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Volumn 231, Issue 3, 2008, Pages 384-392

Increased oxidative stress and antioxidant expression in mouse keratinocytes following exposure to paraquat

Author keywords

Glutathione S transferase; MAPEG; Oxidative stress; Paraquat; Skin

Indexed keywords

CATALASE; COPPER ZINC SUPEROXIDE DISMUTASE; GLUTATHIONE PEROXIDASE 1; GLUTATHIONE TRANSFERASE A3; GLUTATHIONE TRANSFERASE A4; GLUTATHIONE TRANSFERASE P1; HEME OXYGENASE 1; HERBICIDE; HYDROGEN PEROXIDE; METALLOTHIONEIN II; PARAQUAT; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SUPEROXIDE; SUPEROXIDE DISMUTASE;

EID: 50849144028     PISSN: 0041008X     EISSN: 10960333     Source Type: Journal    
DOI: 10.1016/j.taap.2008.05.014     Document Type: Article
Times cited : (50)

References (80)
  • 1
    • 0033230607 scopus 로고    scopus 로고
    • Role of redox potential and reactive oxygen species in stress signaling
    • Adler V., Yin Z., Tew K.D., and Ronai Z. Role of redox potential and reactive oxygen species in stress signaling. Oncogene 18 (1999) 6104-6111
    • (1999) Oncogene , vol.18 , pp. 6104-6111
    • Adler, V.1    Yin, Z.2    Tew, K.D.3    Ronai, Z.4
  • 2
    • 0347382286 scopus 로고    scopus 로고
    • A case of multiple skin cancers after occupational exposure to pesticides
    • Anderson K.D., and Scerri G.V. A case of multiple skin cancers after occupational exposure to pesticides. Br. J. Dermatol. 149 (2003) 1088-1089
    • (2003) Br. J. Dermatol. , vol.149 , pp. 1088-1089
    • Anderson, K.D.1    Scerri, G.V.2
  • 3
    • 0026033907 scopus 로고
    • Induction of heme oxygenase: a general response to oxidant stress in cultured mammalian cells
    • Applegate L.A., Luscher P., and Tyrrell R.M. Induction of heme oxygenase: a general response to oxidant stress in cultured mammalian cells. Cancer Res. 51 (1991) 974-978
    • (1991) Cancer Res. , vol.51 , pp. 974-978
    • Applegate, L.A.1    Luscher, P.2    Tyrrell, R.M.3
  • 4
    • 33646857902 scopus 로고    scopus 로고
    • The crystal structure of NAD(P)H quinone oxidoreductase 1 in complex with its potent inhibitor dicoumarol
    • Asher G., Dym O., Tsvetkov P., Adler J., and Shaul Y. The crystal structure of NAD(P)H quinone oxidoreductase 1 in complex with its potent inhibitor dicoumarol. Biochemistry 45 (2006) 6372-6378
    • (2006) Biochemistry , vol.45 , pp. 6372-6378
    • Asher, G.1    Dym, O.2    Tsvetkov, P.3    Adler, J.4    Shaul, Y.5
  • 6
    • 0028036292 scopus 로고
    • Detoxification of base propenals and other alpha, beta-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases
    • Berhane K., Widersten M., Engstrom A., Kozarich J.W., and Mannervik B. Detoxification of base propenals and other alpha, beta-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases. Proc. Natl. Acad. Sci. U. S. A. 91 (1994) 1480-1484
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 1480-1484
    • Berhane, K.1    Widersten, M.2    Engstrom, A.3    Kozarich, J.W.4    Mannervik, B.5
  • 8
    • 0016153291 scopus 로고
    • Superoxide- and singlet oxygen-catalyzed lipid peroxidation as a possible mechanism for paraquat (methyl viologen) toxicity
    • Bus J.S., Aust S.D., and Gibson J.E. Superoxide- and singlet oxygen-catalyzed lipid peroxidation as a possible mechanism for paraquat (methyl viologen) toxicity. Biochem. Biophys. Res. Commun. 58 (1974) 749-755
    • (1974) Biochem. Biophys. Res. Commun. , vol.58 , pp. 749-755
    • Bus, J.S.1    Aust, S.D.2    Gibson, J.E.3
  • 9
    • 0020306966 scopus 로고
