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Volumn 56, Issue 6, 2005, Pages 377-383

Antioxidant and detoxifying enzymes in the liver of rats after subchronic inhalation of the mixture of cyclic hydrocarbons

Author keywords

Antioxidant enzymes; Cyclic hydrocarbons; Isoenzyme pattern SOD; Liver; Rats

Indexed keywords

BENZENE; CYCLOHEXANE; CYCLOHEXANONE; GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE; SUPEROXIDE DISMUTASE;

EID: 17844404780     PISSN: 09402993     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.etp.2005.01.002     Document Type: Article
Times cited : (13)

References (51)
  • 2
    • 0015153416 scopus 로고
    • Superoxide dismutase: Improved assays and an assay applicable to acrylamide gels
    • C.O. Beauchamp, and I. Fridovich Superoxide dismutase: improved assays and an assay applicable to acrylamide gels Anal Biochem 44 1971 276 287
    • (1971) Anal Biochem , vol.44 , pp. 276-287
    • Beauchamp, C.O.1    Fridovich, I.2
  • 3
    • 0030460451 scopus 로고    scopus 로고
    • Population toxicokinetics of benzene
    • F.Y. Bois, E.T. Jackson, and K. Pekari Population toxicokinetics of benzene Environ Health Perspect 104 Suppl. 6 1996 1405 1411
    • (1996) Environ Health Perspect , vol.104 , Issue.SUPPL. 6 , pp. 1405-1411
    • Bois, F.Y.1    Jackson, E.T.2    Pekari, K.3
  • 4
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding Anal Biochem 72 1976 248 254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 5
    • 0018963739 scopus 로고
    • Rat hepatic cytosolic glutathione-dependent enzyme protection against lipid peroxidation in the NADPH-microsomal lipid peroxidation system
    • R.F. Burk, M.J. Trumble, and R.A. Lawrence Rat hepatic cytosolic glutathione-dependent enzyme protection against lipid peroxidation in the NADPH-microsomal lipid peroxidation system Biochim Biophys Acta 618 1980 35 41
    • (1980) Biochim Biophys Acta , vol.618 , pp. 35-41
    • Burk, R.F.1    Trumble, M.J.2    Lawrence, R.A.3
  • 6
    • 0021288059 scopus 로고
    • Paraquat: Model for oxidant-initiated toxicity
    • J.S. Bus, and J.E. Gibson Paraquat: model for oxidant-initiated toxicity Environ Health Persp 55 1984 37 46
    • (1984) Environ Health Persp , vol.55 , pp. 37-46
    • Bus, J.S.1    Gibson, J.E.2
  • 7
    • 0024227428 scopus 로고
    • Molecular immunocytochemistry of the Cu,Zn superoxide dismutase in rat hepatocytes
    • L.Y. Chang, J.W. Slot, H.J. Geuze, and J.D. Crapo Molecular immunocytochemistry of the Cu,Zn superoxide dismutase in rat hepatocytes J Cell Biol 107 1988 2169 2179
    • (1988) J Cell Biol , vol.107 , pp. 2169-2179
    • Chang, L.Y.1    Slot, J.W.2    Geuze, H.J.3    Crapo, J.D.4
  • 8
    • 0035342637 scopus 로고    scopus 로고
    • Relationship between tissue concentrations of polycyclic aromatic hydrocarbons and antioxidative responses of marine mussels, Perna viridis
    • C.C.C. Cheung, G.J. Zheng, A.M.Y. Li, B.J. Richardson, and P.K.S. Lam Relationship between tissue concentrations of polycyclic aromatic hydrocarbons and antioxidative responses of marine mussels, Perna viridis Aquat Toxicol 52 2001 189 203
    • (2001) Aquat Toxicol , vol.52 , pp. 189-203
    • Cheung, C.C.C.1    Zheng, G.J.2    Li, A.M.Y.3    Richardson, B.J.4    Lam, P.K.S.5
  • 9
    • 0021288821 scopus 로고
    • Assays of glutathione peroxidase
    • L. Flohé, and W.A. Günzler Assays of glutathione peroxidase Method Enzymol 105 1984 114 121
    • (1984) Method Enzymol , vol.105 , pp. 114-121
    • Flohé, L.1    Günzler, W.A.2
  • 11
    • 0016414528 scopus 로고
    • Superoxide dismutases
