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Volumn 114, Issue 6, 2014, Pages 476-484

Acute exposure to low lead levels and its implications on the activity and expression of cytosolic thioredoxin reductase in the kidney

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MARKER; LEAD; PORPHOBILINOGEN SYNTHASE; THIOREDOXIN REDUCTASE 1; KEAP1 PROTEIN, RAT; SIGNAL PEPTIDE; TXNRD1 PROTEIN, RAT;

EID: 84900012228     PISSN: 17427835     EISSN: 17427843     Source Type: Journal    
DOI: 10.1111/bcpt.12183     Document Type: Article
Times cited : (8)

References (55)
  • 1
    • 1542329045 scopus 로고    scopus 로고
    • Lead poisoning
    • Needleman H. Lead poisoning. Ann Rev Med 2004;55:209-22.
    • (2004) Ann Rev Med , vol.55 , pp. 209-222
    • Needleman, H.1
  • 2
    • 0003815871 scopus 로고    scopus 로고
    • Agency for Toxic Substances and Disease Registry. US Department of Health and Human Services, Public Health Service, Atlanta, GA
    • Agency for Toxic Substances and Disease Registry. Toxicological Profile for Lead. US Department of Health and Human Services, Public Health Service, Atlanta, GA, 2007.
    • (2007) Toxicological Profile for Lead
  • 4
    • 84877097931 scopus 로고    scopus 로고
    • Lead contamination of paint remediation workers' vehicles
    • Boraiko C, Wright EM, Ralston F. Lead contamination of paint remediation workers' vehicles. J Environ Health 2013;75:22-7.
    • (2013) J Environ Health , vol.75 , pp. 22-27
    • Boraiko, C.1    Wright, E.M.2    Ralston, F.3
  • 5
    • 0024591505 scopus 로고
    • Mechanisms of lead and cadmium nephrotoxicity
    • Goyer RA. Mechanisms of lead and cadmium nephrotoxicity. Toxicol Lett 1989;46:153-62.
    • (1989) Toxicol Lett , vol.46 , pp. 153-162
    • Goyer, R.A.1
  • 6
    • 34247623143 scopus 로고    scopus 로고
    • Biomonitoring of the adverse effects induced by the chronic exposure to lead and cadmium on kidney function: usefulness of alpha-glutathione S-transferase
    • Garçon G, Leleu B, Marez T, Zerimech F, Haguenoer JM, Furon D et al. Biomonitoring of the adverse effects induced by the chronic exposure to lead and cadmium on kidney function: usefulness of alpha-glutathione S-transferase. Sci Total Environ 2007;377:165-72.
    • (2007) Sci Total Environ , vol.377 , pp. 165-172
    • Garçon, G.1    Leleu, B.2    Marez, T.3    Zerimech, F.4    Haguenoer, J.M.5    Furon, D.6
  • 7
    • 0033002445 scopus 로고    scopus 로고
    • Environmental lead exposure and activity of delta-aminolevulinic acid dehydratase (ALA-D) in maternal and cord blood
    • Campagna D, Huel G, Girard F, Sahuquillo J, Blot P. Environmental lead exposure and activity of delta-aminolevulinic acid dehydratase (ALA-D) in maternal and cord blood. Toxicology 1999;134:143-52.
    • (1999) Toxicology , vol.134 , pp. 143-152
    • Campagna, D.1    Huel, G.2    Girard, F.3    Sahuquillo, J.4    Blot, P.5
  • 8
    • 0027439347 scopus 로고
    • Lead-protein interactions as a basis for lead toxicity
    • Goering PL. Lead-protein interactions as a basis for lead toxicity. Neurotoxicology 1993;14:45-60.