    • Mechanisms of superoxide radical-mediated toxicity
    • Bus J.S., and Gibson J.E. Mechanisms of superoxide radical-mediated toxicity. J. Toxicol. Clin. Toxicol. 19 (1982) 689-697
    • (1982) J. Toxicol. Clin. Toxicol. , vol.19 , pp. 689-697
    • Bus, J.S.1    Gibson, J.E.2
  • 10
    • 0021288059 scopus 로고
    • Paraquat: model for oxidant-initiated toxicity
    • Bus J.S., and Gibson J.E. Paraquat: model for oxidant-initiated toxicity. Environ. Health Perspect. 55 (1984) 37-46
    • (1984) Environ. Health Perspect. , vol.55 , pp. 37-46
    • Bus, J.S.1    Gibson, J.E.2
  • 12
    • 0033805383 scopus 로고    scopus 로고
    • Structure-function studies of DT-diaphorase (NQO1) and NRH:quinone oxidoreductase (NQO2)
    • Chen S., Wu K., and Knox R. Structure-function studies of DT-diaphorase (NQO1) and NRH:quinone oxidoreductase (NQO2). Free Radic. Biol. Med. 29 (2000) 276-284
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 276-284
    • Chen, S.1    Wu, K.2    Knox, R.3
  • 13
    • 0842283380 scopus 로고    scopus 로고
    • Catalase transgenic mice: characterization and sensitivity to oxidative stress
    • Chen X., Liang H., Van Remmen H., Vijg J., and Richardson A. Catalase transgenic mice: characterization and sensitivity to oxidative stress. Arch. Biochem. Biophys. 422 (2004) 197-210
    • (2004) Arch. Biochem. Biophys. , vol.422 , pp. 197-210
    • Chen, X.1    Liang, H.2    Van Remmen, H.3    Vijg, J.4    Richardson, A.5
  • 14
    • 0034524859 scopus 로고    scopus 로고
    • Human studies related to protein oxidation: protein carbonyl content as a marker of damage
    • Chevion M., Berenshtein E., and Stadtman E.R. Human studies related to protein oxidation: protein carbonyl content as a marker of damage. Free Radic. Res. 33 (2000) S99-S108
    • (2000) Free Radic. Res. , vol.33
    • Chevion, M.1    Berenshtein, E.2    Stadtman, E.R.3
  • 18
    • 0028197170 scopus 로고
    • Free radicals in cutaneous biology
    • Darr D., and Fridovich I. Free radicals in cutaneous biology. J. Invest. Dermatol. 102 (1994) 671-675
    • (1994) J. Invest. Dermatol. , vol.102 , pp. 671-675
    • Darr, D.1    Fridovich, I.2
  • 19
    • 12844278044 scopus 로고    scopus 로고
    • The oxidative environment and protein damage
    • Davies M.J. The oxidative environment and protein damage. Biochem. Biophys. Acta 1703 (2005) 93-109
    • (2005) Biochem. Biophys. Acta , vol.1703 , pp. 93-109
    • Davies, M.J.1
  • 20
    • 0030246890 scopus 로고    scopus 로고
    • A metalloporphyrin superoxide dismutase mimetic protects against paraquat-induced lung injury
    • Day B.J., and Crapo J.D. A metalloporphyrin superoxide dismutase mimetic protects against paraquat-induced lung injury. Toxicol. Appl. Pharmacol. 140 (1996) 94-100
    • (1996) Toxicol. Appl. Pharmacol. , vol.140 , pp. 94-100
    • Day, B.J.1    Crapo, J.D.2
  • 21
    • 0033607235 scopus 로고    scopus 로고
    • A mechanism of paraquat toxicity involving nitric oxide synthase
    • Day B.J., Patel M., Calavetta L., Chang L.Y., and Stamler J.S. A mechanism of paraquat toxicity involving nitric oxide synthase. PNAS U. S. A. 26 (1999) 12760-12765
    • (1999) PNAS U. S. A. , vol.26 , pp. 12760-12765
    • Day, B.J.1    Patel, M.2    Calavetta, L.3    Chang, L.Y.4    Stamler, J.S.5
  • 23
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • Dean R.T., Fu S., Stocker R., and Davies M.J. Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 324 (1997) 1-18
    • (1997) Biochem. J. , vol.324 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 24
