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Volumn 36, Issue 1, 2010, Pages 45-56

Hypoxia and kinase activity regulate lung epithelial cell glutathione

Author keywords

Antioxidants; Epithelial; Hypoxia; Kinases; Lung; Oxidants

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 4 (4 FLUOROPHENYL) 2 (4 METHYLSULFINYLPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; ACETYLCYSTEINE; ADENOVIRUS VECTOR; CATALASE; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; GLUTATHIONE SYNTHASE; HEAT SHOCK PROTEIN 27; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; PHOSPHOTRANSFERASE;

EID: 76749101154     PISSN: 01902148     EISSN: 15210499     Source Type: Journal    
DOI: 10.3109/01902140903061795     Document Type: Article
Times cited : (6)

References (34)
  • 1
    • 0023263523 scopus 로고
    • Normal alveolar epithelial lining fluid contains high levels of glutathione
    • Cantin A, North S, Hubbard R, Crystal R: Normal alveolar epithelial lining fluid contains high levels of glutathione. J Appl Physiol. 1987;63:152-157.
    • (1987) J Appl Physiol , vol.63 , pp. 152-157
    • Cantin, A.1    North, S.2    Hubbard, R.3    Crystal, R.4
  • 3
    • 45849137517 scopus 로고    scopus 로고
    • Kinase activity Hsp27 phosphorylation and lung epithelial cell glutathione
    • Jackson R, Garcia-Rojas R: Kinase activity, Hsp27 phosphorylation and lung epithelial cell glutathione. Exp Lung Res. 2008;34:245-262.
    • (2008) Exp Lung Res , vol.34 , pp. 245-262
    • Jackson, R.1    Garcia-Rojas, R.2
  • 4
    • 36349009441 scopus 로고    scopus 로고
    • Over expression of human Hsp27 inhibits seruminduced proliferation in airway smooth muscle myocytes and confers resistance to hydrogen peroxide cytotoxicity
    • Salinthone S, BaM, Hanson L,Martin J, Halayko A, Gerthoffer W: Over expression of human Hsp27 inhibits seruminduced proliferation in airway smooth muscle myocytes and confers resistance to hydrogen peroxide cytotoxicity. Am J Physiol Lung Cell Mol Physiol. 2007;293:L1194-L1207.
    • (2007) Am J Physiol Lung Cell Mol Physiol , vol.293
    • Salinthone, S.1    Ba, M.2    Hanson, L.3    Martin, J.4    Halayko, A.5    Gerthoffer, W.6
  • 5
    • 0007404243 scopus 로고    scopus 로고
    • Large unphosphorylated aggregates as the active form of Hsp27, which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNF-α in NIH-3T3-ras cells
    • Mehlen P, Hickey E, Weber L, Arrigo A: Large unphosphorylated aggregates as the active form of Hsp27, which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNF-α in NIH-3T3-ras cells. Biochem Biophys Res Commun. 1997;241:187-192.
    • (1997) Biochem Biophys Res Commun , vol.241 , pp. 187-192
    • Mehlen, P.1    Hickey, E.2    Weber, L.3    Arrigo, A.4
  • 8
    • 0021220094 scopus 로고
    • Synthesis of lung surfactant-associated glycoproteins by A549 cells: Description of an in vitro model for human type II cell dysfunction
    • Balis J, Bumganer S, Paciga J, Paterson J, Shelley S: Synthesis of lung surfactant-associated glycoproteins by A549 cells: description of an in vitro model for human type II cell dysfunction. Exp Lung Res. 1984;6:197-213.
    • (1984) Exp Lung Res , vol.6 , pp. 197-213
    • Balis, J.1    Bumganer, S.2    Paciga, J.3    Paterson, J.4    Shelley, S.5
  • 9
    • 0034009507 scopus 로고    scopus 로고
    • Biophysical and molecular characterization of amiloride-sensitive sodium channels in A549 cells
    • Lazrak A, Samanta A, Matalon S: Biophysical and molecular characterization of amiloride-sensitive sodium channels in A549 cells. Am J Lung Cell Mol Physiol. 2000;278:L848-L857.
    • (2000) Am J Lung Cell Mol Physiol , vol.278
    • Lazrak, A.1    Samanta, A.2    Matalon, S.3
  • 11
    • 0037974679 scopus 로고    scopus 로고
    • Mitochondrial complex i and aconitase during hypoxia-reoxygenation: Modulation of enzyme activities by mitochondrial MnSOD augmentation
    • Powell C, Wright M, Jackson R: Mitochondrial complex I and aconitase during hypoxia-reoxygenation: Modulation of enzyme activities by mitochondrial MnSOD augmentation. Am J Physiol (Lung Cell Mol Physiol). 2003;285:L189-L198.
    • (2003) Am J Physiol (Lung Cell Mol Physiol) , vol.285
    • Powell, C.1    Wright, M.2    Jackson, R.3
  • 12
    • 0023079953 scopus 로고
