancer Chemother. Pharmacol199434677110.1007/BF006861147513621Search in Google Scholar
Iles K.E., Liu R.M.: Mechanisms of glutamate cysteine ligase (GCL) induction by 4-hydroxynonenal. Free Radic. Biol. Med., 2005; 38: 547-556IlesK.E.LiuR.M.Mechanisms of glutamate cysteine ligase (GCL) induction by 4-hydroxynonenalFree Radic. Biol. Med20053854755610.1016/j.freeradbiomed.2004.11.01215683710Search in Google Scholar
Krejsa C.M., Franklin C.C., White C.C., Ledbetter J.A., Schieven G.L., Kavanagh T.J.: Rapid activation of glutamate cysteine ligase following oxidative stress. J. Biol. Chem., 2010; 285: 16116-16124KrejsaC.M.FranklinC.C.WhiteC.C.LedbetterJ.A.SchievenG.L.KavanaghT.J.Rapid activation of glutamate cysteine ligase following oxidative stressJ. Biol. Chem2010285161161612410.1074/jbc.M110.116210287148020332089Search in Google Scholar
Liu R.M., Gao L., Choi J., Forman H.J.: Gamma-glutamylcysteine synthetase: mRNA stabilization and independent subunit transcription by 4-hydroxy-2-nonenal. Am. J. Physiol., 1998; 275: L861-L869LiuR.M.GaoL.ChoiJ.FormanH.J.Gamma-glutamylcysteine synthetase: mRNA stabilization and independent subunit transcription by 4-hydroxy-2-nonenalAm. J. Physiol1998275L861L86910.1152/ajplung.1998.275.5.L8619815102Search in Google Scholar
Liu R.M., Hu H., Robison T.W., Forman H.J.: 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., 1996; 14: 186-191LiuR.M.HuH.RobisonT.W.FormanH.J.Differential enhancement of γ-glutamyl transpeptidase and γ-glutamylcysteine synthetase by tert-butylhydroquinone in rat lung epithelial L2 cellsAm. J. Respir. Cell Mol. Biol19961418619110.1165/ajrcmb.14.2.86302698630269Search in Google Scholar
Zhang H., Court N., Forman H.J.: Submicromolar concentrations of 4-hydroxynonenal induce glutamate cysteine ligase expression in HBE1 cells. Redox Rep., 2007; 12: 101-106ZhangH.CourtN.FormanH.J.Submicromolar concentrations of 4-hydroxynonenal induce glutamate cysteine ligase expression in HBE1 cellsRedox Rep20071210110610.1179/135100007X162266273048917263920Search in Google Scholar
Benassi B., Fanciulli M., Fiorentino F., Porrello A., Chiorino G., Loda M., Zupi G., Biroccio A.: c-Myc phosphorylation is required for cellular response to oxidative stress. Mol. Cell., 2006; 21: 509519BenassiB.FanciulliM.FiorentinoF.PorrelloA.ChiorinoG.LodaM.ZupiG.BiroccioA.c-Myc phosphorylation is required for cellular response to oxidative stressMol. Cell20062150951910.1016/j.molcel.2006.01.00916483932Search in Google Scholar
Cai J., Huang Z.Z., Lu S.C.: Differential regulation of γ-glutamylcysteine synthetase heavy and light subunit gene expression. Biochem. J., 1997; 326: 167-172CaiJ.HuangZ.Z.LuS.C.Differential regulation of γ-glutamylcysteine synthetase heavy and light subunit gene expressionBiochem. J199732616717210.1042/bj326016712186509337864Search in Google Scholar
Lu S.C., Kuhlenkamp J., Garcia-Ruiz C., Kaplowitz N.: Hormone-mediated down-regulation of hepatic glutathione synthesis in the rat. J. Clin. Invest., 1991; 88: 260-269LuS.C.KuhlenkampJ.Garcia-RuizC.KaplowitzN.Hormone-mediated down-regulation of hepatic glutathione synthesis in the ratJ. Clin. Invest19918826026910.1172/JCI115286Search in Google Scholar
Kim S.K., Woodcroft K.J., Khodadadeh S.S., Novak R.F.: Insulin signaling regulates γ-glutamylcysteine ligase catalytic subunit expression in primary cultured rat hepatocytes. J. Pharmacol. Exp. Ther., 2004; 311: 99-108KimS.K.WoodcroftK.J.KhodadadehS.S.NovakR.F.Insulin signaling regulates γ-glutamylcysteine ligase catalytic subunit expression in primary cultured rat hepatocytesJ. Pharmacol. Exp. Ther20043119910810.1124/jpet.104.070375Search in Google Scholar
Eaton D.L., Hamel D.M.: Increase in γ-glutamylcysteine synthetase activity as a mechanism for butylated hydroxyanisole-mediated elevation of hepatic glutathione. Toxicol. Appl. Pharmacol., 1994; 126: 145-149EatonD.L.HamelD.M.Increase in γ-glutamylcysteine synthetase activity as a mechanism for butylated hydroxyanisole-mediated elevation of hepatic glutathioneToxicol. Appl. Pharmacol199412614514910.1006/taap.1994.1100Search in Google Scholar