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge W. Free radicals in the physiological control of cell function. Physiol. Rev. 82 (2002) 47-95
    • (2002) Physiol. Rev. , vol.82 , pp. 47-95
    • Droge, W.1
  • 26
    • 0033231361 scopus 로고    scopus 로고
    • Regulation of antioxidant enzyme gene expression in response to oxidative stress and during differentiation of mouse skeletal muscle
    • Franco A.A., Odom R.S., and Rando T.A. Regulation of antioxidant enzyme gene expression in response to oxidative stress and during differentiation of mouse skeletal muscle. Free Radic. Biol. Med. 27 (1999) 1122-1132
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 1122-1132
    • Franco, A.A.1    Odom, R.S.2    Rando, T.A.3
  • 27
    • 0018263443 scopus 로고
    • The biology of oxygen radicals
    • Fridovich I. The biology of oxygen radicals. Science 201 (1978) 875-880
    • (1978) Science , vol.201 , pp. 875-880
    • Fridovich, I.1
  • 29
    • 33845757115 scopus 로고    scopus 로고
    • Dicoumarol impairs mitochondrial electron transport and pyrimidine biosynthesis in human myeloid leukemia HL-60 cells
    • Gonzalez-Aragon D., Ariza J., and Villalba J.M. Dicoumarol impairs mitochondrial electron transport and pyrimidine biosynthesis in human myeloid leukemia HL-60 cells. Biochem. Pharmacol. 73 (2007) 427-439
    • (2007) Biochem. Pharmacol. , vol.73 , pp. 427-439
    • Gonzalez-Aragon, D.1    Ariza, J.2    Villalba, J.M.3
  • 31
    • 0344274396 scopus 로고    scopus 로고
    • Long-term culture of murine epidermal keratinocytes
    • Hager B., Bickenbach J.R., and Fleckman P. Long-term culture of murine epidermal keratinocytes. J. Invest. Dermatol. 112 (1999) 971-976
    • (1999) J. Invest. Dermatol. , vol.112 , pp. 971-976
    • Hager, B.1    Bickenbach, J.R.2    Fleckman, P.3
  • 32
    • 0029266564 scopus 로고
    • Potential contribution of the glutathione S-transferase supergene family to resistance to oxidative stress
    • Hayes J.D., and Strange R.C. Potential contribution of the glutathione S-transferase supergene family to resistance to oxidative stress. Free Radic. Res. 22 (1995) 193-207
    • (1995) Free Radic. Res. , vol.22 , pp. 193-207
    • Hayes, J.D.1    Strange, R.C.2
  • 34
    • 0032874845 scopus 로고    scopus 로고
    • Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defense against oxidative stress
    • Hayes J.D., and McLellan L.I. Glutathione and glutathione-dependent enzymes represent a co-ordinately regulated defense against oxidative stress. Free Radic. Res. 31 (1999) 273-300
    • (1999) Free Radic. Res. , vol.31 , pp. 273-300
    • Hayes, J.D.1    McLellan, L.I.2
  • 35
    • 0030923439 scopus 로고    scopus 로고
    • Identification and characterization of a novel microsomal enzyme with glutathione-dependent transferase and peroxidase activities
    • Jakobsson P.J., Mancini J.A., Riendeau D., and Ford-Hutchinson A.W. Identification and characterization of a novel microsomal enzyme with glutathione-dependent transferase and peroxidase activities. J. Biol. Chem. 272 (1997) 22934-22939
    • (1997) J. Biol. Chem. , vol.272 , pp. 22934-22939
    • Jakobsson, P.J.1    Mancini, J.A.2    Riendeau, D.3    Ford-Hutchinson, A.W.4
  • 36
    • 0033011878 scopus 로고    scopus 로고
    • Common structural features of MAPEG-a widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism
    • Jakobsson P.-J., Morgenstern R., Mancini J., Ford-Hutchinson A., and Persson B. Common structural features of MAPEG-a widespread superfamily of membrane associated proteins with highly divergent functions in eicosanoid and glutathione metabolism. Protein Sci. 8 (1999) 689-692