    • I. Fridovich Superoxide dismutases Annu Rev Biochem 44 1975 147 159
    • (1975) Annu Rev Biochem , vol.44 , pp. 147-159
    • Fridovich, I.1
  • 12
    • 0021735773 scopus 로고
    • Ferrous ion-EDTA-stimulated phospholipid peroxidation
    • J.M.C. Gutteridge Ferrous ion-EDTA-stimulated phospholipid peroxidation Biochem J 224 1984 697 701
    • (1984) Biochem J , vol.224 , pp. 697-701
    • Gutteridge, J.M.C.1
  • 13
    • 0019741605 scopus 로고
    • Assays for differentiation of glutathione-S-transferases
    • W.H. Habig, and W.B. Jakoby Assays for differentiation of glutathione-S-transferases Method Enzymol 77 1981 398 405
    • (1981) Method Enzymol , vol.77 , pp. 398-405
    • Habig, W.H.1    Jakoby, W.B.2
  • 15
    • 0029561598 scopus 로고
    • The glutathione-S-transferase supergene family: Regulation of resistance
    • J.D. Hayes, and D.J. Pulford The glutathione-S-transferase supergene family: regulation of resistance Crit Rev Biochem Mol Biol 30 1995 445 600
    • (1995) Crit Rev Biochem Mol Biol , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 18
    • 0031616770 scopus 로고    scopus 로고
    • Antioxidant and detoxifying enzymes in the liver and kidney of pheasants after intoxication by herbicides MCPA and ANITEN I
    • K. Holovská, V. Lenártová, I. Rosival, M. Kičinková, A. Majerčiaková, and J. Legáth Antioxidant and detoxifying enzymes in the liver and kidney of pheasants after intoxication by herbicides MCPA and ANITEN I J Biochem Mol Toxicol 12 1998 235 244
    • (1998) J Biochem Mol Toxicol , vol.12 , pp. 235-244
    • Holovská, K.1    Lenártová, V.2    Rosival, I.3    Kičinková, M.4    Majerčiaková, A.5    Legáth, J.6
  • 19
    • 0024373401 scopus 로고
    • Hepatic glutathione metabolism and lipid peroxidation response to excess dietary selenomethionine and selenite in mallard ducklings
    • D.J. Hoffman, G.H. Heinz, and A.J. Krynitsky Hepatic glutathione metabolism and lipid peroxidation response to excess dietary selenomethionine and selenite in mallard ducklings J. Toxicol Environ Health 27 1989 263 271
    • (1989) J. Toxicol Environ Health , vol.27 , pp. 263-271
    • Hoffman, D.J.1    Heinz, G.H.2    Krynitsky, A.J.3
  • 20
    • 0020553197 scopus 로고
    • Sex-related difference in hepatic glutathione level and related enzyme activities in rat
    • T. Igarashi, T. Satoh, K. Ueno, and H. Kitagawa Sex-related difference in hepatic glutathione level and related enzyme activities in rat J Biochem 93 1983 33 36
    • (1983) J Biochem , vol.93 , pp. 33-36
    • Igarashi, T.1    Satoh, T.2    Ueno, K.3    Kitagawa, H.4
  • 21
    • 0021191552 scopus 로고
    • Mechanism of lipid peroxide formation in polychlorinated biphenyls (PCB) and dichlorodiphenyltrichloroethane (DDT)-poisoned rats
    • K. Kamohara, N. Yagi, and Y. Itokawa Mechanism of lipid peroxide formation in polychlorinated biphenyls (PCB) and dichlorodiphenyltrichloroethane (DDT)-poisoned rats Environ Res 34 1984 18 23
    • (1984) Environ Res , vol.34 , pp. 18-23
    • Kamohara, K.1    Yagi, N.2    Itokawa, Y.3
  • 22
    • 0025915727 scopus 로고
    • Cu,Zn superoxide dismutase is a peroximal enzyme in human fibroblast and hepatoma cells
    • G.A. Keller, T.G. Warner, K.S. Steimner, and R.A. Hallewell Cu,Zn superoxide dismutase is a peroximal enzyme in human fibroblast and hepatoma cells Proc Natl Acad Sci USA 88 1991 7381 7385
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 7381-7385
    • Keller, G.A.1    Warner, T.G.2    Steimner, K.S.3    Hallewell, R.A.4
  • 23
    • 0024269217 scopus 로고
