메뉴 건너뛰기




Volumn 41, Issue 1, 2013, Pages 106-110

Glutathione and γ-glutamylcysteine in the antioxidant and survival functions of mitochondria

Author keywords

glutamylcysteine; Glutathione; Mitochondrion; Reactive oxygen species

Indexed keywords

ANTIOXIDANT; GAMMA GLUTAMYLCYSTEINE; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; GLUTATHIONE PEROXIDASE 1; GLUTATHIONE TRANSFERASE; MANGANESE PEROXIDASE; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; NITRIC OXIDE; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; S NITROSOGLUTATHIONE;

EID: 84873182560     PISSN: 03005127     EISSN: 14708752     Source Type: Journal    
DOI: 10.1042/BST20120252     Document Type: Conference Paper
Times cited : (39)

References (48)
  • 1
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy, M. P. (2009) How mitochondria produce reactive oxygen species. Biochem. J. 417, 1-13
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 2
    • 79959354999 scopus 로고    scopus 로고
    • Mitochondria and the autophagy-inflammation-cell death axis in organismal aging
    • Green, D. R., Galluzzi, L. and Kroemer, G (2011) Mitochondria and the autophagy-inflammation-cell death axis in organismal aging. Science 333, 1109-1112
    • (2011) Science , vol.333 , pp. 1109-1112
    • Green, D.R.1    Galluzzi, L.2    Kroemer, G.3
  • 3
    • 69849097192 scopus 로고    scopus 로고
    • Mitochondrial generation of free radicals and hypoxic signaling
    • Poyton, R. O., Ball, K. A. and Castello, P. R. (2009) Mitochondrial generation of free radicals and hypoxic signaling. Trends Endocrinol. Metab. 20, 332-340
    • (2009) Trends Endocrinol. Metab. , vol.20 , pp. 332-340
    • Poyton, R.O.1    Ball, K.A.2    Castello, P.R.3
  • 4
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
    • DOI 10.1038/nrm2256, PII NRM2256
    • D'Autreaux, B and Toledano, M. B. (2007) ROS as signalling molecules: mechanisms that generate specificity in ROS homeostasis. Nat. Rev. Mol. Cell Biol. 8, 813-824 (Pubitemid 47462134)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.10 , pp. 813-824
    • D'Autreaux, B.1    Toledano, M.B.2
  • 5
    • 77952541558 scopus 로고    scopus 로고
    • The sites and topology of mitochondrial superoxide production
    • Brand, M. D. (2010) The sites and topology of mitochondrial superoxide production. Exp. Gerontol. 45, 466-472
    • (2010) Exp. Gerontol. , vol.45 , pp. 466-472
    • Brand, M.D.1
  • 6
    • 20444415235 scopus 로고    scopus 로고
    • Complex cellular responses to reactive oxygen species
    • DOI 10.1016/j.tcb.2005.04.003, PII S0962892405001029
    • Temple, M. D., Perrone, G. G. and Dawes, I. W. (2005) Complex cellular responses to reactive oxygen species. Trends Cell Biol. 15, 319-326 (Pubitemid 40805328)
    • (2005) Trends in Cell Biology , vol.15 , Issue.6 , pp. 319-326
    • Temple, M.D.1    Perrone, G.G.2    Dawes, I.W.3
  • 7
    • 72649102227 scopus 로고    scopus 로고
    • Catalytic mechanisms and specificities of glutathione peroxidases: Variations of a basic scheme
    • Toppo, S., Flohe, L., Ursini, F., Vanin, S. and Maiorino, M. (2009) Catalytic mechanisms and specificities of glutathione peroxidases: variations of a basic scheme. Biochim. Biophys. Acta 1790, 1486-1500
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 1486-1500
    • Toppo, S.1    Flohe, L.2    Ursini, F.3    Vanin, S.4    Maiorino, M.5
  • 10
    • 4344587626 scopus 로고    scopus 로고
    • Free aminothiols, glutathione redox state and protein mixed disulphides in aging Drosophila melanogaster
    • DOI 10.1042/BJ20040506