    • (1999) Protein Sci. , vol.8 , pp. 689-692
    • Jakobsson, P.-J.1    Morgenstern, R.2    Mancini, J.3    Ford-Hutchinson, A.4    Persson, B.5
  • 39
    • 0025354323 scopus 로고
    • Alteration of endogenous glutathione peroxidase, manganese superoxide dismutase, and glutathione transferase activity in cells transfected with a copper-zinc superoxide dismutase expression vector. Explanation for variations in paraquat resistance
    • Kelner M.J., and Bagnell R. Alteration of endogenous glutathione peroxidase, manganese superoxide dismutase, and glutathione transferase activity in cells transfected with a copper-zinc superoxide dismutase expression vector. Explanation for variations in paraquat resistance. J. Biol. Chem. 265 (1990) 10872-10875
    • (1990) J. Biol. Chem. , vol.265 , pp. 10872-10875
    • Kelner, M.J.1    Bagnell, R.2
  • 40
    • 0025271438 scopus 로고
    • Induction of the heme oxygenase gene in human skin fibroblasts by hydrogen peroxide and UVA (365 nm) radiation: evidence for the involvement of the hydroxyl radical
    • Keyse S.H., and Tyrrell R.M. Induction of the heme oxygenase gene in human skin fibroblasts by hydrogen peroxide and UVA (365 nm) radiation: evidence for the involvement of the hydroxyl radical. Carcinogenesis 11 (1990) 787-791
    • (1990) Carcinogenesis , vol.11 , pp. 787-791
    • Keyse, S.H.1    Tyrrell, R.M.2
  • 41
    • 0027314637 scopus 로고
    • Inhibitory effects of alpha- and beta-carotene on croton oil-induced or enzymatic lipid peroxidation and hydroperoxide production in mouse skin epidermis
    • Kim-Jun H. Inhibitory effects of alpha- and beta-carotene on croton oil-induced or enzymatic lipid peroxidation and hydroperoxide production in mouse skin epidermis. Int. J. Biochem. 25 (1993) 911-915
    • (1993) Int. J. Biochem. , vol.25 , pp. 911-915
    • Kim-Jun, H.1
  • 42
    • 0036554585 scopus 로고    scopus 로고
    • Effect of dicumarol, a Nad(P)h: quinone acceptor oxidoreductase 1 (DT-diaphorase) inhibitor on ubiquinone redox cycling in cultured rat hepatocytes
    • Kishi T., Takahashi T., Mizobuchi S., Mori K., and Okamoto T. Effect of dicumarol, a Nad(P)h: quinone acceptor oxidoreductase 1 (DT-diaphorase) inhibitor on ubiquinone redox cycling in cultured rat hepatocytes. Free Radic. Res. 36 (2002) 413-419
    • (2002) Free Radic. Res. , vol.36 , pp. 413-419
    • Kishi, T.1    Takahashi, T.2    Mizobuchi, S.3    Mori, K.4    Okamoto, T.5
  • 44
    • 0036569401 scopus 로고    scopus 로고
    • Carbonyl modified proteins in cellular regulation, aging, and disease
    • Levine R.L. Carbonyl modified proteins in cellular regulation, aging, and disease. Free Radic. Biol. Med. 32 (2002) 790-796
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 790-796
    • Levine, R.L.1
  • 45
    • 12344263803 scopus 로고    scopus 로고
    • Enhanced expression of glutathione-S-transferase A1-1 protects against oxidative stress in human retinal pigment epithelial cells
    • Liang F.-Q., Alssadi R., Morehead P., Awasthi Y.C., and Godley B.F. Enhanced expression of glutathione-S-transferase A1-1 protects against oxidative stress in human retinal pigment epithelial cells. Exp. Eye Res. 80 (2005) 113-119
    • (2005) Exp. Eye Res. , vol.80 , pp. 113-119
    • Liang, F.-Q.1    Alssadi, R.2    Morehead, P.3    Awasthi, Y.C.4    Godley, B.F.5
  • 46
    • 0035573719 scopus 로고    scopus 로고
    • The heme oxygenase system and cellular defense mechanisms. Do HO-1 and HO-2 have different functions?
