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Volumn 24, Issue 4, 2011, Pages 559-567

Initial response and cellular protection through the Keap1/Nrf2 system during the exposure of primary mouse hepatocytes to 1,2-naphthoquinone

Author keywords

[No Author keywords available]

Indexed keywords

1,2 NAPHTHOQUINONE; GLUCURONOSYLTRANSFERASE; KELCH LIKE ECH ASSOCIATED PROTEIN 1; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TRANSCRIPTION FACTOR NRF2;

EID: 79954465791     PISSN: 0893228X     EISSN: 15205010     Source Type: Journal    
DOI: 10.1021/tx100427p     Document Type: Article
Times cited : (55)

References (45)
  • 2
    • 33746906658 scopus 로고    scopus 로고
    • Uptake and UV-photooxidation of gas-phase PAHs on the surface of atmospheric water films. 1. Naphthalene
    • DOI 10.1021/jp062560b
    • Chen, J., Ehrenhauser, F. S., Valsaraj, K. T., and Wornat, M. J. (2006) Uptake and UV-photooxidation of gas-phase PAHs on the surface of atmospheric water films. 1. Naphthalene J. Phys. Chem. A 110, 9161-9168 (Pubitemid 44187341)
    • (2006) Journal of Physical Chemistry A , vol.110 , Issue.29 , pp. 9161-9168
    • Chen, J.1    Ehrenhauser, F.S.2    Valsaraj, K.T.3    Wornat, M.J.4
  • 3
    • 0032969410 scopus 로고    scopus 로고
    • Aldose reductase catalyzes the oxidation of naphthalene-1,2-dihydrodiol for the formation of ortho-naphthoquinone
    • Sugiyama, K., Wang, T. C., Simpson, J. T., Rodriguez, L., Kador, P. F., and Sato, S. (1999) Aldose reductase catalyzes the oxidation of naphthalene-1, 2-dihydrodiol for the formation of ortho-naphthoquinone Drug Metab. Dispos. 27, 60-67 (Pubitemid 29061001)
    • (1999) Drug Metabolism and Disposition , vol.27 , Issue.1 , pp. 60-67
    • Sugiyama, K.1    Wang, T.-C.L.2    Simpson, J.T.3    Rodriguez, L.4    Kador, P.F.5    Sato, S.6
  • 4
    • 0030592950 scopus 로고    scopus 로고
    • Characterisation of the toxic metabolite(s) of naphthalene
    • DOI 10.1016/S0300-483X(96)03515-9, PII S0300483X96035159
    • Wilson, A. S., Davis, C. D., Williams, D. P., Buckpitt, A. R., Pirmohamed, M., and Park, B. K. (1996) Characterisation of the toxic metabolite(s) of naphthalene Toxicology 114, 233-242 (Pubitemid 26421936)
    • (1996) Toxicology , vol.114 , Issue.3 , pp. 233-242
    • Wilson, A.S.1    Davis, C.D.2    Williams, D.P.3    Buckpitt, A.R.4    Pirmohamed, M.5    Park, B.K.6
  • 6
    • 36349037272 scopus 로고    scopus 로고
    • Chemical knockdown of protein-tyrosine phosphatase 1B by 1,2-naphthoquinone through covalent modification causes persistent transactivation of epidermal growth factor receptor
    • DOI 10.1074/jbc.M705224200
    • Iwamoto, N., Sumi, D., Ishii, T., Uchida, K., Cho, A. K., Froines, J. R., and Kumagai, Y. (2007) Chemical knockdown of protein-tyrosine phosphatase 1B by 1,2-naphthoquinone through covalent modification causes persistent transactivation of epidermal growth factor receptor J. Biol. Chem. 282, 33396-33404 (Pubitemid 350159512)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.46 , pp. 33396-33404
    • Iwamoto, N.1    Sumi, D.2    Ishii, T.3    Uchida, K.4    Cho, A.K.5    Froines, J.R.6    Kumagai, Y.7
  • 7
    • 34547133038 scopus 로고    scopus 로고
