메뉴 건너뛰기




Volumn 21, Issue 3, 2007, Pages 355-363

Paraquat-induced oxidative stress and dysfunction of cellular redox systems including antioxidative defense enzymes glutathione peroxidase and thioredoxin reductase

Author keywords

Cytotoxicity; Glutathione peroxidase; Glyceraldehyde 3 phosphate dehydrogenase; Oxidative stress; Paraquat; Thioredoxin reductase

Indexed keywords

GLUTATHIONE; GLUTATHIONE PEROXIDASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HYDROGEN PEROXIDE; PARAQUAT; PEROXIREDOXIN; REACTIVE OXYGEN METABOLITE; THIOMALIC ACID; THIOREDOXIN; THIOREDOXIN REDUCTASE; XANTHINE; XANTHINE OXIDASE;

EID: 33947416994     PISSN: 08872333     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tiv.2006.09.003     Document Type: Article
Times cited : (44)

References (37)
  • 1
    • 0033521019 scopus 로고    scopus 로고
    • Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B
    • Barrett W.C., DeGnore J.P., Keng Y.-F., Zhang Z.-Y., Yim M.B., and Chock P.B. Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B. The Journal of Biological Chemistry 274 (1999) 34543-34546
    • (1999) The Journal of Biological Chemistry , vol.274 , pp. 34543-34546
    • Barrett, W.C.1    DeGnore, J.P.2    Keng, Y.-F.3    Zhang, Z.-Y.4    Yim, M.B.5    Chock, P.B.6
  • 2
    • 0029031370 scopus 로고
    • Human thioredoxin reductase directly reduces lipid hydroperoxides by NADPH and selenocystine strongly stimulates the reaction via catalytically generated selenols
    • Björnstedt M., Hamberg M., Kumar S., Xue J., and Holmgren A. Human thioredoxin reductase directly reduces lipid hydroperoxides by NADPH and selenocystine strongly stimulates the reaction via catalytically generated selenols. The Journal of Biological Chemistry 270 (1995) 11761-11764
    • (1995) The Journal of Biological Chemistry , vol.270 , pp. 11761-11764
    • Björnstedt, M.1    Hamberg, M.2    Kumar, S.3    Xue, J.4    Holmgren, A.5
  • 4
    • 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. Biochemical and Biophysical Research Communications 58 (1974) 749-755
    • (1974) Biochemical and Biophysical Research Communications , vol.58 , pp. 749-755
    • Bus, J.S.1    Aust, S.D.2    Gibson, J.E.3
  • 7
    • 0000385805 scopus 로고    scopus 로고
    • Isoforms of mammalian peroxiredoxin that reduce peroxides in presence of thioredoxin
    • Chae H.Z., Kang S.W., and Rhee S.G. Isoforms of mammalian peroxiredoxin that reduce peroxides in presence of thioredoxin. Methods in Enzymology 300 (1999) 219-226
    • (1999) Methods in Enzymology , vol.300 , pp. 219-226
    • Chae, H.Z.1    Kang, S.W.2    Rhee, S.G.3
  • 8
    • 0001445231 scopus 로고    scopus 로고
    • Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin
    • Chae H.Z., Kim H.J., Kang S.W., and Rhee S.G. Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin. Diabetes Research and Clinical Practice 45 (1999) 101-112
    • (1999) Diabetes Research and Clinical Practice , vol.45 , pp. 101-112
    • Chae, H.Z.1    Kim, H.J.2    Kang, S.W.3    Rhee, S.G.4
  • 10
    • 0021360660 scopus 로고
    • Mechanism of selenium-glutathione peroxidase and its inhibition by mercaptocarboxylic acids and other mercaptans
    • Chaudiere J., Wilhelmsen E.C., and Tappel A.L. Mechanism of selenium-glutathione peroxidase and its inhibition by mercaptocarboxylic acids and other mercaptans. The Journal of Biological Chemistry 259 (1984) 1043-1050
    • (1984) The Journal of Biological Chemistry , vol.259 , pp. 1043-1050
    • Chaudiere, J.1    Wilhelmsen, E.C.2    Tappel, A.L.3
  • 11
    • 0022614962 scopus 로고
    • Determination of the number of endothelial cells in culture using an acid phosphatase assay
    • Connolly D.T., Knight M.B., Harakas N.K., Wittwer A.J., and Feder J. Determination of the number of endothelial cells in culture using an acid phosphatase assay. Analytical Biochemistry 152 (1986) 136-140