    • Rebrin, I., Bayne, A. C., Mockett, R. J., Orr, W. C. and Sohal, R. S. (2004) Free aminothiols, glutathione redox state and protein mixed disulphides in aging Drosophila melanogaster. Biochem. J. 382, 131-136 (Pubitemid 39141574)
    • (2004) Biochemical Journal , vol.382 , Issue.1 , pp. 131-136
    • Rebrin, I.1    Bayne, A.-C.V.2    Mockett, R.J.3    Orr, W.C.4    Sohal, R.S.5
  • 11
    • 0034672943 scopus 로고    scopus 로고
    • Metabolism and functions of glutathione in brain
    • DOI 10.1016/S0301-0082(99)00060-X, PII S030100829900060X
    • Dringen, R. (2000) Metabolism and functions of glutathione in brain. Prog. Neurobiol. 62, 649-671 (Pubitemid 30407139)
    • (2000) Progress in Neurobiology , vol.62 , Issue.6 , pp. 649-671
    • Dringen, R.1
  • 12
    • 1542376929 scopus 로고    scopus 로고
    • Glutathione metabolism and its implications for health
    • Wu, G., Fang, Y. Z., Yang, S., Lupton, J. R. and Turner, N. D. (2004) Glutathione metabolism and its implications for health. J. Nutr. 134, 489-492 (Pubitemid 38298485)
    • (2004) Journal of Nutrition , vol.134 , Issue.3 , pp. 489-492
    • Wu, G.1    Fang, Y.-Z.2    Yang, S.3    Lupton, J.R.4    Turner, N.D.5
  • 13
    • 24344452154 scopus 로고    scopus 로고
    • Glutathione synthetase deficiency
    • DOI 10.1007/s00018-005-5163-7
    • Njalsson, R. (2005) Glutathione synthetase deficiency. Cell. Mol. Life Sci. 62, 1938-1945 (Pubitemid 41261841)
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.17 , pp. 1938-1945
    • Njalsson, R.1
  • 14
    • 5344280431 scopus 로고    scopus 로고
    • Genetically altered mice to evaluate glutathione homeostasis in health and disease
    • DOI 10.1016/j.freeradbiomed.2004.06.040, PII S0891584904005349
    • Dalton, T. P., Chen, Y., Schneider, S. N., Nebert, D. W. and Shertzer, H. G. (2004) Genetically altered mice to evaluate glutathione homeostasis in health and disease. Free Radical Biol. Med. 37, 1511-1526 (Pubitemid 39349798)
    • (2004) Free Radical Biology and Medicine , vol.37 , Issue.10 , pp. 1511-1526
    • Dalton, T.P.1    Chen, Y.2    Schneider, S.N.3    Nebert, D.W.4    Shertzer, H.G.5
  • 15
    • 65049089113 scopus 로고    scopus 로고
    • Regulation of glutathione synthesis
    • Lu, S. C. (2009) Regulation of glutathione synthesis. Mol. Aspects Med. 30, 42-59
    • (2009) Mol. Aspects Med. , vol.30 , pp. 42-59
    • Lu, S.C.1
  • 16
    • 33750011601 scopus 로고    scopus 로고
    • Mitochondrial glutathione transport: Physiological, pathological and toxicological implications
    • DOI 10.1016/j.cbi.2006.03.001, PII S0009279706000536
    • Lash, L. H. (2006) Mitochondrial glutathione transport: physiological, pathological and toxicological implications. Chem.-Biol. Interact. 163, 54-67 (Pubitemid 44572210)
    • (2006) Chemico-Biological Interactions , vol.163 , Issue.1-2 , pp. 54-67
    • Lash, L.H.1
  • 17
    • 0021327406 scopus 로고
    • Entamoeba histolytica: A eukaryote without glutathione metabolism
    • Fahey, R. C., Newton, G. L., Arrick, B., Overdank-Bogart, T. and Aley, S. B. (1984) Entamoeba histolytica: a eukaryote without glutathione metabolism. Science 224, 70-72 (Pubitemid 14171643)
    • (1984) Science , vol.224 , Issue.4644 , pp. 70-72
    • Fahey, R.C.1    Newton, G.L.2    Arrick, B.3
  • 18
    • 78751578977 scopus 로고    scopus 로고
    • Laboratory evolution of glutathione biosynthesis reveals natural compensatory pathways
    • Veeravalli, K., Boyd, D., Iverson, B. L., Beckwith, J. and Georgiou, G. (2011) Laboratory evolution of glutathione biosynthesis reveals natural compensatory pathways. Nat. Chem. Biol. 7, 101-105