    • Maines M.D., and Panahian N. The heme oxygenase system and cellular defense mechanisms. Do HO-1 and HO-2 have different functions?. Adv. Exp. Med. Biol. 502 (2001) 249-272
    • (2001) Adv. Exp. Med. Biol. , vol.502 , pp. 249-272
    • Maines, M.D.1    Panahian, N.2
  • 49
    • 0032212488 scopus 로고    scopus 로고
    • Suppression of tumor promoter-induced oxidative stress and inflammatory responses in mouse skin by a superoxide generation inhibitor 1′-acetoxychavicol acetate
    • Nakamura Y., Murakami A., Ohto Y., Torikai K., Tanaka T., and Ohigashi H. Suppression of tumor promoter-induced oxidative stress and inflammatory responses in mouse skin by a superoxide generation inhibitor 1′-acetoxychavicol acetate. Cancer Res. 58 (1998) 4832-4839
    • (1998) Cancer Res. , vol.58 , pp. 4832-4839
    • Nakamura, Y.1    Murakami, A.2    Ohto, Y.3    Torikai, K.4    Tanaka, T.5    Ohigashi, H.6
  • 50
    • 0027479814 scopus 로고
    • Studies on the inhibitory mechanisms of iodonium compounds with special reference to neutrophil NADPH oxidase
    • O'Donnell V.B., Tew D.G., Jones O.T.G., and England P.J. Studies on the inhibitory mechanisms of iodonium compounds with special reference to neutrophil NADPH oxidase. Biochem. J. 290 (1993) 41-49
    • (1993) Biochem. J. , vol.290 , pp. 41-49
    • O'Donnell, V.B.1    Tew, D.G.2    Jones, O.T.G.3    England, P.J.4
  • 51
    • 0028898841 scopus 로고
    • Hazards of antioxidant combinations containing superoxide dismutase
    • Paller M.S., and Eaton J.W. Hazards of antioxidant combinations containing superoxide dismutase. Free Radic. Biol. Med. 18 (1995) 883-890
    • (1995) Free Radic. Biol. Med. , vol.18 , pp. 883-890
    • Paller, M.S.1    Eaton, J.W.2
  • 52
    • 0030886054 scopus 로고    scopus 로고
    • Reduced stress defense in heme oxygenase 1-deficient cells
    • Poss K.D., and Tonegawa S. Reduced stress defense in heme oxygenase 1-deficient cells. Proc. Natl. Acad. Sci. U. S. A. 94 (1997) 10925-10930
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 10925-10930
    • Poss, K.D.1    Tonegawa, S.2
  • 53
    • 33745865136 scopus 로고    scopus 로고
    • Protective effects of catalase overexpression on UVB-induced apoptosis in normal human keratinocytes
    • Rezvani H.R., Mazurier F., Cario-Andre M., Pain C., Ged C., Taieb A., and de Verneuil H. Protective effects of catalase overexpression on UVB-induced apoptosis in normal human keratinocytes. J. Biol. Chem. 281 (2006) 17999-18007
    • (2006) J. Biol. Chem. , vol.281 , pp. 17999-18007
    • Rezvani, H.R.1    Mazurier, F.2    Cario-Andre, M.3    Pain, C.4    Ged, C.5    Taieb, A.6    de Verneuil, H.7
  • 54
    • 9144274479 scopus 로고    scopus 로고
    • Diphenyleneiodonium inhibits the cell redox metabolism and induces oxidative stress
    • Riganti C., Gazzano E., Polimeni M., Costamagna C., Bosia A., and Ghigo D. Diphenyleneiodonium inhibits the cell redox metabolism and induces oxidative stress. J. Biol. Chem. 279 (2004) 47726-47731
    • (2004) J. Biol. Chem. , vol.279 , pp. 47726-47731
    • Riganti, C.1    Gazzano, E.2    Polimeni, M.3    Costamagna, C.4    Bosia, A.5    Ghigo, D.6