Urata Y., Honma S., Goto S., Todoroki S., Iida T., Cho S., Honma K., Kondo T.: Melatonin induces γ-glutamylcysteine synthetase mediated by activator protein-1 in human vascular endothelial cells. Free Radic. Biol. Med., 1999; 27: 838-847UrataY.HonmaS.GotoS.TodorokiS.IidaT.ChoS.HonmaK.KondoT.Melatonin induces γ-glutamylcysteine synthetase mediated by activator protein-1 in human vascular endothelial cellsFree Radic. Biol. Med19992783884710.1016/S0891-5849(99)00131-8Search in Google Scholar
Langston J.W., Li W., Harrison L., Aw T.Y.: 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., 2011; 51: 1749-1757LangstonJ.W.LiW.HarrisonL.AwT.Y.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 synthesisFree Radic. Biol. Med2011511749175710.1016/j.freeradbiomed.2011.08.004318833721871559Search in Google Scholar
Kensler T.W., Wakabayashi N., Biswal S.: Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathway. Annu. Rev. Pharmacol. Toxicol., 2007; 47: 89-116KenslerT.W.WakabayashiN.BiswalS.Cell survival responses to environmental stresses via the Keap1-Nrf2-ARE pathwayAnnu. Rev. Pharmacol. Toxicol2007478911610.1146/annurev.pharmtox.46.120604.14104616968214Search in Google Scholar
Chan K., Han X.D., Kan Y.W.: An important function of Nrf2 in combating oxidative stress: Detoxification of acetaminophen. Proc. Natl. Acad. Sci. USA, 2001; 98: 4611-4616ChanK.HanX.D.KanY.W.An important function of Nrf2 in combating oxidative stress: Detoxification of acetaminophenProc. Natl. Acad. Sci. USA2001984611461610.1073/pnas.0810820983188211287661Search in Google Scholar
Wild A.C., Moinova H.R., Mulcahy R.T.: Regulation of γ-glutamylcysteine synthetase subunit gene expression by the transcription factor Nrf2. J. Biol. Chem., 1999; 274: 33627-33636WildA.C.MoinovaH.R.MulcahyR.T.Regulation of γ-glutamylcysteine synthetase subunit gene expression by the transcription factor Nrf2J. Biol. Chem1999274336273363610.1074/jbc.274.47.3362710559251Search in Google Scholar
Chen Y., Shertzer H.G., Schneider S.N., Nebert D.W., Dalton T.P.: Glutamate cysteine ligase catalysis: Dependence on ATP and modifier subunit for regulation of tissue glutathione levels. J. Biol. Chem., 2005; 280: 33766-33774ChenY.ShertzerH.G.SchneiderS.N.NebertD.W.DaltonT.P.Glutamate cysteine ligase catalysis: Dependence on ATP and modifier subunit for regulation of tissue glutathione levelsJ. Biol. Chem2005280337663377410.1074/jbc.M50460420016081425Search in Google Scholar
Fraser J.A., Kansagra P., Kotecki C., Saunders R.D., McLellan L.I.: The modifier subunit of Drosophila glutamate-cysteine ligase regulates catalytic activity by covalent and noncovalent interactions and influences glutathione homeostasis in vivo. J. Biol. Chem., 2003; 278: 46369-46377FraserJ.A.KansagraP.KoteckiC.SaundersR.D.McLellanL.I.The modifier subunit of Drosophila glutamate-cysteine ligase regulates catalytic activity by covalent and noncovalent interactions and influences glutathione homeostasis in vivoJ. Biol. Chem2003278463694637710.1074/jbc.M30803520012954617Search in Google Scholar
Huang C.S., Chang L.S., Anderson M.E., Meister A.: Catalytic and regulatory properties of the heavy subunit of rat kidney gamma-glutamylcysteine synthetase. J. Biol. Chem., 1993; 268: 19675-19680HuangC.S.ChangL.S.AndersonM.E.MeisterA.Catalytic and regulatory properties of the heavy subunit of rat kidney gamma-glutamylcysteine synthetaseJ. Biol. Chem1993268196751968010.1016/S0021-9258(19)36569-XSearch in Google Scholar
Levonen A.L., Landar A., Ramachandran A., Ceaser E.K., Dickinson D.A., Zanoni G., Morrow J.D., Darley-Usmar V.M.: Cellular mechanisms of redox cell signalling: Role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products. Biochem. J., 2004; 378: 373-382LevonenA.L.LandarA.RamachandranA.CeaserE.K.DickinsonD.A.ZanoniG.MorrowJ.D.Darley-UsmarV.M.Cellular mechanisms of redox cell signalling: Role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation productsBiochem. J200437837338210.1042/bj20031049Search in Google Scholar