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 101-105
    • Veeravalli, K.1    Boyd, D.2    Iverson, B.L.3    Beckwith, J.4    Georgiou, G.5
  • 20
    • 0034694871 scopus 로고    scopus 로고
    • Knockout of the mouse glutamate cysteine ligase catalytic subunit (Gclc) gene: Embryonic lethal when homozygous, and proposed model for moderate glutathione deficiency when heterozygous
    • DOI 10.1006/bbrc.2000.3930
    • Dalton, T. P., Dieter, M. Z., Yang, Y., Shertzer, H. G. and Nebert, D. W. (2000) Knockout of the mouse glutamate cysteine ligase catalytic subunit (Gclc) gene: embryonic lethal when homozygous, and proposed model for moderate glutathione deficiency when heterozygous. Biochem. Biophys. Res. Commun. 279, 324-329 (Pubitemid 32016716)
    • (2000) Biochemical and Biophysical Research Communications , vol.279 , Issue.2 , pp. 324-329
    • Dalton, T.P.1    Dieter, M.Z.2    Yang, Y.3    Shertzer, H.G.4    Nebert, D.W.5
  • 21
    • 28244459619 scopus 로고    scopus 로고
    • Knockdown of glutamate-cysteine by ligase by small hairpin RNA reveals that both catalytic and modulatory subunits are essential for the survival of primary neurons
    • DOI 10.1074/jbc.M507065200
    • Diaz-Hernandez, J. I., Almeida, A., Delgado-Esteban, M., Fernandez, E. and Bolanos, J. P. (2005) Knockdown of glutamate-cysteine ligase by small hairpin RNA reveals that both catalytic and modulatory subunits are essential for the survival of primary neurons. J. Biol. Chem. 280, 38992-39001 (Pubitemid 41713849)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.47 , pp. 38992-39001
    • Diaz-Hernandez, J.I.1    Almeida, A.2    Delgado-Esteban, M.3    Fernandez, E.4    Bolanos, J.P.5
  • 22
    • 0035844289 scopus 로고    scopus 로고
    • Control of mitochondrial redox balance and cellular defense against oxidative damage by mitochondrial NADP+-dependent isocitrate dehydrogenase
    • Jo, S. H., Son, M. K., Koh, H. J., Lee, S. M., Song, I. H., Kim, Y. O., Lee, Y. S., Jeong, K. S., Kim, W. B., Park, J. W. et al. (2001) Control of mitochondrial redox balance and cellular defense against oxidative damage by mitochondrial NADP+-dependent isocitrate dehydrogenase. J. Biol. Chem. 276, 16168-16176
    • (2001) J. Biol. Chem. , vol.276 , pp. 16168-16176
    • Jo, S.H.1    Son, M.K.2    Koh, H.J.3    Lee, S.M.4    Song, I.H.5    Kim, Y.O.6    Lee, Y.S.7    Jeong, K.S.8    Kim, W.B.9    Park, J.W.10
  • 23
    • 64349086819 scopus 로고    scopus 로고
    • Mitochondrial glutathione uptake: Characterization in isolated brain mitochondria and astrocytes in culture
    • Wadey, A. L., Muyderman, H., Kwek, P. T. and Sims, N. R. (2009) Mitochondrial glutathione uptake: characterization in isolated brain mitochondria and astrocytes in culture. J. Neurochem. 109(Suppl. 1), 101-108
    • (2009) J. Neurochem. , vol.109 , Issue.SUPPL. 1 , pp. 101-108
    • Wadey, A.L.1    Muyderman, H.2    Kwek, P.T.3    Sims, N.R.4
  • 25
    • 35748976238 scopus 로고    scopus 로고
    • Glutathione binding to the Bcl-2 homology-3 domain groove: A molecular basis for BCL-2 antioxidant function at mitochondria
    • DOI 10.1074/jbc.M702853200
    • Zimmermann, A. K., Loucks, F. A., Schroeder, E. K., Bouchard, R. J., Tyler, K. L. and Linseman, D. A. (2007) Glutathione binding to the Bcl-2 homology-3 domain groove: a molecular basis for Bcl-2 antioxidant function at mitochondria. J. Biol. Chem. 282, 29296-29304 (Pubitemid 350043369)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.40 , pp. 29296-29304
    • Zimmermann, A.K.1    Loucks, F.A.2    Schroeder, E.K.3    Bouchard, R.J.4    Tyler, K.L.5    Linseman, D.A.6
  • 26
