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Volumn 86, Issue 1, 2003, Pages 228-237

Differential effect of nitric oxide on glutathione metabolism and mitochondrial function in astrocytes and neurones: Implications for neuroprotection/neurodegeneration?

Author keywords

glutamyltranspeptidase; Astrocytes; Glutamate cysteine ligase; Glutathione; Neurones; Nitric oxide

Indexed keywords

1 [(2 AMINOETHYL) N (2 AMMONIOETHYL)AMINO]DIAZEN 1 IUM 1,2 DIOLATE; CYSTEINYLGLYCINE; GAMMA GLUTAMYLTRANSFERASE; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; NITRIC OXIDE; NITRIC OXIDE DONOR; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE DEHYDROGENASE; UNCLASSIFIED DRUG;

EID: 0038308447     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2003.01821.x     Document Type: Article
Times cited : (150)

References (51)
  • 1
    • 0035909948 scopus 로고    scopus 로고
    • Different responses of astrocytes and neurons to nitric oxide: The role of glycolytically generated ATP in astrocyte protection
    • Almeida A., Almeida J., Bolaños J. P. and Moncada S. (2001) Different responses of astrocytes and neurons to nitric oxide: The role of glycolytically generated ATP in astrocyte protection. Proc. Natl Acad. Sci. USA 98, 15294-15299.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 15294-15299
    • Almeida, A.1    Almeida, J.2    Bolaños, J.P.3    Moncada, S.4
  • 2
    • 0029962693 scopus 로고    scopus 로고
    • Glutathione protects from peroxynitrite-mediated mitochondrial damage: Implications for neuronal/astrocytic trafficking and neurodegeneration
    • Barker J. E., Bolanos J. P., Land J. M., Clark J. B. and Heales S. J. R. (1996) Glutathione protects from peroxynitrite-mediated mitochondrial damage: implications for neuronal/astrocytic trafficking and neurodegeneration. Dev. Neurosci. 18, 391-396.
    • (1996) Dev. Neurosci. , vol.18 , pp. 391-396
    • Barker, J.E.1    Bolanos, J.P.2    Land, J.M.3    Clark, J.B.4    Heales, S.J.R.5
  • 3
    • 0034057120 scopus 로고    scopus 로고
    • Oxidative stress and S-nitrosylation of proteins in cells
    • Beltran B., Orsi A., Clementi E. and Moncada S. (2000) Oxidative stress and S-nitrosylation of proteins in cells. Br. J. Pharmacol. 129, 953-960.
    • (2000) Br. J. Pharmacol. , vol.129 , pp. 953-960
    • Beltran, B.1    Orsi, A.2    Clementi, E.3    Moncada, S.4
  • 4
    • 0028145462 scopus 로고
    • Nitric oxide-mediated inhibition of the mitochondrial respiratory chain in cultured astrocytes
    • Bolanos J. P., Peuchen S., Heales S. J. R., Land J. M. and Clark J. B. (1994) Nitric oxide-mediated inhibition of the mitochondrial respiratory chain in cultured astrocytes. J. Neurochem. 63, 910-916.
    • (1994) J. Neurochem. , vol.63 , pp. 910-916
    • Bolanos, J.P.1    Peuchen, S.2    Heales, S.J.R.3    Land, J.M.4    Clark, J.B.5
  • 5
    • 0028952832 scopus 로고
    • Effect of peroxynitrite on the mitochondrial respiratory chain: Differential susceptibility of neurones and astrocytes in primary culture
    • Bolanos J. P., Heales S. J. R., Land J. M. and Clark J. B. (1995) Effect of peroxynitrite on the mitochondrial respiratory chain: Differential susceptibility of neurones and astrocytes in primary culture. J. Neurochem. 64, 1965-1972.
    • (1995) J. Neurochem. , vol.64 , pp. 1965-1972
    • Bolanos, J.P.1    Heales, S.J.R.2    Land, J.M.3    Clark, J.B.4
  • 7
    • 0029033427 scopus 로고
    • Nitric oxide produced by activated astrocytes rapidly and reversibly inhibits cellular respiration
    • Brown G. C., Bolanos J. P., Heales S. J. R. and Clark J. B. (1995) Nitric oxide produced by activated astrocytes rapidly and reversibly inhibits cellular respiration. Neurosci. Lett. 193, 201-204.