  • 55
    • 23944491356 scopus 로고    scopus 로고
    • Tissue, species, and environmental differences in absolute quantities of murine mRNAs coding for alpha, mu, omega, pi and theta glutathione S-transferases
    • Ruiz-Laguna J., Abril N., Prieto-Alamo M.J., Lopez-Barea J., and Puyeo C. Tissue, species, and environmental differences in absolute quantities of murine mRNAs coding for alpha, mu, omega, pi and theta glutathione S-transferases. Gene. Exp. 12 (2005) 165-176
    • (2005) Gene. Exp. , vol.12 , pp. 165-176
    • Ruiz-Laguna, J.1    Abril, N.2    Prieto-Alamo, M.J.3    Lopez-Barea, J.4    Puyeo, C.5
  • 57
    • 0031127706 scopus 로고    scopus 로고
    • Effects of a single exposure to UVB radiation on the activities and protein levels of copper-zinc and manganese superoxide dismutase in cultured human keratinocytes
    • Sasaki H., Akamatsu H., and Horio T. Effects of a single exposure to UVB radiation on the activities and protein levels of copper-zinc and manganese superoxide dismutase in cultured human keratinocytes. Photochem. Photobiol. 65 (1997) 707-713
    • (1997) Photochem. Photobiol. , vol.65 , pp. 707-713
    • Sasaki, H.1    Akamatsu, H.2    Horio, T.3
  • 58
    • 23144451444 scopus 로고    scopus 로고
    • Oxidative stress: molecular perception and transduction of signals triggering antioxidant defenses
    • Scandalios J.G. Oxidative stress: molecular perception and transduction of signals triggering antioxidant defenses. Braz. J. Med. Biol. Res. 38 (2005) 995-1014
    • (2005) Braz. J. Med. Biol. Res. , vol.38 , pp. 995-1014
    • Scandalios, J.G.1
  • 59
    • 20044377792 scopus 로고    scopus 로고
    • E7-expressing HaCaT keratinocyte cells are resistant to oxidative stress-induced cell death via the induction of catalase
    • Shim J.H., Cho K.J., Lee R.A., Kim S.H., Myung P.K., Choe Y.K., and Yoon D.Y. E7-expressing HaCaT keratinocyte cells are resistant to oxidative stress-induced cell death via the induction of catalase. Proteomics 5 (2005) 2112-2122
    • (2005) Proteomics , vol.5 , pp. 2112-2122
    • Shim, J.H.1    Cho, K.J.2    Lee, R.A.3    Kim, S.H.4    Myung, P.K.5    Choe, Y.K.6    Yoon, D.Y.7
  • 60
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and metal-catalyzed reactions
    • Stadtman E.R. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and metal-catalyzed reactions. Ann. Rev. Biochem. 62 (1993) 797
    • (1993) Ann. Rev. Biochem. , vol.62 , pp. 797
    • Stadtman, E.R.1
  • 61
    • 0037350198 scopus 로고    scopus 로고
    • Association between a glutathione S-transferase A1 promoter polymorphism and survival after breast cancer treatment
    • Sweeney C., Ambrosone C.B., Joseph L., Stone A., Hutchins L.F., Kadlubar F.F., and Coles B.F. Association between a glutathione S-transferase A1 promoter polymorphism and survival after breast cancer treatment. Int. J. Cancer 103 (2003) 810-814
    • (2003) Int. J. Cancer , vol.103 , pp. 810-814
    • Sweeney, C.1    Ambrosone, C.B.2    Joseph, L.3    Stone, A.4    Hutchins, L.F.5    Kadlubar, F.F.6    Coles, B.F.7
  • 62
    • 0032820451 scopus 로고    scopus 로고