Tu Z., Anders M.W.: Identification of an important cysteine residue in human glutamate-cysteine ligase catalytic subunit by site-directed mutagenesis. Biochem. J., 1998; 336: 675-680TuZ.AndersM.W.Identification of an important cysteine residue in human glutamate-cysteine ligase catalytic subunit by site-directed mutagenesisBiochem. J199833667568010.1042/bj3360675Search in Google Scholar
Backos D.S., Fritz K.S., Roede J.R., Petersen D.R., Franklin C.C.: Posttranslational modification and regulation of glutamatecysteine ligase by the α,β-unsaturated aldehyde 4-hydroxy-2-non-enal. Free Radic. Biol. Med., 2011; 50: 14-26BackosD.S.FritzK.S.RoedeJ.R.PetersenD.R.FranklinC.C.Posttranslational modification and regulation of glutamatecysteine ligase by the α,β-unsaturated aldehyde 4-hydroxy-2-non-enalFree Radic. Biol. Med201150142610.1016/j.freeradbiomed.2010.10.694Search in Google Scholar
Hayashi H., Iimuro M., Matsumoto Y., Kaneko M.: Effects of gamma-glutamylcysteine ethyl ester on heart mitochondrial creatine kinase activity: Involvement of sulfhydryl groups. Eur. J. Pharmacol., 1998; 349: 133-136HayashiH.IimuroM.MatsumotoY.KanekoM.Effects of gamma-glutamylcysteine ethyl ester on heart mitochondrial creatine kinase activity: Involvement of sulfhydryl groupsEur. J. Pharmacol199834913313610.1016/S0014-2999(98)00266-0Search in Google Scholar
Toroser D., Yarian C.S., Orr W.C., Sohal R.S.: Mechanisms of γ-glutamylcysteine ligase regulation. Biochim. Biophys. Acta, 2006; 1760: 233-244ToroserD.YarianC.S.OrrW.C.SohalR.S.Mechanisms of γ-glutamylcysteine ligase regulationBiochim. Biophys. Acta2006176023324410.1016/j.bbagen.2005.10.010Search in Google Scholar
Sekhar K.R., Freeman M.L.: Autophosphorylation inhibits the activity of γ-glutamylcysteine synthetase. J. Enzyme Inhib., 1999; 14: 323-330SekharK.R.FreemanM.L.Autophosphorylation inhibits the activity of γ-glutamylcysteine synthetaseJ. Enzyme Inhib19991432333010.3109/14756369909030325Search in Google Scholar
Zhu M., Bowden G.T.: Molecular mechanism(s) for UV-B irradiation-induced glutathione depletion in cultured human keratinocytes. Photochem. Photobiol., 2004; 80: 191-196ZhuM.BowdenG.T.Molecular mechanism(s) for UV-B irradiation-induced glutathione depletion in cultured human keratinocytesPhotochem. Photobiol20048019119610.1562/2004-02-26-RA-091.1Search in Google Scholar
Soltaninassab S.R., Sekhar K.R., Meredith M.J., Freeman M.L.: Multi-faceted regulation of γ-glutamylcysteine synthetase. J. Cell Physiol., 2000; 182: 163-170SoltaninassabS.R.SekharK.R.MeredithM.J.FreemanM.L.Multi-faceted regulation of γ-glutamylcysteine synthetaseJ. Cell Physiol200018216317010.1002/(SICI)1097-4652(200002)182:2<163::AID-JCP4>3.0.CO;2-1Search in Google Scholar
Abdelmegeed M.A., Jang S., Banerjee A., Hardwick J.P., Song B.J.: Robust protein nitration contributes to acetaminophen-induced mitochondrial dysfunction and acute liver injury. Free Radic. Biol. Med., 2013; 60: 211-222AbdelmegeedM.A.JangS.BanerjeeA.HardwickJ.P.SongB.J.Robust protein nitration contributes to acetaminophen-induced mitochondrial dysfunction and acute liver injuryFree Radic. Biol. Med20136021122210.1016/j.freeradbiomed.2013.02.018Search in Google Scholar
Braidy N., Zarka M., Jugder B.E., Welch J., Jayasena T., Chan D.K.Y., Sachdev P., Bridge W.: The precursor to glutathione (GSH), γ-Glutamylcysteine (GGC), can ameliorate oxidative damage and neuroinflammation induced by Aβ40 oligomers in human astrocytes. Front Aging Neurosci., 2019; 11: 177BraidyN.ZarkaM.JugderB.E.WelchJ.JayasenaT.ChanD.K.Y.SachdevP.BridgeW.The precursor to glutathione (GSH), γ-Glutamylcysteine (GGC), can ameliorate oxidative damage and neuroinflammation induced by Aβ40 oligomers in human astrocytesFront Aging Neurosci20191117710.3389/fnagi.2019.00177669429031440155Search in Google Scholar