    • 1,2-Naphthoquinone disrupts the function of cAMP response element-binding protein through covalent modification
    • DOI 10.1016/j.bbrc.2007.07.024, PII S0006291X07014854
    • Endo, A., Sumi, D., and Kumagai, Y. (2007) 1,2-Naphthoquinone disrupts the function of cAMP response element-binding protein through covalent modification Biochem. Biophys. Res. Commun. 361, 243-248 (Pubitemid 47102292)
    • (2007) Biochemical and Biophysical Research Communications , vol.361 , Issue.1 , pp. 243-248
    • Endo, A.1    Sumi, D.2    Kumagai, Y.3
  • 8
    • 33846868665 scopus 로고    scopus 로고
    • Formation of depurinating N3adenine and N7guanine adducts after reaction of 1,2-naphthoquinone or enzyme-activated 1,2-dihydroxynaphthalene with DNA. Implications for the mechanism of tumor initiation by naphthalene
    • DOI 10.1016/j.cbi.2006.12.007, PII S0009279706003577
    • Saeed, M., Higginbotham, S., Rogan, E., and Cavalieri, E. (2007) Formation of depurinating N3adenine and N7guanine adducts after reaction of 1,2-naphthoquinone or enzyme-activated 1,2-dihydroxynaphthalene with DNA. Implications for the mechanism of tumor initiation by naphthalene Chem.-Biol. Interact. 165, 175-188 (Pubitemid 46227364)
    • (2007) Chemico-Biological Interactions , vol.165 , Issue.3 , pp. 175-188
    • Saeed, M.1    Higginbotham, S.2    Rogan, E.3    Cavalieri, E.4
  • 9
    • 33645846293 scopus 로고    scopus 로고
    • Inhibition of endothelial nitric oxide synthase activity and suppression of endothelium-dependent vasorelaxation by 1,2-naphthoquinone, a component of diesel exhaust particles
    • Sun, Y., Taguchi, K., Sumi, D., Yamano, S., and Kumagai, Y. (2006) Inhibition of endothelial nitric oxide synthase activity and suppression of endothelium-dependent vasorelaxation by 1,2-naphthoquinone, a component of diesel exhaust particles Arch. Toxicol. 80, 280-285
    • (2006) Arch. Toxicol. , vol.80 , pp. 280-285
    • Sun, Y.1    Taguchi, K.2    Sumi, D.3    Yamano, S.4    Kumagai, Y.5
  • 10
    • 29044448156 scopus 로고    scopus 로고
    • 1,2-Naphthoquinone activates vanilloid receptor 1 through increased protein tyrosine phosphorylation, leading to contraction of guinea pig trachea
    • DOI 10.1016/j.taap.2005.06.015, PII S0041008X05003807
    • Kikuno, S., Taguchi, K., Iwamoto, N., Yamano, S., Cho, A. K., Froines, J. R., and Kumagai, Y. (2006) 1,2-Naphthoquinone activates vanilloid receptor 1 through increased protein tyrosine phosphorylation, leading to contraction of guinea pig trachea Toxicol. Appl. Pharmacol. 210, 47-54 (Pubitemid 41790550)
    • (2006) Toxicology and Applied Pharmacology , vol.210 , Issue.1-2 , pp. 47-54
    • Kikuno, S.1    Taguchi, K.2    Iwamoto, N.3    Yamano, S.4    Cho, A.K.5    Froines, J.R.6    Kumagai, Y.7
  • 11
    • 0036227531 scopus 로고    scopus 로고
    • Oxidation of proximal protein sulfhydryls by phenanthraquinone, a component of diesel exhaust particles
    • DOI 10.1021/tx0100993
    • Kumagai, Y., Koide, S., Taguchi, K., Endo, A., Nakai, Y., Yoshikawa, T., and Shimojo, N. (2002) Oxidation of proximal protein sulfhydryls by phenanthraquinone, a component of diesel exhaust particles Chem. Res. Toxicol. 15, 483-489 (Pubitemid 34326929)