    • Glutathione transferases-structure and catalytic activity
    • B. Mannervik, and U.H. Danielson Glutathione transferases-structure and catalytic activity CRC Crit Rev Biochem 23 1988 283 337
    • (1988) CRC Crit Rev Biochem , vol.23 , pp. 283-337
    • Mannervik, B.1    Danielson, U.H.2
  • 24
    • 85030804935 scopus 로고
    • Přehled průmyslové toxikologie
    • J. Marhold Přehled průmyslové toxikologie Avicenum Praha 1986 19 289
    • (1986) Avicenum Praha , pp. 19-289
    • Marhold, J.1
  • 25
    • 0014691242 scopus 로고
    • Superoxide dismutase: An enzymic function for erythrocuprein
    • J.M. McCord, and J. Fridovich Superoxide dismutase: an enzymic function for erythrocuprein J Biol Chem 244 1969 6049 6055
    • (1969) J Biol Chem , vol.244 , pp. 6049-6055
    • McCord, J.M.1    Fridovich, J.2
  • 26
    • 0033529261 scopus 로고    scopus 로고
    • A potential mechanism underlying the increased susceptibility of individuals with a polymorphism in NAD(P)H:quinone oxidoreductase 1 (NQO) to benzene toxicity
    • J.L. Moran, D. Siegel, and D. Ross A potential mechanism underlying the increased susceptibility of individuals with a polymorphism in NAD(P)H:quinone oxidoreductase 1 (NQO) to benzene toxicity Proc Natl Acad Sci USA 96 1999 8150 8155
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8150-8155
    • Moran, J.L.1    Siegel, D.2    Ross, D.3
  • 27
    • 0027276544 scopus 로고
    • Evidence that rat liver microsomal glutathione transferase is responsible for glutathione-dependent protection against lipid peroxidation
    • E. Mosialou, G. Ekström, A.E.P. Adaud, and R. Morgenstern Evidence that rat liver microsomal glutathione transferase is responsible for glutathione-dependent protection against lipid peroxidation Biochem Pharmacol 45 1993 1645 1651
    • (1993) Biochem Pharmacol , vol.45 , pp. 1645-1651
    • Mosialou, E.1    Ekström, G.2    Adaud, A.E.P.3    Morgenstern, R.4
  • 28
    • 0344676781 scopus 로고
    • Postintoxication hypothermia and free-radical lipid oxidation in the brain and heart of rats poisoned with organophosphorous cholinesterase inhibitors
    • V.A. Myshkin, A.F. Vakarina, S.A. Bashkatov, G.A. Sofronov, and D.A. Enikeev Postintoxication hypothermia and free-radical lipid oxidation in the brain and heart of rats poisoned with organophosphorous cholinesterase inhibitors Bull Exp Biol Med 113 1992 664 665
    • (1992) Bull Exp Biol Med , vol.113 , pp. 664-665
    • Myshkin, V.A.1    Vakarina, A.F.2    Bashkatov, S.A.3    Sofronov, G.A.4    Enikeev, D.A.5
  • 30
    • 0027352840 scopus 로고
    • Purification of Cu,Zn-superoxide dismutase isoenzymes from fish liver: Appearance of new isoforms as consequence of pollution
    • J.R. Pedrajas, J. Peinado, and J. López-barea Purification of Cu,Zn-superoxide dismutase isoenzymes from fish liver: appearance of new isoforms as consequence of pollution Free Radic Res Commun 19 1993 29 41
    • (1993) Free Radic Res Commun , vol.19 , pp. 29-41
    • Pedrajas, J.R.1    Peinado, J.2    López-Barea, J.3
  • 31
    • 0029619096 scopus 로고
    • Oxidative stress in fish exposed to model xenobiotics. Oxidatively modified forms of Cu,Zn-superoxide dismutase as potential biomarkers
    • J.R. Pedrajas, J. Peinado, and J. López-Barea Oxidative stress in fish exposed to model xenobiotics. Oxidatively modified forms of Cu,Zn-superoxide dismutase as potential biomarkers Chemico-Biologic Interact 98 1995 267 282
    • (1995) Chemico-Biologic Interact , vol.98 , pp. 267-282
    • Pedrajas, J.R.1    Peinado, J.2    López-Barea, J.3
  • 32
    • 0037073278 scopus 로고    scopus 로고
