메뉴 건너뛰기




Volumn 527, Issue , 2013, Pages 129-144

Glutathione and γ-glutamylcysteine in hydrogen peroxide detoxification

Author keywords

[No Author keywords available]

Indexed keywords

BUFFER; GAMMA GLUTAMYLCYSTEINE; GLUTATHIONE; HYDROGEN PEROXIDE;

EID: 84879859448     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/B978-0-12-405882-8.00007-6     Document Type: Chapter
Times cited : (24)

References (46)
  • 1
    • 79951518607 scopus 로고    scopus 로고
    • Molecular targets of oxidative stress
    • S.V. Avery Molecular targets of oxidative stress The Biochemical Journal 434 2011 201 210
    • (2011) The Biochemical Journal , vol.434 , pp. 201-210
    • Avery, S.V.1
  • 2
    • 0018408230 scopus 로고
    • Purification and properties of glutathione peroxidase from human placenta
    • Y.C. Awasthi, D.D. Dao, A.K. Lal, and S.K. Srivastava Purification and properties of glutathione peroxidase from human placenta The Biochemical Journal 177 1979 471 476
    • (1979) The Biochemical Journal , vol.177 , pp. 471-476
    • Awasthi, Y.C.1    Dao, D.D.2    Lal, A.K.3    Srivastava, S.K.4
  • 5
    • 59249096240 scopus 로고    scopus 로고
    • Redox-sensitive green fluorescent protein: Probes for dynamic intracellular redox responses. A review
    • M.B. Cannon, and S.J. Remington Redox-sensitive green fluorescent protein: Probes for dynamic intracellular redox responses. A review Methods in Molecular Biology 476 2008 51 65
    • (2008) Methods in Molecular Biology , vol.476 , pp. 51-65
    • Cannon, M.B.1    Remington, S.J.2
  • 6
    • 0017659867 scopus 로고
    • Purification by affinity chromatography of yeast glutathione reductase, the enzyme responsible for the NADPH-dependent reduction of the mixed disulfide of coenzyme A and glutathione
    • I. Carlberg, and B. Mannervik Purification by affinity chromatography of yeast glutathione reductase, the enzyme responsible for the NADPH-dependent reduction of the mixed disulfide of coenzyme A and glutathione Biochimica et Biophysica Acta 484 1977 268 274
    • (1977) Biochimica et Biophysica Acta , vol.484 , pp. 268-274
    • Carlberg, I.1    Mannervik, B.2
  • 8
    • 34648813720 scopus 로고    scopus 로고
    • ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis
    • B. D'Autreaux, and M.B. Toledano ROS as signalling molecules: Mechanisms that generate specificity in ROS homeostasis Nature Reviews. Molecular Cell Biology 8 2007 813 824
    • (2007) Nature Reviews. Molecular Cell Biology , vol.8 , pp. 813-824
    • D'Autreaux, B.1    Toledano, M.B.2
  • 10
    • 0037097270 scopus 로고    scopus 로고
    • Elevation of brain glutathione by gamma-glutamylcysteine ethyl ester protects against peroxynitrite-induced oxidative stress
    • J. Drake, J. Kanski, S. Varadarajan, M. Tsoras, and D.A. Butterfield Elevation of brain glutathione by gamma-glutamylcysteine ethyl ester protects against peroxynitrite-induced oxidative stress Journal of Neuroscience Research 68 2002 776 784
    • (2002) Journal of Neuroscience Research , vol.68 , pp. 776-784
    • Drake, J.1    Kanski, J.2    Varadarajan, S.3    Tsoras, M.4    Butterfield, D.A.5
  • 11
    • 0034672943 scopus 로고    scopus 로고
    • Metabolism and functions of glutathione in brain
    • R. Dringen Metabolism and functions of glutathione in brain Progress in Neurobiology 62 2000 649 671
    • (2000) Progress in Neurobiology , vol.62 , pp. 649-671
    • Dringen, R.1
  • 12
    • 0033899176 scopus 로고    scopus 로고
    • Glutathione metabolism in brain metabolic interaction between astrocytes and neurons in the defense against reactive oxygen species
    • R. Dringen, J.M. Gutterer, and J. Hirrlinger Glutathione metabolism in brain metabolic interaction between astrocytes and neurons in the defense against reactive oxygen species European Journal of Biochemistry 267 2000 4912 4916
    • (2000) European Journal of Biochemistry , vol.267 , pp. 4912-4916
    • Dringen, R.1    Gutterer, J.M.2    Hirrlinger, J.3