    • (2002) Chemical Research in Toxicology , vol.15 , Issue.4 , pp. 483-489
    • Kumagai, Y.1    Koide, S.2    Taguchi, K.3    Endo, A.4    Nakai, Y.5    Yoshikawa, T.6    Shimojo, N.7
  • 12
    • 34547093431 scopus 로고    scopus 로고
    • An approach to evaluate two-electron reduction of 9,10-phenanthraquinone and redox activity of the hydroquinone associated with oxidative stress
    • DOI 10.1016/j.freeradbiomed.2007.05.021, PII S0891584907003528
    • Taguchi, K., Fujii, S., Yamano, S., Cho, A. K., Kamisuki, S., Nakai, Y., Sugawara, F., Froines, J. R., and Kumagai, Y. (2007) An approach to evaluate two-electron reduction of 9,10-phenanthraquinone and redox activity of the hydroquinone associated with oxidative stress Free Radical Biol. Med. 43, 789-799 (Pubitemid 47102127)
    • (2007) Free Radical Biology and Medicine , vol.43 , Issue.5 , pp. 789-799
    • Taguchi, K.1    Fujii, S.2    Yamano, S.3    Cho, A.K.4    Kamisuki, S.5    Nakai, Y.6    Sugawara, F.7    Froines, J.R.8    Kumagai, Y.9
  • 13
    • 0001083672 scopus 로고
    • Possible reactions of 1,2-naphthaquinone in the eye
    • Rees, J. R. and Pirie, A. (1967) Possible reactions of 1,2-naphthaquinone in the eye Biochem. J. 102, 853-863
    • (1967) Biochem. J. , vol.102 , pp. 853-863
    • Rees, J.R.1    Pirie, A.2
  • 14
    • 0032827002 scopus 로고    scopus 로고
    • Regulatory mechanisms of cellular response to oxidative stress
    • DOI 10.1080/10715769900300881
    • Itoh, K., Ishii, T., Wakabayashi, N., and Yamamoto, M. (1999) Regulatory mechanisms of cellular response to oxidative stress Free Radical Res. 31, 319-324 (Pubitemid 29452857)
    • (1999) Free Radical Research , vol.31 , Issue.4 , pp. 319-324
    • Itoh, K.1    Ishii, T.2    Wakabayashi, N.3    Yamamoto, M.4
  • 15
    • 0034717329 scopus 로고    scopus 로고
    • Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages
    • DOI 10.1074/jbc.275.21.16023
    • Ishii, T., Itoh, K., Takahashi, S., Sato, H., Yanagawa, T., Katoh, Y., Bannai, S., and Yamamoto, M. (2000) Transcription factor Nrf2 coordinately regulates a group of oxidative stress-inducible genes in macrophages J. Biol. Chem. 275, 16023-16029 (Pubitemid 30366908)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.21 , pp. 16023-16029
    • Ishii, T.1    Itoh, K.2    Takahashi, S.3    Sato, H.4    Yanagawa, T.5    Katoh, Y.6    Bannai, S.7    Yamamoto, M.8
  • 17
    • 0037106099 scopus 로고    scopus 로고
    • Identification of Nrf2-regulated genes induced by the chemopreventive agent sulforaphane by oligonucleotide microarray
    • Thimmulappa, R. K., Mai, K. H., Srisuma, S., Kensler, T. W., Yamamoto, M., and Biswal, S. (2002) Identification of Nrf2-regulated genes induced by the chemopreventive agent sulforaphane by oligonucleotide microarray Cancer Res. 62, 5196-5203 (Pubitemid 35033454)
    • (2002) Cancer Research , vol.62 , Issue.18 , pp. 5196-5203
    • Thimmulappa, R.K.1    Mai, K.H.2    Srisuma, S.3    Kensler, T.W.4    Yamamoto, M.5    Biswal, S.6
  • 18
    • 0035153227 scopus 로고    scopus 로고
    • High sensitivity of Nrf2 knockout mice to acetaminophen hepatotoxicity associated with decreased expression of ARE-regulated drug metabolizing enzymes and antioxidant genes