    • Superoxide production from paraquat evoked by exogenous NADPH in pulmonary endothelial cells
    • Tampo Y., Tsukamoto M., and Yonaha M. Superoxide production from paraquat evoked by exogenous NADPH in pulmonary endothelial cells. Free Radic. Biol. Med. 27 (1999) 588-595
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 588-595
    • Tampo, Y.1    Tsukamoto, M.2    Yonaha, M.3
  • 63
    • 0032835934 scopus 로고    scopus 로고
    • Protein oxidation in human stratum corneum: susceptibility of keratins to oxidation in vitro and presence of a keratin oxidation gradient in vivo
    • Theile J.J., Hseih S.S., Briviba K., and Sies H. Protein oxidation in human stratum corneum: susceptibility of keratins to oxidation in vitro and presence of a keratin oxidation gradient in vivo. J. Invest. Dermatol. 113 (1999) 335-339
    • (1999) J. Invest. Dermatol. , vol.113 , pp. 335-339
    • Theile, J.J.1    Hseih, S.S.2    Briviba, K.3    Sies, H.4
  • 64
    • 0030946857 scopus 로고    scopus 로고
    • In vivo exposure of ozone depletes vitamins C and E and induces lipid peroxidation in epidermal layers of murine skin
    • Thiele J.J., Traber M.G., Tsang K., Cross C.E., and Packer L. In vivo exposure of ozone depletes vitamins C and E and induces lipid peroxidation in epidermal layers of murine skin. Free Radic. Biol. Med. 23 (1997) 385-391
    • (1997) Free Radic. Biol. Med. , vol.23 , pp. 385-391
    • Thiele, J.J.1    Traber, M.G.2    Tsang, K.3    Cross, C.E.4    Packer, L.5
  • 65
    • 20444471551 scopus 로고    scopus 로고
    • Overexpression of superoxide dismutase or glutathione peroxidase protects against the paraquat + maneb-induced Parkinson disease phenotype
    • Thiruchelvam M., Prokopenko O., Cory-Slechta D.A., Richfield E.K., Buckley B., and Mirochnitchenko O. Overexpression of superoxide dismutase or glutathione peroxidase protects against the paraquat + maneb-induced Parkinson disease phenotype. J. Biol. Chem 280 (2005) 22530-22539
    • (2005) J. Biol. Chem , vol.280 , pp. 22530-22539
    • Thiruchelvam, M.1    Prokopenko, O.2    Cory-Slechta, D.A.3    Richfield, E.K.4    Buckley, B.5    Mirochnitchenko, O.6
  • 66
    • 0025884889 scopus 로고
    • Comparison of one-electron reduction activity against the bipyridylium herbicides, paraquat and diquat, in microsomal and mitochondrial fractions of liver, lung and kidney (in vitro)
    • Tomita M. Comparison of one-electron reduction activity against the bipyridylium herbicides, paraquat and diquat, in microsomal and mitochondrial fractions of liver, lung and kidney (in vitro). Biochem. Pharmacol. 42 (1991) 303-309
    • (1991) Biochem. Pharmacol. , vol.42 , pp. 303-309
    • Tomita, M.1
  • 71
    • 0027179230 scopus 로고
    • Phototoxic contact dermatitis with toxic hepatitis due to the percutaneous absorption of paraquat
    • Vilaplana J., Azon A., Romaguera C., and Lecha M. Phototoxic contact dermatitis with toxic hepatitis due to the percutaneous absorption of paraquat. Contact Dermatitis 29 (1993) 163-164
    • (1993) Contact Dermatitis , vol.29 , pp. 163-164
    • Vilaplana, J.1    Azon, A.2    Romaguera, C.3    Lecha, M.4