  • 13
    • 0031004608 scopus 로고    scopus 로고
    • The gamma-glutamyl transpeptidase inhibitor acivicin preserves glutathione released by astroglial cells in culture
    • R. Dringen, O. Kranich, and B. Hamprecht The gamma-glutamyl transpeptidase inhibitor acivicin preserves glutathione released by astroglial cells in culture Neurochemical Research 22 1997 727 733
    • (1997) Neurochemical Research , vol.22 , pp. 727-733
    • Dringen, R.1    Kranich, O.2    Hamprecht, B.3
  • 14
    • 0031808935 scopus 로고    scopus 로고
    • Detoxification of exogenous hydrogen peroxide and organic hydroperoxides by cultured astroglial cells assessed by microtiter plate assay
    • R. Dringen, L. Kussmaul, and B. Hamprecht Detoxification of exogenous hydrogen peroxide and organic hydroperoxides by cultured astroglial cells assessed by microtiter plate assay Brain Research. Brain Research Protocols 2 1998 223 228
    • (1998) Brain Research. Brain Research Protocols , vol.2 , pp. 223-228
    • Dringen, R.1    Kussmaul, L.2    Hamprecht, B.3
  • 17
    • 0036570575 scopus 로고    scopus 로고
    • Determination of glutamate-cysteine ligase (gamma-glutamylcysteine synthetase) activity by high-performance liquid chromatography and electrochemical detection
    • M.E. Gegg, J.B. Clark, and S.J. Heales Determination of glutamate-cysteine ligase (gamma-glutamylcysteine synthetase) activity by high-performance liquid chromatography and electrochemical detection Analytical Biochemistry 304 2002 26 32
    • (2002) Analytical Biochemistry , vol.304 , pp. 26-32
    • Gegg, M.E.1    Clark, J.B.2    Heales, S.J.3
  • 18
    • 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 gamma-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 gamma-glutamylcysteine Molecular Biology of the Cell 8 1997 1699 1707
    • (1997) Molecular Biology of the Cell , vol.8 , pp. 1699-1707
    • Grant, C.M.1    Maciver, F.H.2    Dawes, I.W.3
  • 19
    • 0020444895 scopus 로고
    • Mechanism of action, metabolism, and toxicity of buthionine sulfoximine and its higher homologs, potent inhibitors of glutathione synthesis
    • O.W. Griffith Mechanism of action, metabolism, and toxicity of buthionine sulfoximine and its higher homologs, potent inhibitors of glutathione synthesis The Journal of Biological Chemistry 257 1982 13704 13712
    • (1982) The Journal of Biological Chemistry , vol.257 , pp. 13704-13712
    • Griffith, O.W.1
  • 21
    • 0019023638 scopus 로고
    • Excretion of cysteine and gamma-glutamylcysteine moieties in human and experimental animal gamma-glutamyl transpeptidase deficiency
    • O.W. Griffith, and A. Meister Excretion of cysteine and gamma-glutamylcysteine moieties in human and experimental animal gamma-glutamyl transpeptidase deficiency Proceedings of the National Academy of Sciences of the United States of America 77 1980 3384 3387
    • (1980) Proceedings of the National Academy of Sciences of the United States of America , vol.77 , pp. 3384-3387
    • Griffith, O.W.1    Meister, A.2
  • 22
  • 25
    • 0022065342 scopus 로고
    • A leader peptide is sufficient to direct mitochondrial import of a chimeric protein
    • A.L. Horwich, F. Kalousek, I. Mellman, and L.E. Rosenberg A leader peptide is sufficient to direct mitochondrial import of a chimeric protein The EMBO Journal 4 1985 1129 1135
    • (1985) The EMBO Journal , vol.4 , pp. 1129-1135
    • Horwich, A.L.1    Kalousek, F.2    Mellman, I.3    Rosenberg, L.E.4
  • 27
    • 79959985854 scopus 로고    scopus 로고
    • Gamma-glutamylcysteine ethyl ester protects cerebral endothelial cells during injury and decreases blood-brain barrier permeability after experimental brain trauma
    • J. Lok, W. Leung, S. Zhao, S. Pallast, L.K. van, and S. Guo Gamma-glutamylcysteine ethyl ester protects cerebral endothelial cells during injury and decreases blood-brain barrier permeability after experimental brain trauma Journal of Neurochemistry 118 2011 248 255