    • DOI 10.1093/toxsci/59.1.169
    • Enomoto, A., Itoh, K., Nagayoshi, E., Haruta, J., Kimura, T., O'Connor, T., Harada, T., and Yamamoto, M. (2001) High sensitivity of Nrf2 knockout mice to acetaminophen hepatotoxicity associated with decreased expression of ARE-regulated drug metabolizing enzymes and antioxidant genes Toxicol. Sci. 59, 169-177 (Pubitemid 32117993)
    • (2001) Toxicological Sciences , vol.59 , Issue.1 , pp. 169-177
    • Enomoto, A.1    Itoh, K.2    Nagayoshi, E.3    Haruta, J.4    Kimura, T.5    O'Connor, T.6    Harada, T.7    Yamamoto, M.8
  • 19
    • 0141534255 scopus 로고    scopus 로고
    • Transcription factor Nrf2 is required for the constitutive and inducible expression of multidrug resistance-associated protein 1 in mouse embryo fibroblasts
    • DOI 10.1016/j.bbrc.2003.09.086
    • Hayashi, A., Suzuki, H., Itoh, K., Yamamoto, M., and Sugiyama, Y. (2003) Transcription factor Nrf2 is required for the constitutive and inducible expression of multidrug resistance-associated protein 1 in mouse embryo fibroblasts Biochem. Biophys. Res. Commun. 310, 824-829 (Pubitemid 37188696)
    • (2003) Biochemical and Biophysical Research Communications , vol.310 , Issue.3 , pp. 824-829
    • Hayashi, A.1    Suzuki, H.2    Itoh, K.3    Yamamoto, M.4    Sugiyama, Y.5
  • 20
    • 0026040838 scopus 로고
    • Molecular mechanisms of quinone cytotoxicity
    • O'Brien, P. J. (1991) Molecular mechanisms of quinone cytotoxicity Chem.-Biol. Interact. 80, 1-41
    • (1991) Chem.-Biol. Interact. , vol.80 , pp. 1-41
    • O'Brien, P.J.1
  • 23
    • 78649878916 scopus 로고    scopus 로고
    • Immunochemical method to detect proteins that undergo selective modification by 1,2-naphthoquinone derived from naphthalene through metabolic activation
    • Miura, T. and Kumagai, Y. (2010) Immunochemical method to detect proteins that undergo selective modification by 1,2-naphthoquinone derived from naphthalene through metabolic activation J. Toxicol. Sci. 35, 843-852
    • (2010) J. Toxicol. Sci. , vol.35 , pp. 843-852
    • Miura, T.1    Kumagai, Y.2
  • 26
    • 28144445947 scopus 로고    scopus 로고
    • Hepatocyte-specific deletion of the keap1 gene activates Nrf2 and confers potent resistance against acute drug toxicity
    • DOI 10.1016/j.bbrc.2005.10.185, PII S0006291X05024733
    • Okawa, H., Motohashi, H., Kobayashi, A., Aburatani, H., Kensler, T. W., and Yamamoto, M. (2006) Hepatocyte-specific deletion of the keap1 gene activates Nrf2 and confers potent resistance against acute drug toxicity Biochem. Biophys. Res. Commun. 339, 79-88 (Pubitemid 41697517)
    • (2006) Biochemical and Biophysical Research Communications , vol.339 , Issue.1 , pp. 79-88
    • Okawa, H.1    Motohashi, H.2    Kobayashi, A.3    Aburatani, H.4    Kensler, T.W.5    Yamamoto, M.6
  • 27
    • 67349248433 scopus 로고    scopus 로고
    • Role of aquaporin 9 in cellular accumulation of arsenic and its cytotoxicity in primary mouse hepatocytes
    • Shinkai, Y., Sumi, D., Toyama, T., Kaji, T., and Kumagai, Y. (2009) Role of aquaporin 9 in cellular accumulation of arsenic and its cytotoxicity in primary mouse hepatocytes Toxicol. Appl. Pharmacol. 237, 232-236