Ristoff E., Larsson A.: Inborn errors in the metabolism of glutathione. Orphanet J. Rare Dis., 2007; 2: 16RistoffE.LarssonA.Inborn errors in the metabolism of glutathioneOrphanet J. Rare Dis200721610.1186/1750-1172-2-16185209417397529Search in Google Scholar
Hamilton D., Wu J.H., Alaoui-Jamali M., Batist G.: A novel missense mutation in the γ-glutamylcysteine synthetase catalytic subunit gene causes both decreased enzymatic activity and glutathione production. Blood, 2003; 102: 725-730HamiltonD.WuJ.H.Alaoui-JamaliM.BatistG.A novel missense mutation in the γ-glutamylcysteine synthetase catalytic subunit gene causes both decreased enzymatic activity and glutathione productionBlood200310272573010.1182/blood-2002-11-362212663448Search in Google Scholar
Mañú Pereira M., Gelbart T., Ristoff E., Crain K.C., Bergua J.M., López Lafuente A., Kalko S.G., García Mateos E., Beutler E., Vives Corrons J.L.: Chronic non-spherocytic hemolytic anemia associated with severe neurological disease due to γ-glutamylcysteine synthetase deficiency in a patient of Moroccan origin. Haematologica, 2007; 92: e102-105MañúPereira M.GelbartT.RistoffE.CrainK.C.BerguaJ.M.LópezLafuente A.KalkoS.G.GarcíaMateos E.BeutlerE.VivesCorrons J.L.Chronic non-spherocytic hemolytic anemia associated with severe neurological disease due to γ-glutamylcysteine synthetase deficiency in a patient of Moroccan originHaematologica200792e10210510.3324/haematol.1123818024385Search in Google Scholar
Gutowicz M.: The influence of reactive oxygen species on the central nervous system. Postępy Hig. Med. Dośw., 2011; 65: 104113GutowiczM.The influence of reactive oxygen species on the central nervous systemPostępy Hig. Med. Dośw20116510411310.5604/17322693.93348621357998Search in Google Scholar
Johnson W.M., Wilson-Delfosse A.L., Mieyal J.J.: Dysregulation of glutathione homeostasis in neurodegenerative diseases. Nutrients, 2012; 4: 1399-1440JohnsonW.M.Wilson-DelfosseA.L.MieyalJ.J.Dysregulation of glutathione homeostasis in neurodegenerative diseasesNutrients201241399144010.3390/nu4101399349700223201762Search in Google Scholar
Pearce R.K., Owen A., Daniel S., Jenner P., Marsden C.D.: Alterations in the distribution of glutathione in the substantia nigra in Parkinson’s disease. J. Neural. Transm., 1997; 104: 661-677PearceR.K.OwenA.DanielS.JennerP.MarsdenC.D.Alterations in the distribution of glutathione in the substantia nigra in Parkinson’s diseaseJ. Neural. Transm199710466167710.1007/BF012918849444566Search in Google Scholar
Garrido M., Tereshchenko Y., Zhevtsova Z., Taschenberger G., Bähr M., Kügler S.: Glutathione depletion and overproduction both initiate degeneration of nigral dopaminergic neurons. Acta Neuropathol., 2011; 121: 475-485GarridoM.TereshchenkoY.ZhevtsovaZ.TaschenbergerG.BährM.KüglerS.Glutathione depletion and overproduction both initiate degeneration of nigral dopaminergic neuronsActa Neuropathol201112147548510.1007/s00401-010-0791-x305835521191602Search in Google Scholar
Sabens E.A., Distler A.M., Mieyal J.J.: Levodopa deactivates enzymes that regulate thiol-disulfide homeostasis and promotes neuronal cell death: Implications for therapy of Parkinson’s disease. Biochemistry, 2010; 49: 2715-2724SabensE.A.DistlerA.M.MieyalJ.J.Levodopa deactivates enzymes that regulate thiol-disulfide homeostasis and promotes neuronal cell death: Implications for therapy of Parkinson’s diseaseBiochemistry2010492715272410.1021/bi9018658320193920141169Search in Google Scholar
Feng W., Rosca M., Fan Y., Hu Y., Feng P., Lee H.G., Monnier V.M., Fan X.: Gclc deficiency in mouse CNS causes mitochondrial damage and neurodegeneration. Hum. Mol. Genet., 2017; 26: 1376-1390FengW.RoscaM.FanY.HuY.FengP.LeeH.G.MonnierV.M.FanX.Gclc deficiency in mouse CNS causes mitochondrial damage and neurodegenerationHum. Mol. Genet2017261376139010.1093/hmg/ddx040607507828158580Search in Google Scholar