    • (1986) Analytical Biochemistry , vol.152 , pp. 136-140
    • Connolly, D.T.1    Knight, M.B.2    Harakas, N.K.3    Wittwer, A.J.4    Feder, J.5
  • 14
    • 0032956855 scopus 로고    scopus 로고
    • Differential protein S-thiolation of glyceraldehyde-3-phosphate dehydrogenase isoenzymes influences sensitivity to oxidative stress
    • Grant C.M., Quinn K.A., and Dawes I.W. Differential protein S-thiolation of glyceraldehyde-3-phosphate dehydrogenase isoenzymes influences sensitivity to oxidative stress. Molecular and Cellular Biology 19 (1999) 2650-2656
    • (1999) Molecular and Cellular Biology , vol.19 , pp. 2650-2656
    • Grant, C.M.1    Quinn, K.A.2    Dawes, I.W.3
  • 15
    • 0027238801 scopus 로고
    • Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase
    • Gravina S.A., and Mieyal J.J. Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase. Biochemistry 32 (1993) 3368-3376
    • (1993) Biochemistry , vol.32 , pp. 3368-3376
    • Gravina, S.A.1    Mieyal, J.J.2
  • 16
    • 0034534165 scopus 로고    scopus 로고
    • Antioxidant function of thioredoxin and glutaredoxin systems
    • Holmgren A. Antioxidant function of thioredoxin and glutaredoxin systems. Antioxidants & Redox Signaling 2 (2000) 811-820
    • (2000) Antioxidants & Redox Signaling , vol.2 , pp. 811-820
    • Holmgren, A.1
  • 18
    • 0019951360 scopus 로고
    • Relevance of NADPH depletion and mixed disulphide formation in rat lung to the mechanism of cell damage following paraquat administration
    • Keeling P.L., and Smith L.L. Relevance of NADPH depletion and mixed disulphide formation in rat lung to the mechanism of cell damage following paraquat administration. Biochemical Pharmacology 31 (1982) 3243-3249
    • (1982) Biochemical Pharmacology , vol.31 , pp. 3243-3249
    • Keeling, P.L.1    Smith, L.L.2
  • 20
    • 0032543374 scopus 로고
    • Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione, catalysis by glutaredoxin
    • Lind C., Gerdes R., Schuppe-Koistinen I., and Cotgreave I.A. Studies on the mechanism of oxidative modification of human glyceraldehyde-3-phosphate dehydrogenase by glutathione, catalysis by glutaredoxin. Biochemical and Biophysical Research Communications 247 (1992) 481-486
    • (1992) Biochemical and Biophysical Research Communications , vol.247 , pp. 481-486
    • Lind, C.1    Gerdes, R.2    Schuppe-Koistinen, I.3    Cotgreave, I.A.4
  • 22
    • 0025895933 scopus 로고
    • Thioltransferase in human red blood cells, purification and properties
    • Mieyal J.J., Starke D.W., Gravina S.A., Dothey C., and Chung J.S. Thioltransferase in human red blood cells, purification and properties. Biochemistry 30 (1991) 6088-6097
    • (1991) Biochemistry , vol.30 , pp. 6088-6097
    • Mieyal, J.J.1    Starke, D.W.2    Gravina, S.A.3    Dothey, C.4    Chung, J.S.5
  • 24
    • 0028170673 scopus 로고
    • S-thiolation of glyceraldehydes-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes
    • Ravichandran V., Seres T., Moriguchi T., Thomas J.A., and Johnston Jr. R.B. S-thiolation of glyceraldehydes-3-phosphate dehydrogenase induced by the phagocytosis-associated respiratory burst in blood monocytes. The Journal of Biological Chemistry 269 (1994) 25010-25015
    • (1994) The Journal of Biological Chemistry , vol.269 , pp. 25010-25015
    • Ravichandran, V.1    Seres, T.2    Moriguchi, T.3    Thomas, J.A.4    Johnston Jr., R.B.5
  • 25
    • 2542486403 scopus 로고    scopus 로고
    • Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue
    • Reddy S., Jones A.D., Cross C.E., Wong P.S., and Van Der Vliet A. Inactivation of creatine kinase by S-glutathionylation of the active-site cysteine residue. The Biochemical Journal 347 (2000) 821-827
    • (2000) The Biochemical Journal , vol.347 , pp. 821-827
    • Reddy, S.1    Jones, A.D.2    Cross, C.E.3    Wong, P.S.4    Van Der Vliet, A.5