    • High performance liquid chromatography of thiols and disulfides: Dinitrophenol derivatives
    • Farriss M, Read D: High performance liquid chromatography of thiols and disulfides: dinitrophenol derivatives. Methods Enzymol. 1987;143:101-109.
    • (1987) Methods Enzymol , vol.143 , pp. 101-109
    • Farriss, M.1    Read, D.2
  • 13
    • 0035830938 scopus 로고    scopus 로고
    • Adenovirus-mediated overexpression of catalase in the cytosolic or mitochondrial compartment protects against cytochrome P450 2E1-dependent toxicity in HepG2 cells
    • Bai J, Cederbaum A: Adenovirus-mediated overexpression of catalase in the cytosolic or mitochondrial compartment protects against cytochrome P450 2E1-dependent toxicity in HepG2 cells. J Biol Chem. 2001;276:4315-4321.
    • (2001) J Biol Chem , vol.276 , pp. 4315-4321
    • Bai, J.1    Cederbaum, A.2
  • 15
    • 33645224817 scopus 로고    scopus 로고
    • Characterization of the bifunctional γ -glutamate-cysteine ligase/glutathione synthetase (GshF) of Pasteurella multocida
    • Vergauwen B, de Vos D, van Beeumen J: Characterization of the bifunctional γ -glutamate-cysteine ligase/glutathione synthetase (GshF) of Pasteurella multocida. J Biol Chem. 2006;2817:4380-4394.
    • (2006) J Biol Chem , vol.2817 , pp. 4380-4394
    • Vergauwen, B.1    De Vos, D.2    Van Beeumen, J.3
  • 16
    • 0019551730 scopus 로고
    • "Western blotting" electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radio iodinated protein a
    • Burnette W: "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radio iodinated protein A. Anal Biochem. 1981;112:195-203.
    • (1981) Anal Biochem , vol.112 , pp. 195-203
    • Burnette, W.1
  • 17
    • 0014481378 scopus 로고
    • Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: Applications to mammalian blood and other tissues
    • Tietze F: Enzymic method for quantitative determination of nanogram amounts of total and oxidized glutathione: applications to mammalian blood and other tissues. Anal Biochem. 1969;27:502-520.
    • (1969) Anal Biochem , vol.27 , pp. 502-520
    • Tietze, F.1
  • 18
    • 0032437922 scopus 로고    scopus 로고
    • Multiple comparison procedures updated
    • Ludbrook J: Multiple comparison procedures updated. Clin Exp Pharmacol Physiol. 1998;25:1032-1037.
    • (1998) Clin Exp Pharmacol Physiol , vol.25 , pp. 1032-1037
    • Ludbrook, J.1
  • 19
    • 0036709597 scopus 로고    scopus 로고
    • Cellular glutathione and thiols metabolism
    • Dickinson D, Forman H: Cellular glutathione and thiols metabolism. Biochem Pharmacol. 2002;64:1019-1026.
    • (2002) Biochem Pharmacol , vol.64 , pp. 1019-1026
    • Dickinson, D.1    Forman, H.2
  • 20
    • 4644317883 scopus 로고    scopus 로고
    • Hypoxic reduction in cellular glutathione levels requires mitochondrial reactive oxygen species
    • Mansfield K, Simon M, Keith B: Hypoxic reduction in cellular glutathione levels requires mitochondrial reactive oxygen species. J Appl Physiol. 2004;97:1358-1366.
    • (2004) J Appl Physiol , vol.97 , pp. 1358-1366
    • Mansfield, K.1    Simon, M.2    Keith, B.3
  • 21
    • 34250745912 scopus 로고    scopus 로고
    • The Q0 site of the mitochondrial complex III is required for the transduction on hypoxic signaling via reactive oxygen species production
    • Bell E, Klimova T, Eisenbart J, Moraes C, Murphy M, Budinger G, Chandel N: The Q0 site of the mitochondrial complex III is required for the transduction on hypoxic signaling via reactive oxygen species production. J Cell Biol. 2007;177:1029-1036.
    • (2007) J Cell Biol , vol.177 , pp. 1029-1036
    • Bell, E.1    Klimova, T.2    Eisenbart, J.3    Moraes, C.4    Murphy, M.5    Budinger, G.6    Chandel, N.7
  • 22
    • 0021149767 scopus 로고
    • Reversible dissociation of γ -glutamylcysteine synthetase into two subunits
    • Seelig G, Simondsen R, Meister A: Reversible dissociation of γ -glutamylcysteine synthetase into two subunits. J Biol Chem. 1984;259:9345-9347.
    • (1984) J Biol Chem , vol.259 , pp. 9345-9347
    • Seelig, G.1    Simondsen, R.2    Meister, A.3
  • 23
    • 0032527047 scopus 로고    scopus 로고
    • Expression and characterization of human glutamate-cysteine ligase
    • Tu Z, Anders M: Expression and characterization of human glutamate-cysteine ligase. Arch Biochem Biophys. 1998;354:247-254.