    • (1993) Neurotoxicology , vol.14 , pp. 45-60
    • Goering, P.L.1
  • 9
    • 31044445288 scopus 로고    scopus 로고
    • Involvement of some low-molecular thiols in the peroxidative mechanisms of lead and ethanol action on rat liver and kidney
    • Jurczuk M, Moniuszko-Jakoniuk J, Brzóska MM. Involvement of some low-molecular thiols in the peroxidative mechanisms of lead and ethanol action on rat liver and kidney. Toxicology 2006;219:11-21.
    • (2006) Toxicology , vol.219 , pp. 11-21
    • Jurczuk, M.1    Moniuszko-Jakoniuk, J.2    Brzóska, M.M.3
  • 10
    • 0024597762 scopus 로고
    • Free radical generation during delta-aminolevulinic acid auto-oxidation: induction by hemoglobin and connections with porphyrinpathies
    • Monteiro HP, Abdalla DSP, Augusto O, Bechara EJ. Free radical generation during delta-aminolevulinic acid auto-oxidation: induction by hemoglobin and connections with porphyrinpathies. Arch Biochem Biophys 1989;271:206-16.
    • (1989) Arch Biochem Biophys , vol.271 , pp. 206-216
    • Monteiro, H.P.1    Abdalla, D.S.P.2    Augusto, O.3    Bechara, E.J.4
  • 12
    • 84871620712 scopus 로고    scopus 로고
    • Blood thioredoxin reductase activity, oxidative stress and hematological parameters in painters and battery workers: relationship with lead and cadmium levels in blood
    • Conterato GMM, Bulcão RP, Sobieski R, Moro AM, Charão MF, Freitas FA et al. Blood thioredoxin reductase activity, oxidative stress and hematological parameters in painters and battery workers: relationship with lead and cadmium levels in blood. J Appl Toxicol 2013;33:142-50.
    • (2013) J Appl Toxicol , vol.33 , pp. 142-150
    • Conterato, G.M.M.1    Bulcão, R.P.2    Sobieski, R.3    Moro, A.M.4    Charão, M.F.5    Freitas, F.A.6
  • 13
    • 0035843863 scopus 로고    scopus 로고
    • Antioxidant effects of alpha tocopherol, ascorbic acid and L-methionine on lead induced oxidative stress to the liver, kidney and brain in rats
    • Patra RC, Swarup D, Dwivedi SK. Antioxidant effects of alpha tocopherol, ascorbic acid and L-methionine on lead induced oxidative stress to the liver, kidney and brain in rats. Toxicology 2001;162:81-8.
    • (2001) Toxicology , vol.162 , pp. 81-88
    • Patra, R.C.1    Swarup, D.2    Dwivedi, S.K.3
  • 14
    • 0035584857 scopus 로고    scopus 로고
    • Reactive oxygen species, antioxidants, and the mammalian thioredoxin system
    • Nordberg J, Arnér EJS. Reactive oxygen species, antioxidants, and the mammalian thioredoxin system. Free Radic Biol Med 2001;31:1287-312.
    • (2001) Free Radic Biol Med , vol.31 , pp. 1287-1312
    • Nordberg, J.1    Arnér, E.J.S.2
  • 15
    • 0032502720 scopus 로고    scopus 로고
    • Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue
    • Zhong L, Arner ES, Ljung J, Aslund F, Homgren A. Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue. J Biol Chem 1998;273:8581-91.
    • (1998) J Biol Chem , vol.273 , pp. 8581-8591
    • Zhong, L.1    Arner, E.S.2    Ljung, J.3    Aslund, F.4    Homgren, A.5
  • 16
    • 67349120863 scopus 로고    scopus 로고
    • Focus on mammalian thioredoxin reductases-important selenoproteins with versatile functions
    • Arner ES. Focus on mammalian thioredoxin reductases-important selenoproteins with versatile functions. Biochim Biophys Acta 2009;1790:495-526.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 495-526
    • Arner, E.S.1
  • 17
    • 29644437160 scopus 로고    scopus 로고
    • 4-Hydroxynonenal induces adaptive response and enhances PC12 cell tolerance primarily through induction of thioredoxin reductase 1 via activation of Nrf2
    • Chen Z-H, Saito Y, Yoshida Y, Sekine A, Noguchi N, Niki E. 4-Hydroxynonenal induces adaptive response and enhances PC12 cell tolerance primarily through induction of thioredoxin reductase 1 via activation of Nrf2. J Biol Chem 2005;280:41921-7.