Fernandez-Fernandez S., Bobo-Jimenez V., Requejo-Aguilar R., Gonzalez-Fernandez S., Resch M., Carabias-Carrasco M., Ros J., Almeida A., Bolaños J.P.: Hippocampal neurons require a large pool of glutathione to sustain dendrite integrity and cognitive function. Redox Biol., 2018; 19: 52-61Fernandez-FernandezS.Bobo-JimenezV.Requejo-AguilarR.Gonzalez-FernandezS.ReschM.Carabias-CarrascoM.RosJ.AlmeidaA.BolañosJ.P.Hippocampal neurons require a large pool of glutathione to sustain dendrite integrity and cognitive functionRedox Biol201819526110.1016/j.redox.2018.08.003609245030107295Search in Google Scholar
Liu R.M.: Down-regulation of γ-glutamylcysteine synthetase regulatory subunit gene expression in rat brain tissue during aging. J. Neurosci. Res., 2002; 68: 344-351LiuR.M.Down-regulation of γ-glutamylcysteine synthetase regulatory subunit gene expression in rat brain tissue during agingJ. Neurosci. Res20026834435110.1002/jnr.1021712111865Search in Google Scholar
Pessayre D., Fromenty B., Berson A., Robin M.A., Lettéron P., Moreau R., Mansouri A.: Central role of mitochondria in drug-induced liver injury. Drug Metab. Rev., 2012; 44: 34-87PessayreD.FromentyB.BersonA.RobinM.A.LettéronP.MoreauR.MansouriA.Central role of mitochondria in drug-induced liver injuryDrug Metab. Rev201244348710.3109/03602532.2011.60408621892896Search in Google Scholar
Chen Y., Dong H., Thompson D.C., Shertzer H.G., Nebert D.W., Vasiliou V.: Glutathione defense mechanism in liver injury: Insights from animal models. Food Chem. Toxicol., 2013; 60: 38-44ChenY.DongH.ThompsonD.C.ShertzerH.G.NebertD.W.VasiliouV.Glutathione defense mechanism in liver injury: Insights from animal modelsFood Chem. Toxicol201360384410.1016/j.fct.2013.07.008380118823856494Search in Google Scholar
Chen Y., Yang Y., Miller M.L., Shen D., Shertzer H.G., Stringer K.F., Wang B., Schneider S.N., Nebert D.W., Dalton T.P.: Hepatocyte-specific Gclc deletion leads to rapid onset of steatosis with mitochondrial injury and liver failure. Hepatology, 2007; 45: 11181128ChenY.YangY.MillerM.L.ShenD.ShertzerH.G.StringerK.F.WangB.SchneiderS.N.NebertD.W.DaltonT.P.Hepatocyte-specific Gclc deletion leads to rapid onset of steatosis with mitochondrial injury and liver failureHepatology2007451118112810.1002/hep.2163517464988Search in Google Scholar
McConnachie L.A., Mohar I., Hudson F.N., Ware C.B., Ladiges W.C., Fernandez C., Chatterton-Kirchmeier S., White C.C., Pierce R.H., Kavanagh T.J.: Glutamate cysteine ligase modifier subunit deficiency and gender as determinants of acetaminophen-induced hepatotoxicity in mice. Toxicol. Sci., 2007; 99: 628-636McConnachieL.A.MoharI.HudsonF.N.WareC.B.LadigesW.C.FernandezC.Chatterton-KirchmeierS.WhiteC.C.PierceR.H.KavanaghT.J.Glutamate cysteine ligase modifier subunit deficiency and gender as determinants of acetaminophen-induced hepatotoxicity in miceToxicol. Sci20079962863610.1093/toxsci/kfm16517584759Search in Google Scholar
Jaeschke H., McGill M.R., Williams C.D., Ramachandran A.: Current issues with acetaminophen hepatotoxicity – a clinically relevant model to test the efficacy of natural products. Life Sci., 2011; 88: 737-745JaeschkeH.McGillM.R.WilliamsC.D.RamachandranA.Current issues with acetaminophen hepatotoxicity – a clinically relevant model to test the efficacy of natural productsLife Sci20118873774510.1016/j.lfs.2011.01.025307652621296090Search in Google Scholar
Pervaiz S., Clement M.V.: Tumor intracellular redox status and drug resistance-serendipity or a causal relationship? Curr. Pharm. Des., 2004; 10: 1969-1977PervaizS.ClementM.V.Tumor intracellular redox status and drug resistance-serendipity or a causal relationship? CurrPharm. Des2004101969197710.2174/1381612043384411Search in Google Scholar
Ballatori N., Krance S.M., Notenboom S., Shi S., Tieu K., Hammond C.L.: Glutathione dysregulation and the etiology and progression of human diseases. Biol. Chem., 2009; 390: 191-214BallatoriN.KranceS.M.NotenboomS.ShiS.TieuK.HammondC.L.Glutathione dysregulation and the etiology and progression of human diseasesBiol. Chem200939019121410.1515/BC.2009.033275615419166318Search in Google Scholar
