메뉴 건너뛰기




Volumn 3, Issue 1, 2008, Pages 5-13

Glutathione and glutathione-dependent enzymes in the control of calcium homeostasis

Author keywords

Calcium homeostasis; Glutathione; Glutathione peroxidase; Glutathione reductase; Glutathione tranferase; Inositol 1,4,5 triphosphate receptor; Ionotropic glutamate receptor; Ryanodine receptor

Indexed keywords


EID: 42449083593     PISSN: 15548643     EISSN: 15548651     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (2)

References (116)
  • 1
    • 0042008053 scopus 로고    scopus 로고
    • The network of calcium regulation in muscle
    • Martonosi AN, Pikula S. The network of calcium regulation in muscle. Acta Biochim Polon 2003; 50:1-30.
    • (2003) Acta Biochim Polon , vol.50 , pp. 1-30
    • Martonosi, A.N.1    Pikula, S.2
  • 2
    • 0001487636 scopus 로고
    • On the biochemistry of glutathione
    • Taneguchi N, Higashi T, Sakamoto Y, Meister A, eds, San Diego: Academic Press
    • Meister A. On the biochemistry of glutathione. In: Taneguchi N, Higashi T, Sakamoto Y, Meister A, eds. Glutathione Centennial: Molecular Perspectives and Clinical Implications. San Diego: Academic Press, 1989:3-21.
    • (1989) Glutathione Centennial: Molecular Perspectives and Clinical Implications , pp. 3-21
    • Meister, A.1
  • 3
    • 0018195287 scopus 로고
    • The glutathione status of cells
    • Kosower NS, Kosower EM. The glutathione status of cells. Int Rev Cytol 1978; 54:109-60.
    • (1978) Int Rev Cytol , vol.54 , pp. 109-160
    • Kosower, N.S.1    Kosower, E.M.2
  • 4
    • 0029561319 scopus 로고
    • Glutathione in health and disease: Pharmacotherapeutic issues
    • Lomaestro BM, Malone M. Glutathione in health and disease: Pharmacotherapeutic issues. Ann Pharmacother 1995; 29:1263-73.
    • (1995) Ann Pharmacother , vol.29 , pp. 1263-1273
    • Lomaestro, B.M.1    Malone, M.2
  • 5
    • 0032848124 scopus 로고    scopus 로고
    • Glutathione efflux induced by NMDA and kainate: Implications in neurotoxicity?
    • Wallin C, Weber SG, Sandberg M. Glutathione efflux induced by NMDA and kainate: Implications in neurotoxicity? J Neurochem 1999; 73:1566-72.
    • (1999) J Neurochem , vol.73 , pp. 1566-1572
    • Wallin, C.1    Weber, S.G.2    Sandberg, M.3
  • 6
    • 0030782430 scopus 로고    scopus 로고
    • Requirement for cGMP in nerve cell death caused by glutathione depletion
    • Li Y, Maher P, Schubert D. Requirement for cGMP in nerve cell death caused by glutathione depletion. J Cell Biol 1997; 139:1317-24.
    • (1997) J Cell Biol , vol.139 , pp. 1317-1324
    • Li, Y.1    Maher, P.2    Schubert, D.3
  • 7
    • 0033231162 scopus 로고    scopus 로고
    • Biologic and pharmacologic regulation of mammalian glutathione synthesis
    • Griffith O. Biologic and pharmacologic regulation of mammalian glutathione synthesis. Free Radic Biol Med 1999; 27:922-35.
    • (1999) Free Radic Biol Med , vol.27 , pp. 922-935
    • Griffith, O.1
  • 8
    • 0017761529 scopus 로고
    • Fluxes and distribution of calcium in rat liver cells: Kinetic analysis and identification of pools
    • Claret-Berthon B, Claret M, Mazet JL. Fluxes and distribution of calcium in rat liver cells: Kinetic analysis and identification of pools. J Physiol (London) 1977; 272:529-52.
    • (1977) J Physiol (London) , vol.272 , pp. 529-552
    • Claret-Berthon, B.1    Claret, M.2    Mazet, J.L.3
  • 9
    • 17444419342 scopus 로고    scopus 로고
    • Molecular mechanisms of reduced glutathione transport: Role of the MPR/CFTR/ABCC and OATP/ SLC21A families of membrane proteins
    • Ballatori N, Hammond CL, Cunningham JB, Krance SM, Marchan R. Molecular mechanisms of reduced glutathione transport: Role of the MPR/CFTR/ABCC and OATP/ SLC21A families of membrane proteins. Toxicol Appl Pharmacol 2005; 204:238-55.
    • (2005) Toxicol Appl Pharmacol , vol.204 , pp. 238-255
    • Ballatori, N.1    Hammond, C.L.2    Cunningham, J.B.3    Krance, S.M.4    Marchan, R.5
  • 10
    • 33750011601 scopus 로고    scopus 로고
    • Mitochondrial glutathione transport: Physiological, pathological and toxicological implications
    • Lash LH. Mitochondrial glutathione transport: Physiological, pathological and toxicological implications. Chem Biol Interact 2006; 163:54-67.
    • (2006) Chem Biol Interact , vol.163 , pp. 54-67
    • Lash, L.H.1
  • 11
    • 17444419341 scopus 로고    scopus 로고
    • Role of glutathione transport processes in kidney function
    • Lash LH. Role of glutathione transport processes in kidney function. Toxicol Appl Pharmacol 2005; 204:329-42.
    • (2005) Toxicol Appl Pharmacol , vol.204 , pp. 329-342
    • Lash, L.H.1
  • 13
    • 0029033862 scopus 로고
    • Mitochondrial changes associated with glutathione deficiency
    • Meister A. Mitochondrial changes associated with glutathione deficiency. Biochim Biophys Acta 1995; 1271:35-42.