    • (2005) J Biol Chem , vol.280 , pp. 41921-41927
    • Chen, Z.-H.1    Saito, Y.2    Yoshida, Y.3    Sekine, A.4    Noguchi, N.5    Niki, E.6
  • 18
    • 12344329415 scopus 로고    scopus 로고
    • Induction of thioredoxin reductase as an adaptive response to acrolein in human umbilical vein endothelial cells
    • Park YS, Misonou Y, Fujiwara N, Takahashi M, Miyamoto Y, Koh YH et al. Induction of thioredoxin reductase as an adaptive response to acrolein in human umbilical vein endothelial cells. Biochem Biophys Res Commun 2005;327:1058-65.
    • (2005) Biochem Biophys Res Commun , vol.327 , pp. 1058-1065
    • Park, Y.S.1    Misonou, Y.2    Fujiwara, N.3    Takahashi, M.4    Miyamoto, Y.5    Koh, Y.H.6
  • 19
    • 18244386712 scopus 로고    scopus 로고
    • Transcriptional regulation of thioredoxin reductase-1 expression by cadmium in vascular endothelial cells: role of NF-E2-related factor-2
    • Sakurai A, Nishimoto N, Himeno S, Imura N, Tsujimoto M, Kunimoto M et al. Transcriptional regulation of thioredoxin reductase-1 expression by cadmium in vascular endothelial cells: role of NF-E2-related factor-2. J Cell Physiol 2005;203:529-37.
    • (2005) J Cell Physiol , vol.203 , pp. 529-537
    • Sakurai, A.1    Nishimoto, N.2    Himeno, S.3    Imura, N.4    Tsujimoto, M.5    Kunimoto, M.6
  • 20
    • 43049122485 scopus 로고    scopus 로고
    • Effect of mercury (II) on Nrf2, thioredoxin reductase-1 and thioredoxin-1 in human monocytes
    • Wataha JC, Lewis JB, Mccloud VV, Shaw M, Omata Y, Lockwood PE et al. Effect of mercury (II) on Nrf2, thioredoxin reductase-1 and thioredoxin-1 in human monocytes. Dent Mater 2008;24:765-72.
    • (2008) Dent Mater , vol.24 , pp. 765-772
    • Wataha, J.C.1    Lewis, J.B.2    Mccloud, V.V.3    Shaw, M.4    Omata, Y.5    Lockwood, P.E.6
  • 21
    • 84945029397 scopus 로고
    • European standardized method for the determination of d-aminolevulinic acid dehydratase activity in blood
    • Berlin A, Schaller KH. European standardized method for the determination of d-aminolevulinic acid dehydratase activity in blood. Z Klin Chem Klin Biochem 1974;12:389-90.
    • (1974) Z Klin Chem Klin Biochem , vol.12 , pp. 389-390
    • Berlin, A.1    Schaller, K.H.2
  • 22
    • 0020426709 scopus 로고
    • Delta-aminolevulinic acid dehydratase assay
    • Sassa S. Delta-aminolevulinic acid dehydratase assay. Enzyme 1982;28:133-45.
    • (1982) Enzyme , vol.28 , pp. 133-145
    • Sassa, S.1
  • 23
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction
    • Ohkawa H, Ohishi N, Yagi K. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal Biochem 1979;95:351-8.
    • (1979) Anal Biochem , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 26
    • 0029187491 scopus 로고
    • Thioredoxin and thioredoxin reductase
    • doi:10.1016/0076-6879(95)52023-6.