Estrela J.M., Ortega A., Obrador E.: Glutathione in cancer biology and therapy. Crit. Rev. Clin. Lab. Sci., 2006; 43: 143-181EstrelaJ.M.OrtegaA.ObradorE.Glutathione in cancer biology and therapyCrit. Rev. Clin. Lab. Sci20064314318110.1080/1040836050052387816517421Search in Google Scholar
Traverso N., Ricciarelli R., Nitti M., Marengo B., Furfaro A.L., Pronzato M.A., Marinari U.M., Domenicotti C.: Role of glutathione in cancer progression and chemoresistance. Oxid. Med. Cell. Longev., 2013; 2013: 972913TraversoN.RicciarelliR.NittiM.MarengoB.FurfaroA.L.PronzatoM.A.MarinariU.M.DomenicottiC.Role of glutathione in cancer progression and chemoresistanceOxid. Med. Cell. Longev2013201397291310.1155/2013/972913367333823766865Search in Google Scholar
Briehl M.M., Tome M.E., Wilkinson S.T., Jaramillo M.C., Lee K.: Mitochondria and redox homoeostasis as chemotherapeutic targets. Biochem. Soc. Trans., 2014; 42: 939-944BriehlM.M.TomeM.E.WilkinsonS.T.JaramilloM.C.LeeK.Mitochondria and redox homoeostasis as chemotherapeutic targetsBiochem. Soc. Trans20144293994410.1042/BST20140087556432725109983Search in Google Scholar
Jang J.H., Surh Y.J.: Bcl-2 attenuation of oxidative cell death is associated with up-regulation of γ-glutamylcysteine ligase via constitutive NF-κB activation. J. Biol. Chem., 2004; 279: 38779-38786JangJ.H.SurhY.J.Bcl-2 attenuation of oxidative cell death is associated with up-regulation of γ-glutamylcysteine ligase via constitutive NF-κB activationJ. Biol. Chem2004279387793878610.1074/jbc.M40637120015208316Search in Google Scholar
Järvinen K., Soini Y., Kahlos K., Kinnula V.L.: Overexpression of γ-glutamylcysteine synthetase in human malignant mesothelioma. Hum. Pathol., 2002; 33: 748-755JärvinenK.SoiniY.KahlosK.KinnulaV.L.Overexpression of γ-glutamylcysteine synthetase in human malignant mesotheliomaHum. Pathol20023374875510.1053/hupa.2002.12619112196927Search in Google Scholar
Kim A.D., Zhang R., Han X., Kang K.A., Piao M.J., Maeng Y.H., Chang W.Y., Hyun J.W.: Involvement of glutathione and glutathione metabolizing enzymes in human colorectal cancer cell lines and tissues. Mol. Med. Rep., 2015; 12: 4314-4319KimA.D.ZhangR.HanX.KangK.A.PiaoM.J.MaengY.H.ChangW.Y.HyunJ.W.Involvement of glutathione and glutathione metabolizing enzymes in human colorectal cancer cell lines and tissuesMol. Med. Rep2015124314431910.3892/mmr.2015.390226059756Search in Google Scholar
Nguyen A., Loo J.M., Mital R., Weinberg E.M., Man F.Y., Zeng Z., Paty P.B., Saltz L., Janjigian Y.Y., de Stanchina E., Tavazoie S.F.: PKLR promotes colorectal cancer liver colonization through induction of glutathione synthesis. J. Clin. Invest., 2016; 126: 681-694NguyenA.LooJ.M.MitalR.WeinbergE.M.ManF.Y.ZengZ.PatyP.B.SaltzL.JanjigianY.Y.de StanchinaE.TavazoieS.F.PKLR promotes colorectal cancer liver colonization through induction of glutathione synthesisJ. Clin. Invest201612668169410.1172/JCI83587473116526784545Search in Google Scholar
Sun J., Zhou C., Ma Q., Chen W., Atyah M., Yin Y., Fu P., Liu S., Hu B., Ren N., Zhou H.: High GCLC level in tumor tissues is associated with poor prognosis of hepatocellular carcinoma after curative resection. J. Cancer., 2019; 10: 3333-3343SunJ.ZhouC.MaQ.ChenW.AtyahM.YinY.FuP.LiuS.HuB.RenN.ZhouH.High GCLC level in tumor tissues is associated with poor prognosis of hepatocellular carcinoma after curative resectionJ. Cancer2019103333334310.7150/jca.29769660342431293636Search in Google Scholar
Fiorillo M., Sotgia F., Sisci D., Cappello A.R., Lisanti M.P.: Mitochondrial “power” drives tamoxifen resistance: NQO1 and GCLC are new therapeutic targets in breast cancer. Oncotarget, 2017; 8: 20309-20327FiorilloM.SotgiaF.SisciD.CappelloA.R.LisantiM.P.Mitochondrial “power” drives tamoxifen resistance: NQO1 and GCLC are new therapeutic targets in breast cancerOncotarget20178203092032710.18632/oncotarget.15852538676428411284Search in Google Scholar