    • (2009) Toxicol. Appl. Pharmacol. , vol.237 , pp. 232-236
    • Shinkai, Y.1    Sumi, D.2    Toyama, T.3    Kaji, T.4    Kumagai, Y.5
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227, 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0021678736 scopus 로고
    • Electroblotting of multiple gels: A simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose
    • DOI 10.1016/0165-022X(84)90040-X
    • Kyhse-Andersen, J. (1984) Electroblotting of multiple gels: a simple apparatus without buffer tank for rapid transfer of proteins from polyacrylamide to nitrocellulose J. Biochem. Biophys. Methods 10, 203-209 (Pubitemid 15171298)
    • (1984) Journal of Biochemical and Biophysical Methods , vol.10 , Issue.3-4 , pp. 203-209
    • Kyhse-Andersen, J.1
  • 30
    • 0022445670 scopus 로고
    • Rapid colorimetric assay for cell growth and survival - Modifications to the tetrazolium dye procedure giving improved sensitivity and reliability
    • DOI 10.1016/0022-1759(86)90368-6
    • Denizot, F. and Lang, R. (1986) Rapid colorimetric assay for cell growth and survival. Modifications to the tetrazolium dye procedure giving improved sensitivity and reliability J. Immunol. Methods 89, 271-277 (Pubitemid 16080782)
    • (1986) Journal of Immunological Methods , vol.89 , Issue.2 , pp. 271-277
    • Denizot, F.1    Lang, R.2
  • 33
    • 1642330416 scopus 로고    scopus 로고
    • Transport of Ethinylestradiol Glucuronide and Ethinylestradiol Sulfate by the Multidrug Resistance Proteins MRP1, MRP2, and MRP3
    • DOI 10.1124/jpet.103.062091
    • Chu, X. Y., Huskey, S. E., Braun, M. P., Sarkadi, B., Evans, D. C., and Evers, R. (2004) Transport of ethinylestradiol glucuronide and ethinylestradiol sulfate by the multidrug resistance proteins MRP1, MRP2, and MRP3 J. Pharmacol. Exp. Ther. 309, 156-164 (Pubitemid 38393126)
    • (2004) Journal of Pharmacology and Experimental Therapeutics , vol.309 , Issue.1 , pp. 156-164
    • Chu, X.-Y.1    Huskey, S.-E.W.2    Braun, M.P.3    Sarkadi, B.4    Evans, D.C.5    Evers, R.6
  • 34
    • 77951296034 scopus 로고    scopus 로고
    • Validated assay for studying activity profiles of human liver UGTs after drug exposure: Inhibition and induction studies
    • Donato, M. T., Montero, S., Castell, J. V., Gomez-Lechon, M. J., and Lahoz, A. (2010) Validated assay for studying activity profiles of human liver UGTs after drug exposure: inhibition and induction studies Anal. Bioanal. Chem. 396, 2251-2263
    • (2010) Anal. Bioanal. Chem. , vol.396 , pp. 2251-2263
    • Donato, M.T.1    Montero, S.2    Castell, J.V.3    Gomez-Lechon, M.J.4    Lahoz, A.5
  • 35
    • 33644777840 scopus 로고    scopus 로고
    • Multidrug resistance protein 1 (MRP1, ABCC1) mediates resistance to mitoxantrone via glutathione-dependent drug efflux
    • Morrow, C. S., Peklak-Scott, C., Bishwokarma, B., Kute, T. E., Smitherman, P. K., and Townsend, A. J. (2006) Multidrug resistance protein 1 (MRP1, ABCC1) mediates resistance to mitoxantrone via glutathione-dependent drug efflux Mol. Pharmacol. 69, 1499-1505
    • (2006) Mol. Pharmacol. , vol.69 , pp. 1499-1505
    • Morrow, C.S.1    Peklak-Scott, C.2    Bishwokarma, B.3    Kute, T.E.4    Smitherman, P.K.5    Townsend, A.J.6