    • 67349249403 scopus 로고    scopus 로고
    • The bioenergetic and antioxidant status of neurons is controlled by continuous degradation of a key glycolytic enzyme by APC/C-Cdh1
    • Herrero-Mendez, A., Almeida, A., Fernandez, E., Maestre, C., Moncada, S. and Bolanos, J. P. (2009) The bioenergetic and antioxidant status of neurons is controlled by continuous degradation of a key glycolytic enzyme by APC/C-Cdh1. Nat. Cell Biol. 11, 747-752
    • (2009) Nat. Cell Biol. , vol.11 , pp. 747-752
    • Herrero-Mendez, A.1    Almeida, A.2    Fernandez, E.3    Maestre, C.4    Moncada, S.5    Bolanos, J.P.6
  • 28
    • 0036175622 scopus 로고    scopus 로고
    • Impairment of brain mitochondrial function by reactive nitrogen species: The role of glutathione in dictating susceptibility
    • DOI 10.1016/S0197-0186(01)00117-6, PII S0197018601001176
    • Heales, S. J. and Bolanos, J. P. (2002) Impairment of brain mitochondrial function by reactive nitrogen species: the role of glutathione in dictating susceptibility. Neurochem. Int. 40, 469-474 (Pubitemid 34159147)
    • (2002) Neurochemistry International , vol.40 , Issue.6 , pp. 469-474
    • Heales, S.J.R.1    Bolanos, J.P.2
  • 29
    • 4644327947 scopus 로고    scopus 로고
    • Highly selective and prolonged depletion of mitochondrial glutathione in astrocytes markedly increases sensitivity to peroxynitrite
    • DOI 10.1523/JNEUROSCI.1103-04.2004
    • Muyderman, H., Nilsson, M. and Sims, N. R. (2004) Highly selective and prolonged depletion of mitochondrial glutathione in astrocytes markedly increases sensitivity to peroxynitrite. J. Neurosci. 24, 8019-8028 (Pubitemid 39280821)
    • (2004) Journal of Neuroscience , vol.24 , Issue.37 , pp. 8019-8028
    • Muyderman, H.1    Nilsson, M.2    Sims, N.R.3
  • 32
    • 0041845184 scopus 로고    scopus 로고
    • Biochemical and genetic characterization of a murine class Kappa glutathione S-transferase
    • DOI 10.1042/BJ20030415
    • Jowsey, I. R., Thomson, R. E., Orton, T. C., Elcombe, C. R. and Hayes, J. D. (2003) Biochemical and genetic characterization of a murine class Kappa glutathione S-transferase. Biochem. J. 373, 559-569 (Pubitemid 36897858)
    • (2003) Biochemical Journal , vol.373 , Issue.2 , pp. 559-569
    • Jowsey, I.R.1    Thomson, R.E.2    Orton, T.C.3    Elcombe, C.R.4    Hayes, J.D.5
  • 34
    • 78650068036 scopus 로고    scopus 로고
    • Regulation of mitochondrial glutathione redox status and protein glutathionylation by respiratory substrates
    • Garcia, J., Han, D., Sancheti, H., Yap, L. P., Kaplowitz, N. and Cadenas, E. (2010) Regulation of mitochondrial glutathione redox status and protein glutathionylation by respiratory substrates. J. Biol. Chem. 285, 39646-39654
    • (2010) J. Biol. Chem. , vol.285 , pp. 39646-39654
    • Garcia, J.1    Han, D.2    Sancheti, H.3    Yap, L.P.4    Kaplowitz, N.5    Cadenas, E.6
  • 35
    • 49349085256 scopus 로고    scopus 로고
    • Redox compartmentalization in eukaryotic cells
    • Go, Y. M. and Jones, D. P. (2008) Redox compartmentalization in eukaryotic cells. Biochim. Biophys. Acta 1780, 1273-1290
    • (2008) Biochim. Biophys. Acta , vol.1780 , pp. 1273-1290
    • Go, Y.M.1    Jones, D.P.2
  • 36
    • 80054690509 scopus 로고    scopus 로고
    • Mia40-dependent oxidation of cysteines in domain I of Ccs1 controls its distribution between mitochondria and the cytosol
    • Kloppel, C., Suzuki, Y., Kojer, K., Petrungaro, C., Longen, S., Fiedler, S., Keller, S. and Riemer, J. (2011) Mia40-dependent oxidation of cysteines in domain I of Ccs1 controls its distribution between mitochondria and the cytosol. Mol. Biol. Cell 22, 3749-3757