    • (1995) Biochim Biophys Acta , vol.1271 , pp. 35-42
    • Meister, A.1
  • 14
    • 0025049139 scopus 로고
    • High-affinity transport of glutathione is part of a multicomponent system essential for mitochondrial function
    • Martensson J, Lai JC, Meister A. High-affinity transport of glutathione is part of a multicomponent system essential for mitochondrial function. Proc Natl Acad Sci USA 1990; 87:7185-9.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 7185-7189
    • Martensson, J.1    Lai, J.C.2    Meister, A.3
  • 15
    • 0036313070 scopus 로고    scopus 로고
    • The effects of focal ischemia and reperfusion on the glutathione content of mitochondria from rat brain subregions
    • Anderson MF, Sims NR. The effects of focal ischemia and reperfusion on the glutathione content of mitochondria from rat brain subregions. J Neurochem 2002; 81:541-9.
    • (2002) J Neurochem , vol.81 , pp. 541-549
    • Anderson, M.F.1    Sims, N.R.2
  • 16
    • 0019324933 scopus 로고
    • Protection of thiol groups and retention of calcium ions by cardiac mitochondria
    • Harris EJ, Baum H. Protection of thiol groups and retention of calcium ions by cardiac mitochondria. Biochem J 1980; 186:725-32.
    • (1980) Biochem J , vol.186 , pp. 725-732
    • Harris, E.J.1    Baum, H.2
  • 18
    • 4644327947 scopus 로고    scopus 로고
    • Highly selective and prolonged depletion of mitochondrial glutathione in astrocytes markedly increases sensitivity to peroxynitrite
    • Muyderman H, Nilsson M, Sims NR. Highly selective and prolonged depletion of mitochondrial glutathione in astrocytes markedly increases sensitivity to peroxynitrite. J Neurosci 2004; 24:8019-28.
    • (2004) J Neurosci , vol.24 , pp. 8019-8028
    • Muyderman, H.1    Nilsson, M.2    Sims, N.R.3
  • 19
    • 0037103764 scopus 로고    scopus 로고
    • Multiple isoforms of mitochondrial glutathiglutathione S-transferases and their differential induction under oxidative stress
    • Raza H, Robin MA, Fang JK, Avadhani NG. Multiple isoforms of mitochondrial glutathiglutathione S-transferases and their differential induction under oxidative stress. Biochem J 2002; 366:45-55.
    • (2002) Biochem J , vol.366 , pp. 45-55
    • Raza, H.1    Robin, M.A.2    Fang, J.K.3    Avadhani, N.G.4
  • 22
    • 0035917814 scopus 로고    scopus 로고
    • Mitochondrial permeability transition and oxidative stress
    • Kowaltowski AJ, Castilho RF, Vercesi AE. Mitochondrial permeability transition and oxidative stress. FEBS Lett 2001; 495:12-5.
    • (2001) FEBS Lett , vol.495 , pp. 12-15
    • Kowaltowski, A.J.1    Castilho, R.F.2    Vercesi, A.E.3
  • 23
    • 9644300972 scopus 로고    scopus 로고
    • Cytochrome bc(1) regulates the mitochondrial permeability transition by two distinct pathways
    • Armstrong JS, Yang HY, Duan W, Whiteman M. Cytochrome bc(1) regulates the mitochondrial permeability transition by two distinct pathways. J Biol Chem 2004; 279:50420-8.
    • (2004) J Biol Chem , vol.279 , pp. 50420-50428
    • Armstrong, J.S.1    Yang, H.Y.2    Duan, W.3    Whiteman, M.4
  • 24
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer FQ, Buettner GR. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med 2001; 30:1191-212.
    • (2001) Free Radic Biol Med , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 25
    • 1842430709 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and glutamate excitotoxicity studied in primary neuronal cultures
    • Nicholls DG. Mitochondrial dysfunction and glutamate excitotoxicity studied in primary neuronal cultures. Curr Mol Med 2004; 4:149-77.
    • (2004) Curr Mol Med , vol.4 , pp. 149-177
    • Nicholls, D.G.1
  • 26
    • 33644688266 scopus 로고    scopus 로고
    • Acute glutathione depletion restricts mitochondrial ATP export in cerebellar granule neurons
    • Vesce S, Jekabsons MB, Johnson-Cadwell LI, Nicholls DG. Acute glutathione depletion restricts mitochondrial ATP export in cerebellar granule neurons. J Biol Chem 2005; 280:38720-28.
    • (2005) J Biol Chem , vol.280 , pp. 38720-38728
    • Vesce, S.1    Jekabsons, M.B.2    Johnson-Cadwell, L.I.3    Nicholls, D.G.4
  • 27
    • 14644416354 scopus 로고    scopus 로고
    • Glutathione depletion resulting in selective mitochondrial complex I inhibition in dopaminergic cells is via an NO-mediated pathway not involving peroxynitrite: Implications for Parkinson's disease
    • Hsu M, Srinivas B, Kumar J, Subramanian R, Andersen J. Glutathione depletion resulting in selective mitochondrial complex I inhibition in dopaminergic cells is via an NO-mediated pathway not involving peroxynitrite: Implications for Parkinson's disease. J Neurochem 2005; 92:1091-103.
    • (2005) J Neurochem , vol.92 , pp. 1091-1103
    • Hsu, M.1    Srinivas, B.2    Kumar, J.3    Subramanian, R.4    Andersen, J.5
  • 28
    • 0028799706 scopus 로고
    • Depletion of brain glutathione is accompanied by impaired mitochondrial function and decreased N-acetyl aspartate concentration
    • Heales SJ, Davies SE, Bates TE, Clark JB. Depletion of brain glutathione is accompanied by impaired mitochondrial function and decreased N-acetyl aspartate concentration. Neurochem Res 1995; 20:31-8.