  • 27
    • 0028204459 scopus 로고
    • S-thiolation of human endothelial cell glyceraldehydes-3-phosphate dehydrogenase after hydrogen peroxide treatment
    • Schuppe-Koistinen I., Moldéus P., Bergman T., and Cotgreave I.A. S-thiolation of human endothelial cell glyceraldehydes-3-phosphate dehydrogenase after hydrogen peroxide treatment. European Journal of Biochemistry 221 (1994) 1033-1037
    • (1994) European Journal of Biochemistry , vol.221 , pp. 1033-1037
    • Schuppe-Koistinen, I.1    Moldéus, P.2    Bergman, T.3    Cotgreave, I.A.4
  • 28
    • 0032030445 scopus 로고    scopus 로고
    • Mitochondrial NADH-quinone oxidoreductase of the outer membrane is responsible for paraquat cytotoxicity in rat livers
    • Shimada H., Hirai K., Shimamura E., and Pan J. Mitochondrial NADH-quinone oxidoreductase of the outer membrane is responsible for paraquat cytotoxicity in rat livers. Archives of Biochemistry and Biophysics 351 (1998) 75-81
    • (1998) Archives of Biochemistry and Biophysics , vol.351 , pp. 75-81
    • Shimada, H.1    Hirai, K.2    Shimamura, E.3    Pan, J.4
  • 31
    • 0038015010 scopus 로고    scopus 로고
    • Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase)
    • Starke D.W., Chock P.B., and Mieyal J.J. Glutathione-thiyl radical scavenging and transferase properties of human glutaredoxin (thioltransferase). The Journal of Biological Chemistry 278 (2003) 14607-14613
    • (2003) The Journal of Biological Chemistry , vol.278 , pp. 14607-14613
    • Starke, D.W.1    Chock, P.B.2    Mieyal, J.J.3
  • 32
    • 0037201949 scopus 로고    scopus 로고
    • Role of antioxidants in paraquat toxicity
    • Suntres Z.E. Role of antioxidants in paraquat toxicity. Toxicology 30 (2002) 65-77
    • (2002) Toxicology , vol.30 , pp. 65-77
    • Suntres, Z.E.1
  • 33
    • 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 Radical Biology and Medicine 27 (1998) 588-595
    • (1998) Free Radical Biology and Medicine , vol.27 , pp. 588-595
    • Tampo, Y.1    Tsukamoto, M.2    Yonaha, M.3
  • 34
    • 0029015864 scopus 로고
    • Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation
    • Thomas J.A., Poland B., and Honzatko R. Protein sulfhydryls and their role in the antioxidant function of protein S-thiolation. Archives of Biochemistry and Biophysics 319 (1995) 1-9
    • (1995) Archives of Biochemistry and Biophysics , vol.319 , pp. 1-9
    • Thomas, J.A.1    Poland, B.2    Honzatko, R.3
  • 35
    • 0034097757 scopus 로고    scopus 로고
    • Paraquat-induced membrane dysfunction in pulmonary microvascular endothelial cells
    • Tsukamoto M., Tampo Y., Sawada M., and Yonaha M. Paraquat-induced membrane dysfunction in pulmonary microvascular endothelial cells. Pharmacology and Toxicology 86 (2000) 102-109
    • (2000) Pharmacology and Toxicology , vol.86 , pp. 102-109
    • Tsukamoto, M.1    Tampo, Y.2    Sawada, M.3    Yonaha, M.4
  • 36
    • 0037081736 scopus 로고    scopus 로고
    • Paraquat-induced oxidative stress and dysfunction of the glutathione redox cycle in pulmonary microvascular endothelial cells
    • Tsukamoto M., Tampo Y., Sawada M., and Yonaha M. Paraquat-induced oxidative stress and dysfunction of the glutathione redox cycle in pulmonary microvascular endothelial cells. Toxicology and Applied Pharmacology 178 (2002) 82-92
    • (2002) Toxicology and Applied Pharmacology , vol.178 , pp. 82-92
    • Tsukamoto, M.1    Tampo, Y.2    Sawada, M.3    Yonaha, M.4
  • 37
    • 0034674566 scopus 로고    scopus 로고
    • Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations
    • Zhong L., and Holmgren A. Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations. The Journal of Biological Chemistry 275 (2000) 18121-18128
    • (2000) The Journal of Biological Chemistry , vol.275 , pp. 18121-18128
    • Zhong, L.1    Holmgren, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.