    • (2011) Mol. Biol. Cell , vol.22 , pp. 3749-3757
    • Kloppel, C.1    Suzuki, Y.2    Kojer, K.3    Petrungaro, C.4    Longen, S.5    Fiedler, S.6    Keller, S.7    Riemer, J.8
  • 40
    • 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
    • Grant, C. M., MacIver, F. H. and Dawes, I. W. (1997) 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 β-glutamylcysteine. Mol. Biol. Cell 8, 1699-1707 (Pubitemid 27411135)
    • (1997) Molecular Biology of the Cell , vol.8 , Issue.9 , pp. 1699-1707
    • Grant, C.M.1    MacIver, F.H.2    Dawes, I.W.3
  • 41
    • 0035990307 scopus 로고    scopus 로고
    • Oxidative stress in inborn errors of metabolism: Lessons from glutathione deficiency
    • DOI 10.1023/A:1015634032042
    • Ristoff, E. and Larsson, A. (2002) Oxidative stress in inborn errors of metabolism: lessons from glutathione deficiency. J. Inherit. Metab. Dis. 25, 223-226 (Pubitemid 34700313)
    • (2002) Journal of Inherited Metabolic Disease , vol.25 , Issue.3 , pp. 223-226
    • Ristoff, E.1    Larsson, A.2
  • 44
    • 77149120128 scopus 로고    scopus 로고
    • Mitochondrial disulfide bond formation is driven by intersubunit electron transfer in Erv1 and proofread by glutathione
    • Bien, M., Longen, S., Wagener, N., Chwalla, I., Herrmann, J. M. and Riemer, J. (2010) Mitochondrial disulfide bond formation is driven by intersubunit electron transfer in Erv1 and proofread by glutathione. Mol. Cell 37, 516-528
    • (2010) Mol. Cell , vol.37 , pp. 516-528
    • Bien, M.1    Longen, S.2    Wagener, N.3    Chwalla, I.4    Herrmann, J.M.5    Riemer, J.6
  • 45
    • 33744543755 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae proteome of oxidized protein thiols: Contrasted functions for the thioredoxin and glutathione pathways
    • DOI 10.1074/jbc.M513346200
    • Le, M. N., Clement, G., Le, M. S., Tacnet, F. and Toledano, M. B. (2006) The Saccharomyces cerevisiae proteome of oxidized protein thiols: contrasted functions for the thioredoxin and glutathione pathways. J. Biol. Chem. 281, 10420-10430 (Pubitemid 43864581)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.15 , pp. 10420-10430
    • Le Moan, N.1    Clement, G.2    Le Maout, S.3    Tacnet, F.4    Toledano, M.B.5
  • 46
    • 21844446870 scopus 로고    scopus 로고
    • Glutathione redox state regulates mitochondrial reactive oxygen production
    • DOI 10.1074/jbc.M500095200
    • Shen, D., Dalton, T. P., Nebert, D. W. and Shertzer, H. G. (2005) Glutathione redox state regulates mitochondrial reactive oxygen production. J. Biol. Chem. 280, 25305-25312 (Pubitemid 40962232)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.27 , pp. 25305-25312
    • Shen, D.1    Dalton, T.P.2    Nebert, D.W.3    Shertzer, H.G.4
  • 47
    • 57649183232 scopus 로고    scopus 로고
    • The redox environment in the mitochondrial intermembrane space is maintained separately from the cytosol and matrix
    • Hu, J., Dong, L. and Outten, C. E. (2008) The redox environment in the mitochondrial intermembrane space is maintained separately from the cytosol and matrix. J. Biol. Chem. 283, 29126-29134
    • (2008) J. Biol. Chem. , vol.283 , pp. 29126-29134
    • Hu, J.1    Dong, L.2    Outten, C.E.3
  • 48
    • 77957315403 scopus 로고    scopus 로고
    • Redox compartmentalization and cellular stress
    • Jones, D. P. and Go, Y. M. (2010) Redox compartmentalization and cellular stress. Diabetes, Obes. Metab. 12(Suppl. 2), 116-125
    • (2010) Diabetes, Obes. Metab. , vol.12 , Issue.SUPPL. 2 , pp. 116-125
    • Jones, D.P.1    Go, Y.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.