    • (1995) Neurochem Res , vol.20 , pp. 31-38
    • Heales, S.J.1    Davies, S.E.2    Bates, T.E.3    Clark, J.B.4
  • 29
    • 0033515794 scopus 로고    scopus 로고
    • Differential effects of L-buthionine sulfoximine and ethacrynic acid on glutathione levels and mitochondrial function in PC12 cells
    • Seyfried J, Soldner F, Schulz JB, Klockgether T, Kovar KA, Wüllner U. Differential effects of L-buthionine sulfoximine and ethacrynic acid on glutathione levels and mitochondrial function in PC12 cells. Neurosci Lett 1999; 264:1-4.
    • (1999) Neurosci Lett , vol.264 , pp. 1-4
    • Seyfried, J.1    Soldner, F.2    Schulz, J.B.3    Klockgether, T.4    Kovar, K.A.5    Wüllner, U.6
  • 30
    • 0028840853 scopus 로고
    • Translocation of loops regulates transport activity of mitochondrial ADP/ATP carrier deduced from formation of a specific intermolecular disulfide bridge catalyzed by copper-o-phenanthroline
    • Majima E, Ikawa K, Takeda M, Hashimoto M, Shinohara Y, Terada H. Translocation of loops regulates transport activity of mitochondrial ADP/ATP carrier deduced from formation of a specific intermolecular disulfide bridge catalyzed by copper-o-phenanthroline. J Biol Chem 1995; 270:29548-54.
    • (1995) J Biol Chem , vol.270 , pp. 29548-29554
    • Majima, E.1    Ikawa, K.2    Takeda, M.3    Hashimoto, M.4    Shinohara, Y.5    Terada, H.6
  • 31
    • 3142536289 scopus 로고
    • Regulation of intracellular calcium compartmentation: Studies with isolated hepatocytes and t-butyl hydroperoxide
    • Bellomo G, Jewell SA, Thor H, Orrenius S. Regulation of intracellular calcium compartmentation: Studies with isolated hepatocytes and t-butyl hydroperoxide. Proc Natl Acad Sci USA 1982; 79:6842-6.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 6842-6846
    • Bellomo, G.1    Jewell, S.A.2    Thor, H.3    Orrenius, S.4
  • 33
    • 42449163596 scopus 로고    scopus 로고
    • Orrenius S, Jewell SA, Bellomo G, Thor H, Jones DP, Smith MT. Regulation of calcium compartmentation in the hepatocyte: A critical role of glutathione. In: Larsson A, Orrenius S, Holmgren A, Mannervik B, eds. Functions of Glutathione. Biochemical, Physiological, Toxicological, and Clinical Aspects. New York: Raven Press, 1983:261-71.
    • Orrenius S, Jewell SA, Bellomo G, Thor H, Jones DP, Smith MT. Regulation of calcium compartmentation in the hepatocyte: A critical role of glutathione. In: Larsson A, Orrenius S, Holmgren A, Mannervik B, eds. Functions of Glutathione. Biochemical, Physiological, Toxicological, and Clinical Aspects. New York: Raven Press, 1983:261-71.
  • 34
    • 0022364266 scopus 로고
    • Altered thiol and calcium homeostasis in oxidative hepatocellular injury
    • Bellomo G, Orrenius S. Altered thiol and calcium homeostasis in oxidative hepatocellular injury. Hepatology 1985; 5:876-82.
    • (1985) Hepatology , vol.5 , pp. 876-882
    • Bellomo, G.1    Orrenius, S.2
  • 35
    • 0025171519 scopus 로고
    • Extracellular calcium effects on cell viability and thiol homeostasis
    • Reed DJ, Pascoe GA, Thomas CE. Extracellular calcium effects on cell viability and thiol homeostasis. Environ Health Perspect 1990; 84:113-20.
    • (1990) Environ Health Perspect , vol.84 , pp. 113-120
    • Reed, D.J.1    Pascoe, G.A.2    Thomas, C.E.3
  • 36
    • 0023371943 scopus 로고
    • A role of vitamin E in protection against cell injury: Maintenance of intracellular glutathione precursors and biosynthesis
    • Pascoe GA, Fariss MW, Olafsdottir K, Reed DJ. A role of vitamin E in protection against cell injury: Maintenance of intracellular glutathione precursors and biosynthesis. Eur J Biochem 1987; 166:241-7.
    • (1987) Eur J Biochem , vol.166 , pp. 241-247
    • Pascoe, G.A.1    Fariss, M.W.2    Olafsdottir, K.3    Reed, D.J.4
  • 37
    • 0019348696 scopus 로고
    • On the cycles of glutathione metabolism and transport
    • Meister A. On the cycles of glutathione metabolism and transport. Curr Top Cell Regul 1981; 18:21-58.
    • (1981) Curr Top Cell Regul , vol.18 , pp. 21-58
    • Meister, A.1
  • 38
    • 0024264526 scopus 로고
    • Glutathione metabolism and it selective modification
    • Meister A. Glutathione metabolism and it selective modification. Journ Biol Chem 1988; 263:17205-20.
    • (1988) Journ Biol Chem , vol.263 , pp. 17205-17220
    • Meister, A.1
  • 39
    • 0034981152 scopus 로고    scopus 로고
    • Glutathione-nutritional and pharmacological viewpoints: Part II
    • Valencia E, Marin A, Hardy G. Glutathione-nutritional and pharmacological viewpoints: Part II. Nutrition 2001; 17:485-6.