    • (1995) Neurosci. Lett. , vol.193 , pp. 201-204
    • Brown, G.C.1    Bolanos, J.P.2    Heales, S.J.R.3    Clark, J.B.4
  • 8
    • 0033989132 scopus 로고    scopus 로고
    • Induction of nitric oxide synthesis lowers intracellular glutathione in microglia of primary glial cultures
    • Chatterjee S., Noack H., Possel H. and Wolf G. (2000) Induction of nitric oxide synthesis lowers intracellular glutathione in microglia of primary glial cultures. Glia 29, 98-101.
    • (2000) Glia , vol.29 , pp. 98-101
    • Chatterjee, S.1    Noack, H.2    Possel, H.3    Wolf, G.4
  • 9
    • 0024459683 scopus 로고
    • Purification of astroglial-cell cultures from rat spinal cord: The use of D-valine to inhibit fibroblast growth
    • Cholewinski A. J., Reid J. C., McDermott A. M. and Wilkin G. P. (1989) Purification of astroglial-cell cultures from rat spinal cord: The use of D-valine to inhibit fibroblast growth. Neurochem. Int. 15, 365-369.
    • (1989) Neurochem. Int. , vol.15 , pp. 365-369
    • Cholewinski, A.J.1    Reid, J.C.2    McDermott, A.M.3    Wilkin, G.P.4
  • 10
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidium thiocyanate phenol chloroform extraction
    • Chomczynski P. and Sacchi N. (1987) Single-step method of RNA isolation by acid guanidium thiocyanate phenol chloroform extraction. Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 11
    • 0032560572 scopus 로고    scopus 로고
    • Persistent inhibition of cell respiration by nitric oxide: Crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione
    • Clementi E., Brown G. C., Feelisch M. and Moncada S. (1998) Persistent inhibition of cell respiration by nitric oxide: Crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione. Proc. Natl Acad. Sci. USA 95, 7631-7636.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 7631-7636
    • Clementi, E.1    Brown, G.C.2    Feelisch, M.3    Moncada, S.4
  • 12
    • 0028091176 scopus 로고
    • Indices of oxidative stress and mitochondrial function in individuals with incidental Lewy body disease
    • Dexter D. T et al. (1994) Indices of oxidative stress and mitochondrial function in individuals with incidental Lewy body disease. Ann. Neurol. 35, 38-44.
    • (1994) Ann. Neurol. , vol.35 , pp. 38-44
    • Dexter, D.T.1
  • 13
    • 0031004608 scopus 로고    scopus 로고
    • The γ-glutamyltranspeptidase inhibitor preserves glutathione released by astroglial cells in culture
    • Dringen R., Kranich O. and Hamprecht B. (1997) The γ-glutamyltranspeptidase inhibitor preserves glutathione released by astroglial cells in culture. Neurochem. Res. 22, 727-733.
    • (1997) Neurochem. Res. , vol.22 , pp. 727-733
    • Dringen, R.1    Kranich, O.2    Hamprecht, B.3
  • 14
    • 0033555806 scopus 로고    scopus 로고
    • Synthesis of the antioxidant glutathione in neurones: Supply by astrocytes of Cys-Gly as precursor for neuronal glutathione
    • Dringen R., Pfeiffer B. and Hamprecht B. (1999) Synthesis of the antioxidant glutathione in neurones: Supply by astrocytes of Cys-Gly as precursor for neuronal glutathione. J. Neurosci. 19, 562-569.
    • (1999) J. Neurosci. , vol.19 , pp. 562-569
    • Dringen, R.1    Pfeiffer, B.2    Hamprecht, B.3
  • 16
    • 0036570575 scopus 로고    scopus 로고
    • Determination of glutamate-cysteine ligase (γ-glutamylcysteine synthetase) activity by high-performance liquid chromatography and electrochemical detection
    • Gegg M. E., Clark J. B. and Heales S. J. R. (2002) Determination of glutamate-cysteine ligase (γ-glutamylcysteine synthetase) activity by high-performance liquid chromatography and electrochemical detection. Anal. Biochem. 304, 26-32.