    • (2011) Journal of Neurochemistry , vol.118 , pp. 248-255
    • Lok, J.1    Leung, W.2    Zhao, S.3    Pallast, S.4    Van L., K.5    Guo, S.6
  • 28
    • 0023522192 scopus 로고
    • Characterization of the major hydroperoxide-reducing activity of human plasma. Purification and properties of a selenium-dependent glutathione peroxidase
    • K.R. Maddipati, and L.J. Marnett Characterization of the major hydroperoxide-reducing activity of human plasma. Purification and properties of a selenium-dependent glutathione peroxidase The Journal of Biological Chemistry 262 1987 17398 17403
    • (1987) The Journal of Biological Chemistry , vol.262 , pp. 17398-17403
    • Maddipati, K.R.1    Marnett, L.J.2
  • 30
    • 0014429143 scopus 로고
    • Purification and subunit structure of glutathione reductase from bakers' yeast
    • R.D. Mavis, and E. Stellwagen Purification and subunit structure of glutathione reductase from bakers' yeast The Journal of Biological Chemistry 243 1968 809 814
    • (1968) The Journal of Biological Chemistry , vol.243 , pp. 809-814
    • Mavis, R.D.1    Stellwagen, E.2
  • 31
    • 0025572626 scopus 로고
    • 2 +/calmodulin-dependent nitric oxide synthase from porcine cerebellum. Cofactor role of tetrahydrobiopterin
    • 2 +/calmodulin-dependent nitric oxide synthase from porcine cerebellum. Cofactor role of tetrahydrobiopterin FEBS Letters 277 1990 215 219
    • (1990) FEBS Letters , vol.277 , pp. 215-219
    • Mayer, B.1    John, M.2    Bohme, E.3
  • 32
    • 0014691242 scopus 로고
    • Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein)
    • J.M. McCord, and I. Fridovich Superoxide dismutase. An enzymic function for erythrocuprein (hemocuprein) The Journal of Biological Chemistry 244 1969 6049 6055
    • (1969) The Journal of Biological Chemistry , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, I.2
  • 33
    • 0000485273 scopus 로고
    • The purification and properties of glutathione peroxidase of erythrocytes
    • G.C. Mills The purification and properties of glutathione peroxidase of erythrocytes The Journal of Biological Chemistry 234 1959 502 506
    • (1959) The Journal of Biological Chemistry , vol.234 , pp. 502-506
    • Mills, G.C.1
  • 34
    • 40449114628 scopus 로고    scopus 로고
    • Evaluation of BEH C18, BEH HILIC, and HSS T3 (C18) column chemistries for the UPLC-MS-MS analysis of glutathione, glutathione disulfide, and ophthalmic acid in mouse liver and human plasma
    • L.S. New, and E.C. Chan Evaluation of BEH C18, BEH HILIC, and HSS T3 (C18) column chemistries for the UPLC-MS-MS analysis of glutathione, glutathione disulfide, and ophthalmic acid in mouse liver and human plasma Journal of Chromatographic Science 46 2008 209 214
    • (2008) Journal of Chromatographic Science , vol.46 , pp. 209-214
    • New, L.S.1    Chan, E.C.2
  • 36
    • 0019447626 scopus 로고
    • Rapid microassays for the measurement of superoxide and hydrogen peroxide production by macrophages in culture using an automatic enzyme immunoassay reader
    • E. Pick, and D. Mizel Rapid microassays for the measurement of superoxide and hydrogen peroxide production by macrophages in culture using an automatic enzyme immunoassay reader Journal of Immunological Methods 46 1981 211 226
    • (1981) Journal of Immunological Methods , vol.46 , pp. 211-226
    • Pick, E.1    Mizel, D.2
  • 38
    • 0028344781 scopus 로고
    • A fluorimetric assay for hydrogen peroxide, suitable for NAD(P)H-dependent superoxide generating redox systems
    • R. Rapoport, I. Hanukoglu, and D. Sklan A fluorimetric assay for hydrogen peroxide, suitable for NAD(P)H-dependent superoxide generating redox systems Analytical Biochemistry 218 1994 309 313
    • (1994) Analytical Biochemistry , vol.218 , pp. 309-313
    • Rapoport, R.1    Hanukoglu, I.2    Sklan, D.3
  • 39
    • 77955048966 scopus 로고    scopus 로고