    • (2001) Nutrition , vol.17 , pp. 485-486
    • Valencia, E.1    Marin, A.2    Hardy, G.3
  • 40
    • 1542376929 scopus 로고    scopus 로고
    • Glutathione metabolism and its implications for health
    • Wu G, Fang Y, Yang S, Lupton J, Turner N. Glutathione metabolism and its implications for health. Journ Nutr 2004; 134:489-92.
    • (2004) Journ Nutr , vol.134 , pp. 489-492
    • Wu, G.1    Fang, Y.2    Yang, S.3    Lupton, J.4    Turner, N.5
  • 41
    • 0029052835 scopus 로고
    • Evidence for Altered regulation of y-glutamylcysteine synthetase gene expression among cisplatin-sensitive and cisplatin-resistant human ovarian cancer cell lines
    • Yao K, Godwin A, Johnson S, Ozols R, Dwyer P, Hamilton T. Evidence for Altered regulation of y-glutamylcysteine synthetase gene expression among cisplatin-sensitive and cisplatin-resistant human ovarian cancer cell lines. Cancer Research 1995; 55:4367-74.
    • (1995) Cancer Research , vol.55 , pp. 4367-4374
    • Yao, K.1    Godwin, A.2    Johnson, S.3    Ozols, R.4    Dwyer, P.5    Hamilton, T.6
  • 42
    • 0031591651 scopus 로고    scopus 로고
    • Proximal 59-flanking sequence of the human gammaglutamylcysteine synthetase heavy subunit gene is involved in cisplatin-induced transcriptional upregulation in a lung cancer cell line SBC-3
    • Tomonari A, Nishio K, Kurokawa H, Fukumoto H, Fukuoka K, Iwamoto Y, Usuda J, Suzuki T, Itakura M, Saijo N. Proximal 59-flanking sequence of the human gammaglutamylcysteine synthetase heavy subunit gene is involved in cisplatin-induced transcriptional upregulation in a lung cancer cell line SBC-3. Biochem Biophys Res Commun 1997; 236:616-21.
    • (1997) Biochem Biophys Res Commun , vol.236 , pp. 616-621
    • Tomonari, A.1    Nishio, K.2    Kurokawa, H.3    Fukumoto, H.4    Fukuoka, K.5    Iwamoto, Y.6    Usuda, J.7    Suzuki, T.8    Itakura, M.9    Saijo, N.10
  • 43
    • 0030670301 scopus 로고    scopus 로고
    • Regulation of human g-glutamylcysteine synthetase: Co-ordinate induction of the catalytic and regulatory subunits in HepG2 cells
    • Galloway DC, Blake DG, Shepherd AG, McLellan LI. Regulation of human g-glutamylcysteine synthetase: Co-ordinate induction of the catalytic and regulatory subunits in HepG2 cells. Biochem J 1997; 328:99-104.
    • (1997) Biochem J , vol.328 , pp. 99-104
    • Galloway, D.C.1    Blake, D.G.2    Shepherd, A.G.3    McLellan, L.I.4
  • 44
    • 0032987187 scopus 로고    scopus 로고
    • Mechanisms involved in the regulation of key enzymes of cysteine metabolism in rat liver in vivo
    • Bella D, Hirschberger Yu Hosokawa L, Stipanuk M. Mechanisms involved in the regulation of key enzymes of cysteine metabolism in rat liver in vivo. Am J Physiol 1999; 276:326-35.
    • (1999) Am J Physiol , vol.276 , pp. 326-335
    • Bella, D.1    Hirschberger2    Yu Hosokawa, L.3    Stipanuk, M.4
  • 45
    • 0036709597 scopus 로고    scopus 로고
    • Cellular glutathione and thiol metabolism
    • Dickinson D, Forman H. Cellular glutathione and thiol metabolism. Bioch Pharm 2002; 64:1019-26.
    • (2002) Bioch Pharm , vol.64 , pp. 1019-1026
    • Dickinson, D.1    Forman, H.2
  • 47
    • 33846018435 scopus 로고    scopus 로고
    • A functional transsulfuration pathway in the brain links to glutathione homeostasis
    • Vitvitsky V, Thomas M, Ghorpade A, Gendelman H, Banerjee R. A functional transsulfuration pathway in the brain links to glutathione homeostasis. Journ Biol Chem 2006; 281:35785-93.
    • (2006) Journ Biol Chem , vol.281 , pp. 35785-35793
    • Vitvitsky, V.1    Thomas, M.2    Ghorpade, A.3    Gendelman, H.4    Banerjee, R.5
  • 48
    • 0029848066 scopus 로고    scopus 로고
    • Regulation of γ-glutamylcysteine synthetase by protein phosphorylation
    • Sun W, Huang Z, Lu S. Regulation of γ-glutamylcysteine synthetase by protein phosphorylation. Biochem 1996; 320:321-8.
    • (1996) Biochem , vol.320 , pp. 321-328
    • Sun, W.1    Huang, Z.2    Lu, S.3
  • 49
    • 3042802690 scopus 로고    scopus 로고
    • Glutathione: An overview of biosynthesis and modulation
    • Anderson M. Glutathione: An overview of biosynthesis and modulation. Chemico-Biological Interaction 1998; 111-112:1-14.
    • (1998) Chemico-Biological Interaction
    • Anderson, M.1
  • 50
    • 7444224116 scopus 로고    scopus 로고
    • Thimerosal neurotoxicity is associated with glutathione depletion: Protection with glutathione precursors
    • James S, Slikker W, Melnyk S, New E, Pogribna M, Jerniga S. Thimerosal neurotoxicity is associated with glutathione depletion: protection with glutathione precursors. NeuroToxicology 2005; 26:1-8.