    • (2002) Anal. Biochem. , vol.304 , pp. 26-32
    • Gegg, M.E.1    Clark, J.B.2    Heales, S.J.R.3
  • 17
    • 0027171195 scopus 로고
    • Catalytic and regulatory properties of the heavy subunit of rat kidney γ-glutamylcysteine synthetase
    • Huang C. S., Chang L. S., Anderson M. E. and Meister A. (1993) Catalytic and regulatory properties of the heavy subunit of rat kidney γ-glutamylcysteine synthetase. J. Biol. Chem. 268, 19675-19680.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19675-19680
    • Huang, C.S.1    Chang, L.S.2    Anderson, M.E.3    Meister, A.4
  • 19
    • 0032973861 scopus 로고    scopus 로고
    • Glial cells protect neurones against oxidative stress via transcriptional upregulation of the glutathione synthesis
    • Iwata-Ichikawa E., Kondo Y., Miyazaki I., Asanuma M. and Ogawa N. (1999) Glial cells protect neurones against oxidative stress via transcriptional upregulation of the glutathione synthesis. J. Neurochem. 72, 2334-2344.
    • (1999) J. Neurochem. , vol.72 , pp. 2334-2344
    • Iwata-Ichikawa, E.1    Kondo, Y.2    Miyazaki, I.3    Asanuma, M.4    Ogawa, N.5
  • 20
    • 0031687793 scopus 로고    scopus 로고
    • Understanding cell death in Parkinson's disease
    • Jenner P. and Olanow C. W. (1998) Understanding cell death in Parkinson's disease. Ann. Neurol. 44, S72-S84.
    • (1998) Ann. Neurol. , vol.44
    • Jenner, P.1    Olanow, C.W.2
  • 21
    • 0036436025 scopus 로고    scopus 로고
    • Peroxynitrite activates NF-E2 related factor 2/antioxidant response element through the pathway of phosphatidylinositol 3-kinase: The role of nitric oxide synthase in rat glutathione S-transferase A2 induction
    • Kang K. W., Choi S. H. and Kim S. G. (2002) Peroxynitrite activates NF-E2 related factor 2/antioxidant response element through the pathway of phosphatidylinositol 3-kinase: The role of nitric oxide synthase in rat glutathione S-transferase A2 induction. Nitric Oxide 7, 244-253.
    • (2002) Nitric Oxide , vol.7 , pp. 244-253
    • Kang, K.W.1    Choi, S.H.2    Kim, S.G.3
  • 22
    • 0030606289 scopus 로고    scopus 로고
    • Different preferences in the utilization of amino acids for glutathione synthesis in cultured neurons and astroglial cells derived from rat brain
    • Kranich O., Hamprecht B. and Dringen R. (1996) Different preferences in the utilization of amino acids for glutathione synthesis in cultured neurons and astroglial cells derived from rat brain. Neurosci. Lett. 219, 211-214.
    • (1996) Neurosci. Lett. , vol.219 , pp. 211-214
    • Kranich, O.1    Hamprecht, B.2    Dringen, R.3
  • 23
    • 0015519878 scopus 로고
    • The effect of potassium on neuronal differentiation in cultures of dissociated newborn rat cerebellum
    • Lasher R. S. and Zagon I. S. (1972) The effect of potassium on neuronal differentiation in cultures of dissociated newborn rat cerebellum. Brain Res. 41, 482-488.
    • (1972) Brain Res. , vol.41 , pp. 482-488
    • Lasher, R.S.1    Zagon, I.S.2
  • 26
    • 0033655446 scopus 로고    scopus 로고
    • Regulation of glutathione synthesis
    • Lu S. C. (2000) Regulation of glutathione synthesis. Curr. Top. Cell. Regul. 36, 95-116.
    • (2000) Curr. Top. Cell. Regul. , vol.36 , pp. 95-116
    • Lu, S.C.1
  • 27
    • 0027976087 scopus 로고
    • Vitamin E, ascorbate, glutathione, glutathione disulfide, and enzymes of glutathione metabolism in cultures of chick astrocytes and neurons: Evidence that astrocytes play an important role in antioxidative processes in the brain
    • Makar T. K., Nedergaard M., Preuss A., Gelbard A. S., Perumal A. S. and Cooper A. J. L. (1994) Vitamin E, ascorbate, glutathione, glutathione disulfide, and enzymes of glutathione metabolism in cultures of chick astrocytes and neurons: Evidence that astrocytes play an important role in antioxidative processes in the brain. J. Neurochem. 62, 45-53.