Hiyama N., Ando T., Maemura K., Sakatani T., Amano Y., Watanabe K., Kage H., Yatomi Y., Nagase T., Nakajima J., Takai D.: Glutamate-cysteine ligase catalytic subunit is associated with cisplatin resistance in lung adenocarcinoma. Jpn. J. Clin. Oncol., 2018; 48: 303-307HiyamaN.AndoT.MaemuraK.SakataniT.AmanoY.WatanabeK.KageH.YatomiY.NagaseT.NakajimaJ.TakaiD.Glutamate-cysteine ligase catalytic subunit is associated with cisplatin resistance in lung adenocarcinomaJpn. J. Clin. Oncol20184830330710.1093/jjco/hyy013589286029474642Search in Google Scholar
Lin L.C., Chen C.F., Ho C.T., Liu J.J., Liu T.Z., Chern C.L.: γ-Glutamylcysteine synthetase (γ-GCS) as a target for overcoming chemo- and radio-resistance of human hepatocellular carcinoma cells. Life Sci., 2018; 198: 25-31LinL.C.ChenC.F.HoC.T.LiuJ.J.LiuT.Z.ChernC.L.γ-Glutamylcysteine synthetase (γ-GCS) as a target for overcoming chemo- and radio-resistance of human hepatocellular carcinoma cellsLife Sci2018198253110.1016/j.lfs.2018.02.01529549912Search in Google Scholar
Liu C.W., Hua K.T., Li K.C., Kao H.F., Hong R.L., Ko J.Y., Hsiao M., Kuo M.L., Tan C.T.: Histone methyltransferase G9a drives chemotherapy resistance by regulating the glutamate-cysteine ligase catalytic subunit in head and neck squamous cell carcinoma. Mol. Cancer Ther., 2017; 16: 1421-1434LiuC.W.HuaK.T.LiK.C.KaoH.F.HongR.L.KoJ.Y.HsiaoM.KuoM.L.TanC.T.Histone methyltransferase G9a drives chemotherapy resistance by regulating the glutamate-cysteine ligase catalytic subunit in head and neck squamous cell carcinomaMol. Cancer Ther2017161421143410.1158/1535-7163.MCT-16-0567-T28265008Search in Google Scholar
Nowakowska A., Tarasiuk J.: Invasion and metastasis of tumour cells resistant to chemotherapy. Postępy Hig. Med. Dośw., 2017; 71: 380-397NowakowskaA.TarasiukJ.Invasion and metastasis of tumour cells resistant to chemotherapyPostępy Hig. Med. Dośw20177138039710.5604/01.3001.0010.382228513462Search in Google Scholar
Almusafri F., Elamin H.E., Khalaf T.E., Ali A., Ben-Omran T., El-Hattab A.W.: Clinical and molecular characterization of 6 children with glutamate-cysteine ligase deficiency causing hemolytic anemia. Blood Cells Mol. Dis., 2017; 65: 73-77AlmusafriF.ElaminH.E.KhalafT.E.AliA.Ben-OmranT.El-HattabA.W.Clinical and molecular characterization of 6 children with glutamate-cysteine ligase deficiency causing hemolytic anemiaBlood Cells Mol. Dis201765737710.1016/j.bcmd.2017.05.01128571779Search in Google Scholar
Chen Y., Johansson E., Yang Y., Miller M.L., Shen D., Orlicky D.J., Shertzer H.G., Vasiliou V., Nebert D.W., Dalton T.P.: Oral N-acetylcysteine rescues lethality of hepatocyte-specific Gclcknockout mice, providing a model for hepatic cirrhosis. J. Hepatol., 2010; 53: 1085-1094ChenY.JohanssonE.YangY.MillerM.L.ShenD.OrlickyD.J.ShertzerH.G.VasiliouV.NebertD.W.DaltonT.P.Oral N-acetylcysteine rescues lethality of hepatocyte-specific Gclcknockout mice, providing a model for hepatic cirrhosisJ. Hepatol2010531085109410.1016/j.jhep.2010.05.028297066320810184Search in Google Scholar
Rushworth G.F., Megson I.L.: Existing and potential therapeutic uses for N-acetylcysteine: The need for conversion to intracellular glutathione for antioxidant benefits. Pharmacol. Ther., 2014; 141: 150-159RushworthG.F.MegsonI.L.Existing and potential therapeutic uses for N-acetylcysteine: The need for conversion to intracellular glutathione for antioxidant benefitsPharmacol. Ther201414115015910.1016/j.pharmthera.2013.09.00624080471Search in Google Scholar
Witschi A., Reddy S., Stofer B., Lauterburg B.H.: The systemic availability of oral glutathione. Eur. J. Clin. Pharmacol., 1992; 43: 667-669WitschiA.ReddyS.StoferB.LauterburgB.H.The systemic availability of oral glutathioneEur. J. Clin. Pharmacol19924366766910.1007/BF022849711362956Search in Google Scholar
Levy E.J., Anderson M.E., Meister A.: Transport of glutathione diethyl ester into human cells. Proc. Natl. Acad. Sci. USA, 1993; 90: 9171-9175LevyE.J.AndersonM.E.MeisterA.Transport of glutathione diethyl ester into human cellsProc. Natl. Acad. Sci. USA1993909171917510.1073/pnas.90.19.9171475248415673Search in Google Scholar