    • Methods for detection and measurement of hydrogen peroxide inside and outside of cells
    • S.G. Rhee, T.S. Chang, W. Jeong, and D. Kang Methods for detection and measurement of hydrogen peroxide inside and outside of cells Molecules and Cells 29 2010 539 549
    • (2010) Molecules and Cells , vol.29 , pp. 539-549
    • Rhee, S.G.1    Chang, T.S.2    Jeong, W.3    Kang, D.4
  • 40
    • 0036881444 scopus 로고    scopus 로고
    • Glutathione synthetase deficiency: Is gamma-glutamylcysteine accumulation a way to cope with oxidative stress in cells with insufficient levels of glutathione?
    • E. Ristoff, C. Hebert, R. Njalsson, S. Norgren, O. Rooyackers, and A. Larsson Glutathione synthetase deficiency: Is gamma-glutamylcysteine accumulation a way to cope with oxidative stress in cells with insufficient levels of glutathione? Journal of Inherited Metabolic Disease 25 2002 577 584
    • (2002) Journal of Inherited Metabolic Disease , vol.25 , pp. 577-584
    • Ristoff, E.1    Hebert, C.2    Njalsson, R.3    Norgren, S.4    Rooyackers, O.5    Larsson, A.6
  • 41
    • 84855948520 scopus 로고    scopus 로고
    • Dynamic measurements of mitochondrial hydrogen peroxide concentration and glutathione redox state in rat pancreatic beta-cells using ratiometric fluorescent proteins: Confounding effects of pH with HyPer but not roGFP1
    • L.P. Roma, J. Duprez, H.K. Takahashi, P. Gilon, A. Wiederkehr, and J.C. Jonas Dynamic measurements of mitochondrial hydrogen peroxide concentration and glutathione redox state in rat pancreatic beta-cells using ratiometric fluorescent proteins: Confounding effects of pH with HyPer but not roGFP1 The Biochemical Journal 441 2012 971 978
    • (2012) The Biochemical Journal , vol.441 , pp. 971-978
    • Roma, L.P.1    Duprez, J.2    Takahashi, H.K.3    Gilon, P.4    Wiederkehr, A.5    Jonas, J.C.6
  • 42
    • 0033525924 scopus 로고    scopus 로고
    • Oxidative phosphorylation at the fin de siecle
    • M. Saraste Oxidative phosphorylation at the fin de siecle Science 283 1999 1488 1493
    • (1999) Science , vol.283 , pp. 1488-1493
    • Saraste, M.1
  • 43
    • 72649102227 scopus 로고    scopus 로고
    • Catalytic mechanisms and specificities of glutathione peroxidases: Variations of a basic scheme
    • S. Toppo, L. Flohe, F. Ursini, S. Vanin, and M. Maiorino Catalytic mechanisms and specificities of glutathione peroxidases: Variations of a basic scheme Biochimica et Biophysica Acta 1790 2009 1486 1500
    • (2009) Biochimica et Biophysica Acta , vol.1790 , pp. 1486-1500
    • Toppo, S.1    Flohe, L.2    Ursini, F.3    Vanin, S.4    Maiorino, M.5
  • 44
    • 0021221671 scopus 로고
    • Direct measurement of hydrogen peroxide release from rat alveolar macrophages: Artifactual effect of horseradish peroxidase
    • M.R. Van Scott, P.R. Miles, and V. Castranova Direct measurement of hydrogen peroxide release from rat alveolar macrophages: Artifactual effect of horseradish peroxidase Experimental Lung Research 6 1984 103 114
    • (1984) Experimental Lung Research , vol.6 , pp. 103-114
    • Van Scott, M.R.1    Miles, P.R.2    Castranova, V.3
  • 45
    • 0035097462 scopus 로고    scopus 로고
    • Depletion of glutathione up-regulates mitochondrial complex i expression in glial cells
    • O.L. Vasquez, A. Almeida, and J.P. Bolanos Depletion of glutathione up-regulates mitochondrial complex I expression in glial cells Journal of Neurochemistry 76 2001 1593 1596
    • (2001) Journal of Neurochemistry , vol.76 , pp. 1593-1596
    • Vasquez, O.L.1    Almeida, A.2    Bolanos, J.P.3
  • 46
    • 0022893844 scopus 로고
    • Stability of NADPH: Effect of various factors on the kinetics of degradation
    • J.T. Wu, L.H. Wu, and J.A. Knight Stability of NADPH: Effect of various factors on the kinetics of degradation Clinical Chemistry 32 1986 314 319
    • (1986) Clinical Chemistry , vol.32 , pp. 314-319
    • Wu, J.T.1    Wu, L.H.2    Knight, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.