    • Comparative study of the xenobiotic metabolising system in the digestive gland of the bivalve molluscs in different aquatic ecosystems and in aquaria experiments
    • N. Petushok, T. Gabryelak, D. Palecz, L. Zavodnik, I.S. Varga, and K.A. Deer Comparative study of the xenobiotic metabolising system in the digestive gland of the bivalve molluscs in different aquatic ecosystems and in aquaria experiments Aquat Toxicol 61 2002 65 72
    • (2002) Aquat Toxicol , vol.61 , pp. 65-72
    • Petushok, N.1    Gabryelak, T.2    Palecz, D.3    Zavodnik, L.4    Varga, I.S.5    Deer, K.A.6
  • 33
    • 0024377341 scopus 로고
    • Glutathione-S-transferases: Gene structure, regulation, and biological function
    • C.B. Pickett, and A.Y.H. Lu Glutathione-S-transferases: gene structure, regulation, and biological function Annu Rev Biochem 58 1989 743 764
    • (1989) Annu Rev Biochem , vol.58 , pp. 743-764
    • Pickett, C.B.1    Lu, A.Y.H.2
  • 35
    • 0014478046 scopus 로고
    • The effect of age and sex on glutathione reductase and glutathione peroxidase activities and aerobic glutathione oxidation in rat liver homogenates
    • R.E. Pinto, and W. Bartley The effect of age and sex on glutathione reductase and glutathione peroxidase activities and aerobic glutathione oxidation in rat liver homogenates Biochem J 112 1969 109 115
    • (1969) Biochem J , vol.112 , pp. 109-115
    • Pinto, R.E.1    Bartley, W.2
  • 36
    • 0025755648 scopus 로고
    • Changes in Cu,Zn-superoxide dismutase, cytochrome c oxidase, glutathiohne peroxidase and glutathione transferase activities in copper-deficient mice and rats
    • J.R. Prohaska Changes in Cu,Zn-superoxide dismutase, cytochrome c oxidase, glutathiohne peroxidase and glutathione transferase activities in copper-deficient mice and rats J Nutr 121 1991 355 363
    • (1991) J Nutr , vol.121 , pp. 355-363
    • Prohaska, J.R.1
  • 37
    • 0027255913 scopus 로고
    • Comparison of liver glutathione peroxidase activity and mRNA in female and male mice and rats
    • J.R. Prohaska, and R.A. Sunde Comparison of liver glutathione peroxidase activity and mRNA in female and male mice and rats Comp Biochem Physiol 105B 1 1993 111 116
    • (1993) Comp Biochem Physiol , vol.105 , Issue.1 , pp. 111-116
    • Prohaska, J.R.1    Sunde, R.A.2
  • 39
    • 0026469348 scopus 로고
    • 2 plus Cu,Zn-superoxide dismutase reflects the activity of free copper released from the oxidatively damage protein
    • 2 plus Cu,Zn-superoxide dismutase reflects the activity of free copper released from the oxidatively damage protein J Biol Chem 267 1992 25371 25377
    • (1992) J Biol Chem , vol.267 , pp. 25371-25377
    • Sato, K.1    Akaike, T.2    Khono, M.3    Ando, M.4    Aeda, H.5
  • 40
    • 0025899026 scopus 로고
    • Modulation of class Pi glutathione transferase activity by sulfhydryl group modification
    • H. Shen, K. Tamai, K. Satoh, I. Hatayama, S. Tsuchida, and K. Sato Modulation of class Pi glutathione transferase activity by sulfhydryl group modification Arch Biochem Biophys 286 1991 178 182
    • (1991) Arch Biochem Biophys , vol.286 , pp. 178-182
    • Shen, H.1    Tamai, K.2    Satoh, K.3    Hatayama, I.4    Tsuchida, S.5    Sato, K.6
  • 41
    • 0018261940 scopus 로고
    • The pathology and biochemistry of paraquat
    • Amsterdam, North Holland, Excerpta Medica (CIBA Foundation Series 65)
    • Smith LL, Rose MS, Wyatt I. The pathology and biochemistry of paraquat. In: Oxygen free radicals and tissue damage. Amsterdam, North Holland, Excerpta Medica (CIBA Foundation Series 65) 1979;321-41.