    • (1998) Arch Biochem Biophys , vol.354 , pp. 247-254
    • Tu, Z.1    Anders, M.2
  • 24
    • 0037144436 scopus 로고    scopus 로고
    • Role of AP-1 in the coordinate regulation of rat glutamate cysteine ligase and glutathione synthetase by tertbutyl hydroquinone
    • Yang H, Zeng Y, Lee T, Yang Y, Ou X, Chen L, Haque M, Rippe R, Lu S: Role of AP-1 in the coordinate regulation of rat glutamate cysteine ligase and glutathione synthetase by tertbutyl hydroquinone. J Biol Chem. 2002;277:35232-35239.
    • (2002) J Biol Chem , vol.277 , pp. 35232-35239
    • Yang, H.1    Zeng, Y.2    Lee, T.3    Yang, Y.4    Ou, X.5    Chen, L.6    Haque, M.7    Rippe, R.8    Lu, S.9
  • 25
    • 65049089113 scopus 로고    scopus 로고
    • Regulation of glutathione synthesis
    • Lu S: Regulation of glutathione synthesis. Mol Mech Med. 2009;30:42-59.
    • (2009) Mol Mech Med , vol.30 , pp. 42-59
    • Lu, S.1
  • 27
    • 0029610424 scopus 로고
    • Intracellular reactive oxygen species as apparent modulators of heat-shock protein 27 (Hsp27) structural organization and phosphorylation in basal and tumour necrosis factor α-treated T47D human carcinoma cells
    • Mehlen P, Kretz-Remy C, Briolay J, Fostan P, Mirault M, Arrigo A: Intracellular reactive oxygen species as apparent modulators of heat-shock protein 27 (Hsp27) structural organization and phosphorylation in basal and tumour necrosis factor α-treated T47D human carcinoma cells. Biochem J. 1995;312:367-375.
    • (1995) Biochem J , vol.312 , pp. 367-375
    • Mehlen, P.1    Kretz-Remy, C.2    Briolay, J.3    Fostan, P.4    Mirault, M.5    Arrigo, A.6
  • 29
    • 1642410281 scopus 로고    scopus 로고
    • P38MAPK and MEK1/2 inhibition contribute to cellular oxidant injury after hypoxia
    • Powell C, Wright M, Jackson R: p38MAPK and MEK1/2 inhibition contribute to cellular oxidant injury after hypoxia. Am J Physiol (Lung Cell Mol Physiol). 2004;286:L826-L833.
    • (2004) Am J Physiol (Lung Cell Mol Physiol) , vol.286
    • Powell, C.1    Wright, M.2    Jackson, R.3
  • 30
    • 0029848066 scopus 로고    scopus 로고
    • Regulation of γ -glutamyl cysteine synthetase by protein phosphorylation
    • Sun W, Huang Z, Lu S: Regulation of γ -glutamyl cysteine synthetase by protein phosphorylation. Biochem J. 1996;320:321-328.
    • (1996) Biochem J , vol.320 , pp. 321-328
    • Sun, W.1    Huang, Z.2    Lu, S.3
  • 31
    • 0029593484 scopus 로고
    • Hydrogen peroxide increases the activity of γ - gglutamylcysteine synthase in cultured Chinese hamster V79 cells
    • Ochi T: Hydrogen peroxide increases the activity of γ - glutamylcysteine synthase in cultured Chinese hamster V79 cells. Arch Toxicol. 1995;70:96-103.
    • (1995) Arch Toxicol , vol.70 , pp. 96-103
    • Ochi, T.1
  • 32
    • 33846849624 scopus 로고    scopus 로고
    • Sub micromolar concentrations of 4-hydroxynonelal induce glutamate cysteine ligase expression in HBE 1 cells
    • Zhang H, Court N, Forman H. Sub micromolar concentrations of 4-hydroxynonelal induce glutamate cysteine ligase expression in HBE 1 cells. Redox Rep. 2007;12:101-106.
    • (2007) Redox Rep , vol.12 , pp. 101-106
    • Zhang, H.1    Court, N.2    Forman, H.3
  • 33
    • 0037044735 scopus 로고    scopus 로고
    • Cytoskeletal changes in hypoxic pulmonary endothelial cells are dependent on MAPK-activated protein kinase MK2
    • KayyaliU, Pennella C, Trujillo C, Villa O, GaestelM,Hassoun P: Cytoskeletal changes in hypoxic pulmonary endothelial cells are dependent on MAPK-activated protein kinase MK2. J Biol Chem. 2002;277:42596-42602.
    • (2002) J Biol Chem , vol.277 , pp. 42596-42602
    • Kayyali, U.1    Pennella, C.2    Trujillo, C.3    Villa, O.4    Gaestel, M.5    Hassoun, P.6
  • 34
    • 36348954401 scopus 로고    scopus 로고
    • Systemic deficiency of the MAPK-activated protein kinase 2 reduces atherosclerosis in hypercolesterolemic mice
    • Jagavelu K, Tietge U, Gaestel M, Drexler H, Schieffer B, Bavendiek U: Systemic deficiency of the MAPK-activated protein kinase 2 reduces atherosclerosis in hypercholesterolemic mice. Circ Res. 2007;101:1104-1112.
    • (2007) Circ Res , vol.101 , pp. 1104-1112
    • Jagavelu, K.1    Tietge, U.2    Gaestel, M.3    Drexler, H.4    Schieffer, B.5    Bavendiek, U.6


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