    • (2005) NeuroToxicology , vol.26 , pp. 1-8
    • James, S.1    Slikker, W.2    Melnyk, S.3    New, E.4    Pogribna, M.5    Jerniga, S.6
  • 51
    • 0033555806 scopus 로고    scopus 로고
    • Synthesis of the antioxidant glutathione in neurons: Supply by astrocytes of CysGly as precursor for neuronal glutathione
    • Dringen R, Pfeiffer B, Hamprecht B. Synthesis of the antioxidant glutathione in neurons: Supply by astrocytes of CysGly as precursor for neuronal glutathione. Jour Neurosc 1999; 19:562-9.
    • (1999) Jour Neurosc , vol.19 , pp. 562-569
    • Dringen, R.1    Pfeiffer, B.2    Hamprecht, B.3
  • 52
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metalcatalyzed reactions
    • Stadtman ER. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metalcatalyzed reactions. Annu Rev Biochem 1993; 62:797-821.
    • (1993) Annu Rev Biochem , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 53
    • 0034185616 scopus 로고    scopus 로고
    • Protein oxidation and age-dependent alteration in calcium homeostasis
    • Thomas C, Squier D, Bigelow J. Protein oxidation and age-dependent alteration in calcium homeostasis. Frontiers in Bioscience 2000; 5:504-26.
    • (2000) Frontiers in Bioscience , vol.5 , pp. 504-526
    • Thomas, C.1    Squier, D.2    Bigelow, J.3
  • 54
    • 0023003551 scopus 로고
    • Antioxidant defense mechanisms of endothelial cells: Glutathione redox cycle versus catalase
    • Suttorp N, Toepfer W, Roka L. Antioxidant defense mechanisms of endothelial cells: Glutathione redox cycle versus catalase. Am J Physiol 1986; 252:C671-80.
    • (1986) Am J Physiol , vol.252
    • Suttorp, N.1    Toepfer, W.2    Roka, L.3
  • 55
    • 0026754574 scopus 로고
    • Reactive oxygen species and the central nervous system
    • Halliwell B. Reactive oxygen species and the central nervous system. J Neurochem 1992; 59:1609-23.
    • (1992) J Neurochem , vol.59 , pp. 1609-1623
    • Halliwell, B.1
  • 57
    • 0034655674 scopus 로고    scopus 로고
    • Mechanism of hydrogen peroxide-induced calcium dysregulation in PC12 cells
    • Wang H, Joseph JA. Mechanism of hydrogen peroxide-induced calcium dysregulation in PC12 cells. Free radical and Medicine 2000; 28:1222-31.
    • (2000) Free radical and Medicine , vol.28 , pp. 1222-1231
    • Wang, H.1    Joseph, J.A.2
  • 59
    • 0025971401 scopus 로고
    • Stimulation of lipid peroxidation increases the intracellular calcium content of isolated hepatocytes
    • Albano E, Bellomo G, Parola M, Carini R, Dianzani MU. Stimulation of lipid peroxidation increases the intracellular calcium content of isolated hepatocytes. Biochim Biophys Acta 1991; 1091:310-6.
    • (1991) Biochim Biophys Acta , vol.1091 , pp. 310-316
    • Albano, E.1    Bellomo, G.2    Parola, M.3    Carini, R.4    Dianzani, M.U.5
  • 62
    • 0036318147 scopus 로고    scopus 로고
    • Disruptive effects of glucocorticoids on glutathione peroxidase biochemistry in hippocampal cultures
    • Patel R, McIntosh L, McLaughlin J, Brooke S, Nimon V, Sapolsky R. Disruptive effects of glucocorticoids on glutathione peroxidase biochemistry in hippocampal cultures. J Neurochem 2002; 82:118-25.
    • (2002) J Neurochem , vol.82 , pp. 118-125
    • Patel, R.1    McIntosh, L.2    McLaughlin, J.3    Brooke, S.4    Nimon, V.5    Sapolsky, R.6
  • 63
    • 0034193467 scopus 로고    scopus 로고
    • Plasma membrane calcium pump isoform 1 gene expression is repressed by corticosterone and stress in rat hippocampus
    • Bhargava A, Meijer OC, Dallman MF, Pearce D. Plasma membrane calcium pump isoform 1 gene expression is repressed by corticosterone and stress in rat hippocampus. J Neurosci 2000; 20:3129-38.
    • (2000) J Neurosci , vol.20 , pp. 3129-3138
    • Bhargava, A.1    Meijer, O.C.2    Dallman, M.F.3    Pearce, D.4
  • 64
    • 0032054442 scopus 로고    scopus 로고
    • Corticosteroid regulation of ion channel conductances and mRNA levels in individual hippocampal CA1 neurons
    • Nair SM, Werkman TR, Craig J, Finnell R, Joels M, Eberwine JH. Corticosteroid regulation of ion channel conductances and mRNA levels in individual hippocampal CA1 neurons. J Neurosci 1998; 18:2685-96.
    • (1998) J Neurosci , vol.18 , pp. 2685-2696
    • Nair, S.M.1    Werkman, T.R.2    Craig, J.3    Finnell, R.4    Joels, M.5    Eberwine, J.H.6
  • 65
    • 0027686249 scopus 로고
    • Oxidative stress, glutamate, and neurodegenerative disorders
    • Coyle JT, Puttfarcken P. Oxidative stress, glutamate, and neurodegenerative disorders. Science 1993; 262:689-95.
    • (1993) Science , vol.262 , pp. 689-695
    • Coyle, J.T.1    Puttfarcken, P.2
  • 66
    • 0347695005 scopus 로고    scopus 로고
    • Over-expression of antioxidant enzymes protects cultured hippocampal and cortical neurons from necrotic insults
    • Wang H, Cheng E, Brooke S, Chang P, Sapolsky R. Over-expression of antioxidant enzymes protects cultured hippocampal and cortical neurons from necrotic insults. J Neurochem 2003; 87:1527-34.