  • 39
  • 41
    • 77953460849 scopus 로고    scopus 로고
    • Genetic analysis of cytoprotective functions supported by graded expression of Keap1
    • Taguchi, K., Maher, J. M., Suzuki, T., Kawatani, Y., Motohashi, H., and Yamamoto, M. (2010) Genetic analysis of cytoprotective functions supported by graded expression of Keap1 Mol. Cell. Biol. 30, 3016-3026
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 3016-3026
    • Taguchi, K.1    Maher, J.M.2    Suzuki, T.3    Kawatani, Y.4    Motohashi, H.5    Yamamoto, M.6
  • 42
    • 0031034402 scopus 로고    scopus 로고
    • Generation of reactive oxygen species during interaction of diesel exhaust particle components with NADPH-cytochrome P450 reductase and involvement of the bioactivation in the DNA damage
    • DOI 10.1016/S0891-5849(96)00341-3, PII S0891584996003413
    • Kumagai, Y., Arimoto, T., Shinyashiki, M., Shimojo, N., Nakai, Y., Yoshikawa, T., and Sagai, M. (1997) Generation of reactive oxygen species during interaction of diesel exhaust particle components with NADPH-cytochrome P450 reductase and involvement of the bioactivation in the DNA damage Free Radical Biol. Med. 22, 479-487 (Pubitemid 27020122)
    • (1997) Free Radical Biology and Medicine , vol.22 , Issue.3 , pp. 479-487
    • Kumagai, Y.1    Arimoto, T.2    Shinyashiki, M.3    Shimojo, N.4    Nakai, Y.5    Yoshikawa, T.6    Sagai, M.7
  • 43
    • 0025980713 scopus 로고
    • The toxicity of menadione (2-methyl-1,4-naphthoquinone) and two thioether conjugates studied with isolated renal epithelial cells
    • Brown, P. C., Dulik, D. M., and Jones, T. W. (1991) The toxicity of menadione (2-methyl-1,4-naphthoquinone) and two thioether conjugates studied with isolated renal epithelial cells Arch. Biochem. Biophys. 285, 187-196
    • (1991) Arch. Biochem. Biophys. , vol.285 , pp. 187-196
    • Brown, P.C.1    Dulik, D.M.2    Jones, T.W.3
  • 44
    • 0024498044 scopus 로고
    • DT-diaphorase-catalysed reduction of 1,4-naphthoquinone derivatives and glutathionyl-quinone conjugates. Effect of substituents on autoxidation rates
    • Buffinton, G. D., Ollinger, K., Brunmark, A., and Cadenas, E. (1989) DT-diaphorase-catalysed reduction of 1,4-naphthoquinone derivatives and glutathionyl-quinone conjugates. Effect of substituents on autoxidation rates Biochem. J. 257, 561-571 (Pubitemid 19040932)
    • (1989) Biochemical Journal , vol.257 , Issue.2 , pp. 561-571
    • Buffinton, G.D.1    Ollinger, K.2    Brunmark, A.3    Cadenas, E.4
  • 45
    • 77950521201 scopus 로고    scopus 로고
    • Cooperation of NAD(P)H:quinone oxidoreductase 1 and UDP- glucuronosyltransferases reduces menadione cytotoxicity in HEK293 cells
    • Nishiyama, T., Izawa, T., Usami, M., Ohnuma, T., Ogura, K., and Hiratsuka, A. (2010) Cooperation of NAD(P)H:quinone oxidoreductase 1 and UDP-glucuronosyltransferases reduces menadione cytotoxicity in HEK293 cells Biochem. Biophys. Res. Commun. 394, 459-463
    • (2010) Biochem. Biophys. Res. Commun. , vol.394 , pp. 459-463
    • Nishiyama, T.1    Izawa, T.2    Usami, M.3    Ohnuma, T.4    Ogura, K.5    Hiratsuka, A.6


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