    • Holmgren A, Björnstedt M. Thioredoxin and thioredoxin reductase. Methods Enzymol 1995;252:199-208. doi:10.1016/0076-6879(95)52023-6.
    • (1995) Methods Enzymol , vol.252 , pp. 199-208
    • Holmgren, A.1    Björnstedt, M.2
  • 27
    • 33745221410 scopus 로고    scopus 로고
    • Sublethal concentrations of diverse gold compounds inhibit mammalian cytosolic thioredoxin reductase (TrxR1)
    • Omata Y, Folan M, Shaw M, Messer RL, Lockwood PE, Hobbs D et al. Sublethal concentrations of diverse gold compounds inhibit mammalian cytosolic thioredoxin reductase (TrxR1). Toxicol In Vitro 2006;20:882-90.
    • (2006) Toxicol In Vitro , vol.20 , pp. 882-890
    • Omata, Y.1    Folan, M.2    Shaw, M.3    Messer, R.L.4    Lockwood, P.E.5    Hobbs, D.6
  • 28
    • 0015523099 scopus 로고
    • The role of superoxide anion in the autooxidation of epinephrine and a simple assay for superoxide dismutase
    • Misra HP, Fridovich I. The role of superoxide anion in the autooxidation of epinephrine and a simple assay for superoxide dismutase. J Biol Chem 1972;247:3170-5.
    • (1972) J Biol Chem , vol.247 , pp. 3170-3175
    • Misra, H.P.1    Fridovich, I.2
  • 29
    • 0018790599 scopus 로고
    • Inhibition of glutathione reductase by interaction of 2,4,6- trinitrobenzenesulfonate with active-site dithiol
    • Carlberg I, Mannervick B. Inhibition of glutathione reductase by interaction of 2, 4, 6- trinitrobenzenesulfonate with active-site dithiol. FEBS Lett 1977;98:263-6.
    • (1977) FEBS Lett , vol.98 , pp. 263-266
    • Carlberg, I.1    Mannervick, B.2
  • 31
    • 34249023638 scopus 로고    scopus 로고
    • Validation of Zebrafish (Danio rerio) reference genes for quantitative real-time RT-PCR normalization
    • Tang R, Dodd A, Lai D, Mcnabb WC, Love DR. Validation of Zebrafish (Danio rerio) reference genes for quantitative real-time RT-PCR normalization. Acta Biochim Biophys Sin 2007;39:384-90.
    • (2007) Acta Biochim Biophys Sin , vol.39 , pp. 384-390
    • Tang, R.1    Dodd, A.2    Lai, D.3    Mcnabb, W.C.4    Love, D.R.5
  • 32
    • 77954087119 scopus 로고    scopus 로고
    • Identification of valid reference genes for gene expression studies of human stomach cancer by reverse transcription-qPCR
    • Rho HW, Lee BC, Choi ES, Choi IJ, Lee YS, Goh SH. Identification of valid reference genes for gene expression studies of human stomach cancer by reverse transcription-qPCR. BMC Cancer 2010;10:1-13.
    • (2010) BMC Cancer , vol.10 , pp. 1-13
    • Rho, H.W.1    Lee, B.C.2    Choi, E.S.3    Choi, I.J.4    Lee, Y.S.5    Goh, S.H.6
  • 33
    • 82855172058 scopus 로고    scopus 로고
    • Selenium homeostasis and induction of thioredoxin reductase during long term selenite supplementation in the rat
    • Erkhembayara S, Mollbrinka A, Erikssona M, Larsen EH, Eriksson LC. Selenium homeostasis and induction of thioredoxin reductase during long term selenite supplementation in the rat. Toxicology 2011;25:254-9.
    • (2011) Toxicology , vol.25 , pp. 254-259
    • Erkhembayara, S.1    Mollbrinka, A.2    Erikssona, M.3    Larsen, E.H.4    Eriksson, L.C.5
  • 34
    • 0016652379 scopus 로고
    • The effect of chelating agents on lead excretion in rats in relation to age
    • Jugo S, Maljkovic T, Kostial K. The effect of chelating agents on lead excretion in rats in relation to age. Environ Res 1975;10:271-9.