    • (2003) J Neurochem , vol.87 , pp. 1527-1534
    • Wang, H.1    Cheng, E.2    Brooke, S.3    Chang, P.4    Sapolsky, R.5
  • 67
    • 0021345735 scopus 로고
    • Oxidation of glutathione during hydroperoxide metabolism: A study using isolated hepatocytes and the glutathione reductase inhibitor 1,3-bis(2-chloroethyl)-1-nitrosourea
    • Eklow L, Moldeus P, Orrenius S. Oxidation of glutathione during hydroperoxide metabolism: A study using isolated hepatocytes and the glutathione reductase inhibitor 1,3-bis(2-chloroethyl)-1-nitrosourea. Eur J Biochem 1984; 138:459-63.
    • (1984) Eur J Biochem , vol.138 , pp. 459-463
    • Eklow, L.1    Moldeus, P.2    Orrenius, S.3
  • 68
    • 0019948316 scopus 로고
    • The relationship of biliary glutathione disulfide efflux and intracellular glutathione disulfide content in perfused rat liver
    • Akerboom TP, Bilzer M, Sies H. The relationship of biliary glutathione disulfide efflux and intracellular glutathione disulfide content in perfused rat liver. J Biol Chem 1982; 257:4248-52.
    • (1982) J Biol Chem , vol.257 , pp. 4248-4252
    • Akerboom, T.P.1    Bilzer, M.2    Sies, H.3
  • 69
    • 0029825678 scopus 로고    scopus 로고
    • Oxidized glutathione mediates cation channel activation in calf vascular endothelial cells during oxidant stress
    • Koliwad SK, Elliott SJ, Kunze DL. Oxidized glutathione mediates cation channel activation in calf vascular endothelial cells during oxidant stress. J Physiol 1996; 495:37-49.
    • (1996) J Physiol , vol.495 , pp. 37-49
    • Koliwad, S.K.1    Elliott, S.J.2    Kunze, D.L.3
  • 70
    • 0029586071 scopus 로고    scopus 로고
    • 2+ store. Biochem J 1995; 312:485-9.
    • 2+ store. Biochem J 1995; 312:485-9.
  • 73
    • 10944257609 scopus 로고    scopus 로고
    • Neurodegenerative conditions associated with ageing: A molecular interplay?
    • Troulinaki K, Tavernarakis N. Neurodegenerative conditions associated with ageing: A molecular interplay? Mech Ageing Dev 2005; 126:23-33.
    • (2005) Mech Ageing Dev , vol.126 , pp. 23-33
    • Troulinaki, K.1    Tavernarakis, N.2
  • 74
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • Behl C, Davis JB, Lesley R, Schubert D. Hydrogen peroxide mediates amyloid beta protein toxicity. Cell 1994; 77:817-27.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 76
    • 0031887764 scopus 로고    scopus 로고
    • 2+ levels in cultured rat astrocytes
    • 2+ levels in cultured rat astrocytes. Neurosci Lett 1998; 243:121-4.
    • (1998) Neurosci Lett , vol.243 , pp. 121-124
    • Stix, B.1    Reiser, G.2
  • 77
    • 33947137730 scopus 로고    scopus 로고
    • Abdellatif Y, Liu D, Gallant EM, Gage PW, Board Dulhunty AF. The Mu class glutathione transferase is abundant in striated muscle and is an isoforms-specific regulator of ryanodine receptor calcium channels. Cell Calcium 2007; 41:429-40.
    • Abdellatif Y, Liu D, Gallant EM, Gage PW, Board PG, Dulhunty AF. The Mu class glutathione transferase is abundant in striated muscle and is an isoforms-specific regulator of ryanodine receptor calcium channels. Cell Calcium 2007; 41:429-40.
  • 78
    • 0347356333 scopus 로고    scopus 로고
    • Evidence for the transport of glutathione through ryanodine receptor channel type 1
    • B'Anhegyi G, Csala M, Nagy G, Sorrentino V, Fulceri R, Benedetti A. Evidence for the transport of glutathione through ryanodine receptor channel type 1. Biochem J 2003; 376:807-12.
    • (2003) Biochem J , vol.376 , pp. 807-812
    • B'Anhegyi, G.1    Csala, M.2    Nagy, G.3    Sorrentino, V.4    Fulceri, R.5    Benedetti, A.6
  • 79
    • 0030936013 scopus 로고    scopus 로고
    • Glutathione modulates ryanodine receptor from skeletal muscle sarcoplasmic reticulum
    • Zable AC, Favero TG, Abramson JJ. Glutathione modulates ryanodine receptor from skeletal muscle sarcoplasmic reticulum. J Biol Chem 1997; 272:7069-77.
    • (1997) J Biol Chem , vol.272 , pp. 7069-7077
    • Zable, A.C.1    Favero, T.G.2    Abramson, J.J.3
  • 81
    • 0029093480 scopus 로고
    • Effect of oxidized glutathione and temperature on inositol 1,4,5-trisphosphate binding in permeabilized hepatocytes
    • Renard-Rooney DC, Joseph SK, Seitz MB, Thomas AP. Effect of oxidized glutathione and temperature on inositol 1,4,5-trisphosphate binding in permeabilized hepatocytes. Biochem 1995; 310:185-92.
    • (1995) Biochem , vol.310 , pp. 185-192
    • Renard-Rooney, D.C.1    Joseph, S.K.2    Seitz, M.B.3    Thomas, A.P.4
  • 83
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • Hayes JD, Pulford DJ. The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Biochem Mol Biol 1995; 30:445-600.