    • (1994) J. Neurochem. , vol.62 , pp. 45-53
    • Makar, T.K.1    Nedergaard, M.2    Preuss, A.3    Gelbard, A.S.4    Perumal, A.S.5    Cooper, A.J.L.6
  • 31
    • 0032951247 scopus 로고    scopus 로고
    • The induction of GSH synthesis by nanomolar concentrations of nitric oxide in epithelial cells: A role for γ-glutamylcysteine synthetase and γ-glutamyltranspeptidase
    • Moellering D., McAndrew J., Patel R. P., Forman H. J., Mulcahy R. T., Jo H. and Darley-Usmar V. M. (1999) The induction of GSH synthesis by nanomolar concentrations of nitric oxide in epithelial cells: a role for γ-glutamylcysteine synthetase and γ-glutamyltranspeptidase. FEBS Lett. 448, 292-296.
    • (1999) FEBS Lett. , vol.448 , pp. 292-296
    • Moellering, D.1    McAndrew, J.2    Patel, R.P.3    Forman, H.J.4    Mulcahy, R.T.5    Jo, H.6    Darley-Usmar, V.M.7
  • 32
    • 2642671110 scopus 로고    scopus 로고
    • An electrophile responsive element (EpRE) regulates α-naphtoflavone induction of human γ-glutamylcysteine synthetase regulatory subunit gene
    • Moinova H. R. and Mulcahy R. T. (1998) An electrophile responsive element (EpRE) regulates α-naphtoflavone induction of human γ-glutamylcysteine synthetase regulatory subunit gene. J. Biol. Chem. 273, 14683-14689.
    • (1998) J. Biol. Chem. , vol.273 , pp. 14683-14689
    • Moinova, H.R.1    Mulcahy, R.T.2
  • 33
    • 0028914295 scopus 로고
    • Identification of a putative antioxidant response element in the 5′-flanking region of the human γ-glutamylcysteine synthetase heavy subunit gene
    • Mulcahy R. T. and Gipp J. J. (1995) 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, 227-233.
    • (1995) Biochem. Biophys. Res. Commun. , vol.209 , pp. 227-233
    • Mulcahy, R.T.1    Gipp, J.J.2
  • 34
    • 0035107463 scopus 로고    scopus 로고
    • Preferential expression of antioxidant response element mediated gene expression in astrocytes
    • Murphy T. H., Yu J., Ng R., Johnson D. A., Shen H., Honey C. R. and Johnson J. A. (2001) Preferential expression of antioxidant response element mediated gene expression in astrocytes. J. Neurochem. 76, 1670-1678.
    • (2001) J. Neurochem. , vol.76 , pp. 1670-1678
    • Murphy, T.H.1    Yu, J.2    Ng, R.3    Johnson, D.A.4    Shen, H.5    Honey, C.R.6    Johnson, J.A.7
  • 36
    • 0027421350 scopus 로고
    • Maintenance of neuronal glutathione by glial cells
    • Sagara J., Miura K. and Bannai S. (1993) Maintenance of neuronal glutathione by glial cells. J. Neurochem. 61, 1672-1676.
    • (1993) J. Neurochem. , vol.61 , pp. 1672-1676
    • Sagara, J.1    Miura, K.2    Bannai, S.3
  • 37
    • 0029988384 scopus 로고    scopus 로고
    • Glutathione efflux from cultured astrocytes
    • Sagara J., Makino N. and Bannai S. (1996) Glutathione efflux from cultured astrocytes. J Neurochem. 66, 1876-1881.
    • (1996) J Neurochem. , vol.66 , pp. 1876-1881
    • Sagara, J.1    Makino, N.2    Bannai, S.3
  • 40
    • 0028075410 scopus 로고
    • Alterations in glutathione levels in Parkinson's disease and other neurodegenerative diseases affecting basal ganglia
    • Sian J., Dexter D. T., Lees A. J., Daniel S., Ayid Y., Savoy-Agid F., Jenner P. and Marsden C. D. (1994a) Alterations in glutathione levels in Parkinson's disease and other neurodegenerative diseases affecting basal ganglia. Ann. Neurol. 36, 348-355.
    • (1994) Ann. Neurol. , vol.36 , pp. 348-355
    • Sian, J.1    Dexter, D.T.2    Lees, A.J.3    Daniel, S.4    Ayid, Y.5    Savoy-Agid, F.6    Jenner, P.7    Marsden, C.D.8
  • 43
    • 0031972780 scopus 로고    scopus 로고
    • Pretreatment of astrocytes with interferon-alpha/beta prevents neuronal mitochondrial respiratory chain damage
    • Stewart V. C., Land J. M., Clark J. B. and Heales S. J. R. (1998) Pretreatment of astrocytes with interferon-alpha/beta prevents neuronal mitochondrial respiratory chain damage. J. Neurochem. 70, 432-434.