    • (1975) Environ Res , vol.10 , pp. 271-279
    • Jugo, S.1    Maljkovic, T.2    Kostial, K.3
  • 35
    • 0016762639 scopus 로고
    • Resorption of lead compounds from the peritoneal cavity in rats
    • Jugo S, Kello D. Resorption of lead compounds from the peritoneal cavity in rats. Health Phys 1975;28:617-18.
    • (1975) Health Phys , vol.28 , pp. 617-618
    • Jugo, S.1    Kello, D.2
  • 36
    • 0004152005 scopus 로고
    • World Health Organization. International Programme on Chemical Safety. Environmental Health Criteria series 165. WHO, Geneva
    • World Health Organization. Inorganic Lead. International Programme on Chemical Safety. Environmental Health Criteria series 165. WHO, Geneva, 1995.
    • (1995) Inorganic Lead
  • 37
    • 0028283263 scopus 로고
    • Validity of lead exposure markers in diagnosis and surveillance
    • Graziano JH. Validity of lead exposure markers in diagnosis and surveillance. Clin Chem 1994;40:1387-90.
    • (1994) Clin Chem , vol.40 , pp. 1387-1390
    • Graziano, J.H.1
  • 38
    • 0027445855 scopus 로고
    • The speciation of lead in erythrocytes in relation to lead toxicity: case studies of two lead-exposed workers
    • Church HJ, Day JP, Braithwaite RA, Brown SS. The speciation of lead in erythrocytes in relation to lead toxicity: case studies of two lead-exposed workers. Neurotoxicology 1993;14:359-64.
    • (1993) Neurotoxicology , vol.14 , pp. 359-364
    • Church, H.J.1    Day, J.P.2    Braithwaite, R.A.3    Brown, S.S.4
  • 39
    • 0023630782 scopus 로고
    • Regulatory roles of high-affinity metal-binding proteins in mediating lead effects on delta-aminolevulinic acid dehydratase
    • Goering PL, Fowler BA. Regulatory roles of high-affinity metal-binding proteins in mediating lead effects on delta-aminolevulinic acid dehydratase. Ann N Y Acad Sci 1987;514:235-47.
    • (1987) Ann N Y Acad Sci , vol.514 , pp. 235-247
    • Goering, P.L.1    Fowler, B.A.2
  • 40
    • 0019868206 scopus 로고
    • Evidence of increased synthesis of & aminolevulinic acid dehydratase in experimental lead-poisoning
    • Fujita H, Orh Y, Sano S. Evidence of increased synthesis of & aminolevulinic acid dehydratase in experimental lead-poisoning. Biochim Biophys Acta 1981;678:39-50.
    • (1981) Biochim Biophys Acta , vol.678 , pp. 39-50
    • Fujita, H.1    Orh, Y.2    Sano, S.3
  • 41
    • 0029080228 scopus 로고
    • Effect of treatment with mercury chloride and lead acetate during the second stage of rapid postnatal brain growth on delta-aminolevulinic acid dehydratase (ALA-D) activity in brain, liver, kidney and blood of suckling rats
    • Rocha JB, Pereira ME, Emanuelli T, Christofari RS, Souza DO. Effect of treatment with mercury chloride and lead acetate during the second stage of rapid postnatal brain growth on delta-aminolevulinic acid dehydratase (ALA-D) activity in brain, liver, kidney and blood of suckling rats. Toxicology 1995;100:27-37.