    • (1995) Biochem Mol Biol , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 84
    • 0001306237 scopus 로고
    • Human glutathione transferases: Classification, tissue distribution, structure and functional properties
    • Luxembourg: European Commission
    • Mannervik B, Widersten M. Human glutathione transferases: Classification, tissue distribution, structure and functional properties. In: Pacifici GM, Fracchia GN. Advances in Drug Metabolism in Man. Luxembourg: European Commission, 1995:407-60.
    • (1995) Pacifici GM, Fracchia GN. Advances in Drug Metabolism in Man , pp. 407-460
    • Mannervik, B.1    Widersten, M.2
  • 85
    • 0031021397 scopus 로고    scopus 로고
    • Structure, catalytic mechanism, and evolution of the glutathione transferases
    • Armstrong RN. Structure, catalytic mechanism, and evolution of the glutathione transferases. Chem Res Toxicol 1997; 10:2-18.
    • (1997) Chem Res Toxicol , vol.10 , pp. 2-18
    • Armstrong, R.N.1
  • 86
    • 0035793617 scopus 로고    scopus 로고
    • Dulhunty A, Gage P, Curtis S, Chelvanayagam G, Board P. The glutathione transferase structural family includes a nuclear chloride channel and a ryanodine receptor calcium release channel modulator. J Biol Chem 2001; 276:3319-23.
    • Dulhunty A, Gage P, Curtis S, Chelvanayagam G, Board P. The glutathione transferase structural family includes a nuclear chloride channel and a ryanodine receptor calcium release channel modulator. J Biol Chem 2001; 276:3319-23.
  • 89
    • 0033582482 scopus 로고    scopus 로고
    • The cloning and characterization of a new stress response protein: A mammalian member of a family of theta class glutathione s-transferase-like proteins
    • Kodym R, Calkins P, Story M. The cloning and characterization of a new stress response protein: A mammalian member of a family of theta class glutathione s-transferase-like proteins. J Biol Chem 1999; 274:5131-7.
    • (1999) J Biol Chem , vol.274 , pp. 5131-5137
    • Kodym, R.1    Calkins, P.2    Story, M.3
  • 90
    • 0030792637 scopus 로고    scopus 로고
    • Multiple roles of glutathione in the central nervous system
    • Cooper AJL, Kristal BS. Multiple roles of glutathione in the central nervous system. Biol Chem 1997; 378:793-802.
    • (1997) Biol Chem , vol.378 , pp. 793-802
    • Cooper, A.J.L.1    Kristal, B.S.2
  • 91
    • 0026683402 scopus 로고
    • The multiple excitatory amino acid receptors and receptor subtypes and their putative interactions
    • Recasens M, Mayat E, Vigres M. The multiple excitatory amino acid receptors and receptor subtypes and their putative interactions. Mol Pharmacol 1992; 2:15-31.
    • (1992) Mol Pharmacol , vol.2 , pp. 15-31
    • Recasens, M.1    Mayat, E.2    Vigres, M.3
  • 93
    • 0029071981 scopus 로고
    • Interaction of glutathione derivatives with brain 2-amino-3-hydroxy- 5-methyl-4- isoxazolepropionate (AMPA) receptors
    • Oja SS, Jana'ky R, Saransaari P, Jenei Z, Varga V. Interaction of glutathione derivatives with brain 2-amino-3-hydroxy- 5-methyl-4- isoxazolepropionate (AMPA) receptors. Proc West Pharmacol Soc 1995; 38:9-11.
    • (1995) Proc West Pharmacol Soc , vol.38 , pp. 9-11
    • Oja, S.S.1    Jana'ky, R.2    Saransaari, P.3    Jenei, Z.4    Varga, V.5
  • 94
    • 0028340001 scopus 로고
    • Molecular diversity and functions of glutamate receptors
    • Nakanishi S, Masu M. Molecular diversity and functions of glutamate receptors. Annu Rev Biophys Biomol Struct 1994; 23:319-48.
    • (1994) Annu Rev Biophys Biomol Struct , vol.23 , pp. 319-348
    • Nakanishi, S.1    Masu, M.2
  • 95
    • 0002956890 scopus 로고    scopus 로고
    • Glutathione and glutathione derivatives: Possible modulators of ionotropic glutamate receptors
    • Shaw CA, ed, Washington, DC: Taylor and Francis
    • Janáky R, Varga V, Jenei Z, Saransaari P, Oja SS. Glutathione and glutathione derivatives: Possible modulators of ionotropic glutamate receptors. In: Shaw CA, ed. Glutathione in the Nervous System. Washington, DC: Taylor and Francis, 1998:163-96.
    • (1998) Glutathione in the Nervous System , pp. 163-196
    • Janáky, R.1    Varga, V.2    Jenei, Z.3    Saransaari, P.4    Oja, S.S.5
  • 96
    • 0028884818 scopus 로고
    • NMDA receptor redox sites: Are they targets for selective neuronal protection?
    • Gozlan H, Ben-Ari Y. NMDA receptor redox sites: Are they targets for selective neuronal protection? Trends Pharmacol Sci 1995; 16:368-74.
    • (1995) Trends Pharmacol Sci , vol.16 , pp. 368-374
    • Gozlan, H.1    Ben-Ari, Y.2
  • 97
    • 0028821474 scopus 로고
    • A possible role of glutathione as an endogenous agonist at the N-methyl-D-aspartate recognition domain in rat brain
    • Ogita K, Enomoto R, Nakahara F, Ishitsubo N, Yoneda Y. A possible role of glutathione as an endogenous agonist at the N-methyl-D-aspartate recognition domain in rat brain. J Neurochem 1995; 64:1088-96.