    • (1998) J. Neurochem. , vol.70 , pp. 432-434
    • Stewart, V.C.1    Land, J.M.2    Clark, J.B.3    Heales, S.J.R.4
  • 44
    • 0036826902 scopus 로고    scopus 로고
    • Preservation of extracellular glutathione by an astrocyte derived factor with properties comparable to extracellular superoxide dismutase
    • Stewart V. C., Stone R., Gegg M. E., Sharpe M. A., Hurst R. D., Clark J. B. and Heales S. J. R. (2002) Preservation of extracellular glutathione by an astrocyte derived factor with properties comparable to extracellular superoxide dismutase. J. Neurochem. 83, 984-991.
    • (2002) J. Neurochem. , vol.83 , pp. 984-991
    • Stewart, V.C.1    Stone, R.2    Gegg, M.E.3    Sharpe, M.A.4    Hurst, R.D.5    Clark, J.B.6    Heales, S.J.R.7
  • 45
    • 0025240043 scopus 로고
    • Identification of a highly reactive threonine residue at the active site of gamma-glutamyl transpeptidase
    • Stole E., Seddon A. P., Wellner D. and Meister A. (1990) Identification of a highly reactive threonine residue at the active site of gamma-glutamyl transpeptidase. Proc. Natl Acad. Sci. USA 87, 1706-1709.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 1706-1709
    • Stole, E.1    Seddon, A.P.2    Wellner, D.3    Meister, A.4
  • 46
    • 0033378590 scopus 로고    scopus 로고
    • Astrocyte nitric oxide causes neuronal mitochondrial damage, but antioxidant release limits neuronal cell death
    • Stone R., Stewart V. C., Hurst R. D., Clark J. B. and Heales S. J. R. (1999) Astrocyte nitric oxide causes neuronal mitochondrial damage, but antioxidant release limits neuronal cell death. Ann. N. Y. Acad. Sci. 893, 400-403.
    • (1999) Ann. N. Y. Acad. Sci. , vol.893 , pp. 400-403
    • Stone, R.1    Stewart, V.C.2    Hurst, R.D.3    Clark, J.B.4    Heales, S.J.R.5
  • 47
    • 0029848066 scopus 로고    scopus 로고
    • Regulation of γ-glutamylcysteine synthetase by protein phosphorylation
    • Sun W., Huang Z. and Lu S. C. (1996) Regulation of γ-glutamylcysteine synthetase by protein phosphorylation. Biochem. J. 320, 321-328.
    • (1996) Biochem. J. , vol.320 , pp. 321-328
    • Sun, W.1    Huang, Z.2    Lu, S.C.3
  • 48
    • 0032527047 scopus 로고    scopus 로고
    • Expression and characterisation of human glutamate-cysteine ligase
    • Tu Z. and Anders M. W. (1998) Expression and characterisation of human glutamate-cysteine ligase. Arch. Biochem. Biophys. 15, 247-254.
    • (1998) Arch. Biochem. Biophys. , vol.15 , pp. 247-254
    • Tu, Z.1    Anders, M.W.2
  • 49
    • 0034071372 scopus 로고    scopus 로고
    • Regulation of γ-glutamylcysteine synthetase subunit gene expression: Insights into transcriptional control of antioxidant defenses
    • Wild A. C. and Mulcahy R. T. (2000) Regulation of γ-glutamylcysteine synthetase subunit gene expression: Insights into transcriptional control of antioxidant defenses. Free Radic. Res. 32, 281-301.
    • (2000) Free Radic. Res. , vol.32 , pp. 281-301
    • Wild, A.C.1    Mulcahy, R.T.2
  • 50
    • 0017187544 scopus 로고
    • The kinetic mechanism of rat kidney γ-glutamylcysteine synthetase
    • Yip B. and Rudolph F. B. (1976) The kinetic mechanism of rat kidney γ-glutamylcysteine synthetase. J. Biol. Chem. 251, 3563-3568.
    • (1976) J. Biol. Chem. , vol.251 , pp. 3563-3568
    • Yip, B.1    Rudolph, F.B.2


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