    • (1995) Toxicology , vol.100 , pp. 27-37
    • Rocha, J.B.1    Pereira, M.E.2    Emanuelli, T.3    Christofari, R.S.4    Souza, D.O.5
  • 42
    • 0022390119 scopus 로고
    • Mechanism of renal lead binding protein reversal of δ-aminolevulinic acid dehydratase inhibition by lead
    • Goering PL, Fowler BA. Mechanism of renal lead binding protein reversal of δ-aminolevulinic acid dehydratase inhibition by lead. J Pharmacol Exp Ther 1985;234:365-71.
    • (1985) J Pharmacol Exp Ther , vol.234 , pp. 365-371
    • Goering, P.L.1    Fowler, B.A.2
  • 43
    • 0021922442 scopus 로고
    • High-affinity lead binding proteins in rat kidney cytosol mediate cell-free nuclear translocation of lead
    • Mistry P, Lucier GW, Fowler BA. High-affinity lead binding proteins in rat kidney cytosol mediate cell-free nuclear translocation of lead. J Pharmacol Exp Ther 1985;232:462-9.
    • (1985) J Pharmacol Exp Ther , vol.232 , pp. 462-469
    • Mistry, P.1    Lucier, G.W.2    Fowler, B.A.3
  • 44
    • 18944362483 scopus 로고    scopus 로고
    • Blood lead levels- United States, 1999-2002
    • Centers for Disease Control and Prevention (CDC)
    • Centers for Disease Control and Prevention (CDC). Blood lead levels- United States, 1999-2002. MMWR Morb Mortal Wkly Rep 2005;54:513-16.
    • (2005) MMWR Morb Mortal Wkly Rep , vol.54 , pp. 513-516
  • 45
    • 28744434298 scopus 로고    scopus 로고
    • Differential oxidation of thioredoxin-1, thioredoxin-2, and glutathione by metal ions
    • Hansen JM, Zhang H, Jones DP. Differential oxidation of thioredoxin-1, thioredoxin-2, and glutathione by metal ions. Free Radic Biol Med 2006;40:138-45.
    • (2006) Free Radic Biol Med , vol.40 , pp. 138-145
    • Hansen, J.M.1    Zhang, H.2    Jones, D.P.3
  • 46
    • 0025317268 scopus 로고
    • Glutathione: toxicological implications
    • Reed DJ. Glutathione: toxicological implications. Annu Rev Pharmacol Toxicol 1990;30:603-31.
    • (1990) Annu Rev Pharmacol Toxicol , vol.30 , pp. 603-631
    • Reed, D.J.1
  • 47
    • 0242501629 scopus 로고    scopus 로고
    • Thioredoxin reductase, a redox active selenoprotein, is secreted by normal and neoplastic cells: presence in human plasma
    • Söderberg A, Sahaf B, Rosén A. Thioredoxin reductase, a redox active selenoprotein, is secreted by normal and neoplastic cells: presence in human plasma. Cancer Res 2000;60:2281-9.
    • (2000) Cancer Res , vol.60 , pp. 2281-2289
    • Söderberg, A.1    Sahaf, B.2    Rosén, A.3
  • 48
    • 34247214633 scopus 로고    scopus 로고
    • Regulation of antioxidants and phase 2 enzymes by shear-induced reactive oxygen species in endothelial cells
    • Jones CI, Zhu H, Martin SF, Han Z, Li Y, Alevriadou BR. Regulation of antioxidants and phase 2 enzymes by shear-induced reactive oxygen species in endothelial cells. Ann Biomed Eng 2007;35:683-93.
    • (2007) Ann Biomed Eng , vol.35 , pp. 683-693
    • Jones, C.I.1    Zhu, H.2    Martin, S.F.3    Han, Z.4    Li, Y.5    Alevriadou, B.R.6
  • 49
    • 77952332154 scopus 로고    scopus 로고
    • Cytochrome P450 2A5 Constitutive expression and induction by heavy metals is dependent on redox-sensitive transcription factor Nrf2 in liver
    • Lämsä V, Levonen AL, Leinonen H, Yla-Herttuala S, Yamamoto M, Hakkola J. Cytochrome P450 2A5 Constitutive expression and induction by heavy metals is dependent on redox-sensitive transcription factor Nrf2 in liver. Chem Res Toxicol 2010;23:977-85.