  • 72
    • 0023151447 scopus 로고
    • Occupational risk and the development of premalignant skin lesions among paraquat manufacturers
    • Wang J.D., Li W.E., Hu F.C., and Hu K.H. Occupational risk and the development of premalignant skin lesions among paraquat manufacturers. Br. J. Ind. Med. 44 (1987) 196-200
    • (1987) Br. J. Ind. Med. , vol.44 , pp. 196-200
    • Wang, J.D.1    Li, W.E.2    Hu, F.C.3    Hu, K.H.4
  • 73
    • 0019881143 scopus 로고
    • Production of hydroxyl radicals from paraquat radicals and H2O2
    • Winterbourn C.C. Production of hydroxyl radicals from paraquat radicals and H2O2. FEBS Lett. 128 (1981) 339-342
    • (1981) FEBS Lett. , vol.128 , pp. 339-342
    • Winterbourn, C.C.1
  • 74
    • 0036351376 scopus 로고    scopus 로고
    • Role of alpha class glutathione S-transferases as antioxidant enzymes in rodent tissues
    • Yang Y., Sharma R., Zimniak P., and Awasthi Y.C. Role of alpha class glutathione S-transferases as antioxidant enzymes in rodent tissues. Toxicol. Appl. Pharmacol. 182 (2002) 105-115
    • (2002) Toxicol. Appl. Pharmacol. , vol.182 , pp. 105-115
    • Yang, Y.1    Sharma, R.2    Zimniak, P.3    Awasthi, Y.C.4
  • 75
    • 33744527765 scopus 로고    scopus 로고
    • Protective effects of N-acetylcysteine treatment post acute paraquat intoxication in rats and human lung epithelial cells
    • Yeh S.T., Gue H.R., Su Y.S., Lin H.J., Hou C.C., Chen H.M., Chang M.C., and Wang Y.J. Protective effects of N-acetylcysteine treatment post acute paraquat intoxication in rats and human lung epithelial cells. Toxicology 223 (2006) 181-190
    • (2006) Toxicology , vol.223 , pp. 181-190
    • Yeh, S.T.1    Gue, H.R.2    Su, Y.S.3    Lin, H.J.4    Hou, C.C.5    Chen, H.M.6    Chang, M.C.7    Wang, Y.J.8
  • 76
    • 0010471495 scopus 로고
    • Cellular defenses against damage from reactive oxygen species
    • Yu B.P. Cellular defenses against damage from reactive oxygen species. Physiol. Rev. 74 (1994) 139-162
    • (1994) Physiol. Rev. , vol.74 , pp. 139-162
    • Yu, B.P.1
  • 78
    • 0024454035 scopus 로고
    • Expression of murine epidermal differentiation markers is tightly regulated by restricted extracellular calcium concentrations in vitro
    • Yuspa S.H., Kilkenny A.E., Steinert P.M., and Roop D.R. Expression of murine epidermal differentiation markers is tightly regulated by restricted extracellular calcium concentrations in vitro. J. Cell Biol. 109 (1989) 1207-1217
    • (1989) J. Cell Biol. , vol.109 , pp. 1207-1217
    • Yuspa, S.H.1    Kilkenny, A.E.2    Steinert, P.M.3    Roop, D.R.4
  • 79
    • 0036667555 scopus 로고    scopus 로고
    • Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression
    • Zelko I.N., Mariani T.J., and Folz R.J. Superoxide dismutase multigene family: a comparison of the CuZn-SOD (SOD1), Mn-SOD (SOD2), and EC-SOD (SOD3) gene structures, evolution, and expression. Free Radic. Biol. Med. 33 (2002) 337-349
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 337-349
    • Zelko, I.N.1    Mariani, T.J.2    Folz, R.J.3


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