    • (1979) Oxygen Free Radicals and Tissue Damage , pp. 321-341
    • Smith, L.L.1    Rose, M.S.2    Wyatt, I.3
  • 42
    • 0023947742 scopus 로고
    • Free radicals in medicine. II. Involvement in human disease
    • P.A. Southorn, and G. Powis Free radicals in medicine. II. Involvement in human disease Mayo Clin Proc 63 1988 390 408
    • (1988) Mayo Clin Proc , vol.63 , pp. 390-408
    • Southorn, P.A.1    Powis, G.2
  • 43
    • 0018565112 scopus 로고
    • Inhibition of glutathione peroxidase by cadmium and other metals ions
    • A.G. Splittgerber, and A.L. Tappel Inhibition of glutathione peroxidase by cadmium and other metals ions Arch Biochem Biophys 197 1979 534 542
    • (1979) Arch Biochem Biophys , vol.197 , pp. 534-542
    • Splittgerber, A.G.1    Tappel, A.L.2
  • 46
    • 0037340868 scopus 로고    scopus 로고
    • Homologous recombination initiated by benzene metabolites: A potential role of oxidative stress
    • L.M. Winn Homologous recombination initiated by benzene metabolites: a potential role of oxidative stress Toxicol Sci 72 2003 143 149
    • (2003) Toxicol Sci , vol.72 , pp. 143-149
    • Winn, L.M.1
  • 47
    • 0025905984 scopus 로고
    • Prooxidant and antioxidant mechanisms in aquatic organisms
    • G.W. Winston, and R.T. Di Giulio Prooxidant and antioxidant mechanisms in aquatic organisms Aquat Toxicol 19 1991 137 161
    • (1991) Aquat Toxicol , vol.19 , pp. 137-161
    • Winston, G.W.1    Di Giulio, R.T.2
  • 48
    • 0035999190 scopus 로고    scopus 로고
    • Sex-specific biotransformation and detoxification after xenobiotic exposure of primary cultured hepatocytes of European flounder (Platichthys flesus L.)
    • K. Winzer, C.J.F. Van Noorden, and A. Köhler Sex-specific biotransformation and detoxification after xenobiotic exposure of primary cultured hepatocytes of European flounder (Platichthys flesus L.) Aquat Toxicol 59 2002 17 33
    • (2002) Aquat Toxicol , vol.59 , pp. 17-33
    • Winzer, K.1    Van Noorden, C.J.F.2    Köhler, A.3
  • 49
    • 0028639528 scopus 로고
    • Lipid peroxides in hepatic, gastrointestinal and pancreatic diseases
    • D. Armstrong Plenum Press New York
    • K. Yagi Lipid peroxides in hepatic, gastrointestinal and pancreatic diseases D. Armstrong Free radicals in diagnostic medicine 1994 Plenum Press New York 165 169
    • (1994) Free Radicals in Diagnostic Medicine , pp. 165-169
    • Yagi, K.1
  • 50
    • 0025285382 scopus 로고
    • Copper-zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide
    • M.B. Yim, P.B. Chock, and E.R. Stadtman Copper-zinc superoxide dismutase catalyzes hydroxyl radical production from hydrogen peroxide Proc Natl Acad Sci USA 87 1990 5006 5010
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5006-5010
    • Yim, M.B.1    Chock, P.B.2    Stadtman, E.R.3
  • 51
    • 0025162166 scopus 로고
    • Induction of hepatic xenobiotic biotransformation enzymes in rainbow trout by β-naphthoflavone. Time course studies
    • Y.S. Zhang, T. Anderson, and L. Förlin Induction of hepatic xenobiotic biotransformation enzymes in rainbow trout by β-naphthoflavone. Time course studies Comp Biochem Physiol 95B 1990 247 252
    • (1990) Comp Biochem Physiol , vol.95 , pp. 247-252
    • Zhang, Y.S.1    Anderson, T.2    Förlin, L.3


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