    • (2010) Chem Res Toxicol , vol.23 , pp. 977-985
    • Lämsä, V.1    Levonen, A.L.2    Leinonen, H.3    Yla-Herttuala, S.4    Yamamoto, M.5    Hakkola, J.6
  • 50
    • 0036249958 scopus 로고    scopus 로고
    • Induction of thioredoxin reductase gene expression by peroxynitrite in human umbilical vein endothelial cells
    • Park YS, Fujiwara N, Koh YH, Miyamoto Y, Suzuki K, Honke K et al. Induction of thioredoxin reductase gene expression by peroxynitrite in human umbilical vein endothelial cells. Biol Chem 2002;383:683-91.
    • (2002) Biol Chem , vol.383 , pp. 683-691
    • Park, Y.S.1    Fujiwara, N.2    Koh, Y.H.3    Miyamoto, Y.4    Suzuki, K.5    Honke, K.6
  • 51
    • 33645218947 scopus 로고    scopus 로고
    • Short-interfering RNA mediated silencing of thioredoxin reductase-1 alters the sensitivity of HeLa cells toward cadmium
    • Nishimoto M, Sakaue M, Hara S. Short-interfering RNA mediated silencing of thioredoxin reductase-1 alters the sensitivity of HeLa cells toward cadmium. Biol Pharm Bull 2006;29:543-6.
    • (2006) Biol Pharm Bull , vol.29 , pp. 543-546
    • Nishimoto, M.1    Sakaue, M.2    Hara, S.3
  • 52
    • 0028072911 scopus 로고
    • Thioredoxin-dependent peroxide reductase from yeast
    • Chae HZ, Chung SJ, Rhee SG. Thioredoxin-dependent peroxide reductase from yeast. J Biol Chem 1994;269:27670-8.
    • (1994) J Biol Chem , vol.269 , pp. 27670-27678
    • Chae, H.Z.1    Chung, S.J.2    Rhee, S.G.3
  • 53
    • 0029031370 scopus 로고
    • Human thioredoxin reductase directly reduces lipid hydroperoxides by NADPH and selenocystine strongly stimulates the reaction via catalytically generated selenols
    • Bjornstedt M, Hamberg M, Kumar S, Xue J, Holmgren A. Human thioredoxin reductase directly reduces lipid hydroperoxides by NADPH and selenocystine strongly stimulates the reaction via catalytically generated selenols. J Biol Chem 1995;270:11761-4.
    • (1995) J Biol Chem , vol.270 , pp. 11761-11764
    • Bjornstedt, M.1    Hamberg, M.2    Kumar, S.3    Xue, J.4    Holmgren, A.5
  • 54
    • 13844297078 scopus 로고    scopus 로고
    • Lead-induced dysregulation of superoxide dismutases, catalase, glutathione peroxidase, and guanylate cyclase
    • Farmand F, Ehdaie A, Roberts CK, Sindhu RK. Lead-induced dysregulation of superoxide dismutases, catalase, glutathione peroxidase, and guanylate cyclase. Environ Res 2005;98:33-9.
    • (2005) Environ Res , vol.98 , pp. 33-39
    • Farmand, F.1    Ehdaie, A.2    Roberts, C.K.3    Sindhu, R.K.4
  • 55
    • 0030070035 scopus 로고    scopus 로고
    • Effects of exposure to lead on selected biochemical and haematological variables
    • Solliway BM, Schaffer A, Pratt H, Yannai S. Effects of exposure to lead on selected biochemical and haematological variables. Pharmacol Toxicol 1996;78:18-22.
    • (1996) Pharmacol Toxicol , vol.78 , pp. 18-22
    • Solliway, B.M.1    Schaffer, A.2    Pratt, H.3    Yannai, S.4


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