    • (1995) J Neurochem , vol.64 , pp. 1088-1096
    • Ogita, K.1    Enomoto, R.2    Nakahara, F.3    Ishitsubo, N.4    Yoneda, Y.5
  • 98
    • 0026682896 scopus 로고
    • Screening of thiol compounds: Depolarization-induced release of glutathione and cysteine from rat brain slices
    • Zängerle L, Cuénod M, Winterhalter KH, Do KQ. Screening of thiol compounds: Depolarization-induced release of glutathione and cysteine from rat brain slices. J Neurochem 1992; 59:181-9.
    • (1992) J Neurochem , vol.59 , pp. 181-189
    • Zängerle, L.1    Cuénod, M.2    Winterhalter, K.H.3    Do, K.Q.4
  • 99
    • 0037321591 scopus 로고    scopus 로고
    • Searching for mechanisms of N-methyl-D-aspartate-induced glutathione efflux in organotypic hippocampal cultures
    • Wallin C, Abbas AK, Tranberg M, Weber SG, Wigstrom H, Sandberg M. Searching for mechanisms of N-methyl-D-aspartate-induced glutathione efflux in organotypic hippocampal cultures. Neurochem Res 2003; 28:281-91.
    • (2003) Neurochem Res , vol.28 , pp. 281-291
    • Wallin, C.1    Abbas, A.K.2    Tranberg, M.3    Weber, S.G.4    Wigstrom, H.5    Sandberg, M.6
  • 102
    • 0031877853 scopus 로고    scopus 로고
    • Interference of S-alkyl derivatives of glutathione with brain ionotropic glutamate receptors
    • Jenei Z, Jana'ky R, Varga V, Saransaari P, Oja SS. Interference of S-alkyl derivatives of glutathione with brain ionotropic glutamate receptors. Neurochem Res 1998; 23:1087-93.
    • (1998) Neurochem Res , vol.23 , pp. 1087-1093
    • Jenei, Z.1    Jana'ky, R.2    Varga, V.3    Saransaari, P.4    Oja, S.S.5
  • 103
    • 0027234701 scopus 로고
    • The TINS/TiPs lecture: The molecular biology of mammalian glutamate receptor channels
    • Seeburg PH. The TINS/TiPs lecture: The molecular biology of mammalian glutamate receptor channels. Trends Neurosci 1993; 16:359-65.
    • (1993) Trends Neurosci , vol.16 , pp. 359-365
    • Seeburg, P.H.1
  • 106
    • 0028075410 scopus 로고
    • Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia
    • Sian J, Dexter DT, Lees AJ, Daniel S, Agid Y, Javoy-Agid F, Jenner P, Marsden CD. Alterations in glutathione levels in Parkinson's disease and other neurodegenerative disorders affecting basal ganglia. Ann Neurol 1994; 36:348-55.
    • (1994) Ann Neurol , vol.36 , pp. 348-355
    • Sian, J.1    Dexter, D.T.2    Lees, A.J.3    Daniel, S.4    Agid, Y.5    Javoy-Agid, F.6    Jenner, P.7    Marsden, C.D.8
  • 107
    • 0026734077 scopus 로고
    • Oxidized glutathione causes sensitization of calcium release to inositol 1,4,5-trisphosphate in permeabilized hepatocytes
    • Renard CD, Seitz MB, Thomas AP. Oxidized glutathione causes sensitization of calcium release to inositol 1,4,5-trisphosphate in permeabilized hepatocytes. Biochem J 1992; 284:507-12.
    • (1992) Biochem J , vol.284 , pp. 507-512
    • Renard, C.D.1    Seitz, M.B.2    Thomas, A.P.3
  • 108
    • 33646846296 scopus 로고    scopus 로고
    • Activation of family C G-protein coupled receptors by the tripeptide glutathione
    • Wang M, Yao Y, Kuang D, Hampson DR. Activation of family C G-protein coupled receptors by the tripeptide glutathione. J Biol Chem 2006; 281:8864-70.
    • (2006) J Biol Chem , vol.281 , pp. 8864-8870
    • Wang, M.1    Yao, Y.2    Kuang, D.3    Hampson, D.R.4
  • 112
    • 33645009947 scopus 로고    scopus 로고
    • Quantitative mapping of oxidation-sensitive cysteine residue in SERCA in vivo by HPLC-electrospray-tandem MS: Selective protein oxidation during biological aging
    • Sharov VS, Dremina ES, Galeva NA, Williams TD, Schöneich C. Quantitative mapping of oxidation-sensitive cysteine residue in SERCA in vivo by HPLC-electrospray-tandem MS: Selective protein oxidation during biological aging. Biochem J 2006; 394:605-15
    • (2006) Biochem J , vol.394 , pp. 605-615
    • Sharov, V.S.1    Dremina, E.S.2    Galeva, N.A.3    Williams, T.D.4    Schöneich, C.5
  • 114
    • 33750449016 scopus 로고    scopus 로고
    • Increases in mitochondrial reactive oxygen species trigger hypoxia-induced calcium responses in pulmonary artery smooth muscle cells
    • Waypa GB, Guzy R, Mungai PT, Mack MM, Marks JD, Roe MW, Schumacker PT. Increases in mitochondrial reactive oxygen species trigger hypoxia-induced calcium responses in pulmonary artery smooth muscle cells. Circ Res 2006; 99:970-8.
    • (2006) Circ Res , vol.99 , pp. 970-978
    • Waypa, G.B.1    Guzy, R.2    Mungai, P.T.3    Mack, M.M.4    Marks, J.D.5    Roe, M.W.6    Schumacker, P.T.7
  • 116
    • 23944503805 scopus 로고    scopus 로고
    • 2+ and ATP. Biochem J 2005; 390:333-43.
    • 2+ and ATP. Biochem J 2005; 390:333-43.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.