Du K., Ramachandran A., Jaeschke H.: Oxidative stress during acetaminophen hepatotoxicity: Sources, pathophysiological role and therapeutic potential. Redox Biol. 2016; 10: 148-156DuK.RamachandranA.JaeschkeH.Oxidative stress during acetaminophen hepatotoxicity: Sources, pathophysiological role and therapeutic potentialRedox Biol20161014815610.1016/j.redox.2016.10.001506564527744120Search in Google Scholar
Quintana-Cabrera R., Fernandez-Fernandez S., Bobo-Jimenez V., Escobar J., Sastre J., Almeida A., Bolaños J.P.: γ-Glutamylcysteine detoxifies reactive oxygen species by acting as glutathione peroxidase-1 cofactor. Nat. Commun., 2012; 3: 718Quintana-CabreraR.Fernandez-FernandezS.Bobo-JimenezV.EscobarJ.SastreJ.AlmeidaA.BolañosJ.P.γ-Glutamylcysteine detoxifies reactive oxygen species by acting as glutathione peroxidase-1 cofactorNat. Commun2012371810.1038/ncomms1722331687722395609Search in Google Scholar
Chandler S.D., Zarka M.H., Vinaya Babu S.N., Suhas Y.S., Raghunatha Reddy K.R., Bridge W.J.: Safety assessment of gammaglutamylcysteine sodium salt. Regul. Toxicol. Pharmacol., 2012; 64: 17-25ChandlerS.D.ZarkaM.H.VinayaBabu S.N.SuhasY.S.RaghunathaReddy K.R.BridgeW.J.Safety assessment of gammaglutamylcysteine sodium saltRegul. Toxicol. Pharmacol201264172510.1016/j.yrtph.2012.05.00822698997Search in Google Scholar
Kobayashi H., Kurokawa T., Kitahara S., Nonami T., Harada A., Nakao A., Sugiyama S., Ozawa T., Takagi H.: The effects of gamma-glutamylcysteine ethyl ester, a prodrug of glutathione, on ischemia-reperfusion-induced liver injury in rats. Transplantation, 1992; 54: 414-418KobayashiH.KurokawaT.KitaharaS.NonamiT.HaradaA.NakaoA.SugiyamaS.OzawaT.TakagiH.The effects of gamma-glutamylcysteine ethyl ester, a prodrug of glutathione, on ischemia-reperfusion-induced liver injury in ratsTransplantation19925441441810.1097/00007890-199209000-000051412719Search in Google Scholar
Le T.M., Jiang H., Cunningham G.R., Magarik J.A., Barge W.S., Cato M.C., Farina M., Rocha J.B., Milatovic D., Lee E. i wsp.: γ-Glutamylcysteine ameliorates oxidative injury in neurons and astrocytes in vitro and increases brain glutathione in vivo. Neurotoxicology, 2011; 32: 518-525LeT.M.JiangH.CunninghamG.R.MagarikJ.A.BargeW.S.CatoM.C.FarinaM.RochaJ.B.MilatovicD.LeeE. i wsp.γ-Glutamylcysteine ameliorates oxidative injury in neurons and astrocytes in vitro and increases brain glutathione in vivoNeurotoxicology20113251852510.1016/j.neuro.2010.11.008307979221159318Search in Google Scholar
Yang Y., Li L., Hang Q., Fang Y., Dong X., Cao P., Yin Z., Luo L.: γ-glutamylcysteine exhibits anti-inflammatory effects by increasing cellular glutathione level. Redox Biol., 2019; 20: 157-166YangY.LiL.HangQ.FangY.DongX.CaoP.YinZ.LuoL.γ-glutamylcysteine exhibits anti-inflammatory effects by increasing cellular glutathione levelRedox Biol20192015716610.1016/j.redox.2018.09.019619743830326393Search in Google Scholar
Salama S.A., Arab H.H., Hassan M.H., Al Robaian M.M., Maghrabi I.A.: Cadmium-induced hepatocellular injury: Modulatory effects of γ-glutamyl cysteine on the biomarkers of inflammation, DNA damage, and apoptotic cell death. J. Trace. Elem. Med. Biol., 2019; 52: 74-82SalamaS.A.ArabH.H.HassanM.H.AlRobaian M.M.MaghrabiI.A.Cadmium-induced hepatocellular injury: Modulatory effects of γ-glutamyl cysteine on the biomarkers of inflammation, DNA damage, and apoptotic cell deathJ. Trace. Elem. Med. Biol201952748210.1016/j.jtemb.2018.12.00330732903Search in Google Scholar
Salama S.A., Arab H.H., Maghrabi I.A., Hassan M.H., AlSaeed M.S.: Gamma-glutamyl cysteine attenuates tissue damage and enhances tissue regeneration in a rat model of lead-induced nephrotoxicity. Biol. Trace Elem. Res., 2016; 173: 96-107SalamaS.A.ArabH.H.MaghrabiI.A.HassanM.H.AlSaeedM.S.Gamma-glutamyl cysteine attenuates tissue damage and enhances tissue regeneration in a rat model of lead-induced nephrotoxicityBiol. Trace Elem. Res20161739610710.1007/s12011-016-0624-426767370Search in Google Scholar