메뉴 건너뛰기




Volumn 20, Issue 1, 2007, Pages 55-64

Reactive oxygen species are possibly involved in the mechanism of flumequine-induced hepatocarcinogenesis in mice

Author keywords

Flumequine; Hepatocarcinogenesis; Mouse; Oxidative stress; Tumor promotion

Indexed keywords


EID: 34247220473     PISSN: 09149198     EISSN: None     Source Type: Journal    
DOI: 10.1293/tox.20.55     Document Type: Article
Times cited : (4)

References (39)
  • 1
    • 0018190794 scopus 로고
    • Activity of flumequine against. Escherichia coli: In vitro comparison with nalidixic and oxolinic acids
    • Greenwood D. Activity of flumequine against. Escherichia coli: in vitro comparison with nalidixic and oxolinic acids. Antimicrob Agents Chemother. 13: 479-483. 1978.
    • (1978) Antimicrob Agents Chemother , vol.13 , pp. 479-483
    • Greenwood, D.1
  • 2
    • 16544384764 scopus 로고    scopus 로고
    • JECFA Evaluation of certain veterinary drug residues in food. Sixty-second report of the Joint FAO/WHO Expert Committee on food additives. World Health Organ. Tech Rep Ser. 925: 18-19. 2004.
    • JECFA Evaluation of certain veterinary drug residues in food. Sixty-second report of the Joint FAO/WHO Expert Committee on food additives. World Health Organ. Tech Rep Ser. 925: 18-19. 2004.
  • 3
    • 34247261277 scopus 로고    scopus 로고
    • JECFA Evaluation of certain veterinary drug residues in food. Forty-eighth report of the Joint FAO/WHO Expert Committee on food additives. World Health Organ. Tech Rep Ser. 879: 35-43. 1998.
    • JECFA Evaluation of certain veterinary drug residues in food. Forty-eighth report of the Joint FAO/WHO Expert Committee on food additives. World Health Organ. Tech Rep Ser. 879: 35-43. 1998.
  • 4
    • 0033017830 scopus 로고    scopus 로고
    • Hepatotoxicity and consequently increased cell proliferation are associated with flumequine hepatocarcinogenesis in mice
    • Yoshida M, Miyajima K, Shiraki K, Ando J, Kudoh K, Nakae D, Takahashi M, and Maekawa A. Hepatotoxicity and consequently increased cell proliferation are associated with flumequine hepatocarcinogenesis in mice. Cancer Lett. 141: 99-107. 1999.
    • (1999) Cancer Lett , vol.141 , pp. 99-107
    • Yoshida, M.1    Miyajima, K.2    Shiraki, K.3    Ando, J.4    Kudoh, K.5    Nakae, D.6    Takahashi, M.7    Maekawa, A.8
  • 5
  • 6
    • 0005017897 scopus 로고    scopus 로고
    • Modifying effects of flumequine on dimethylnitrosamine-induced hepatocarcinogenesis in heterozygous p53 deficient CBA mice
    • Takizawa T, Mitsumori K, Takagi H, Onodera H, Yasuhara K, Tamura T, and Hirose M. Modifying effects of flumequine on dimethylnitrosamine-induced hepatocarcinogenesis in heterozygous p53 deficient CBA mice. J Toxicol Pathol. 14: 135-143. 2001.
    • (2001) J Toxicol Pathol , vol.14 , pp. 135-143
    • Takizawa, T.1    Mitsumori, K.2    Takagi, H.3    Onodera, H.4    Yasuhara, K.5    Tamura, T.6    Hirose, M.7
  • 9
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method
    • Livak KJ and Schmittgen TD. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) Method. Methods. 25: 402-408, 2001.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 10
    • 0018187696 scopus 로고
    • Gamma-glutamyltransferase in putative premalignant liver cell populations during hepatocarcinogenesis
    • Cameron R, Kellen J, Kolin A, Malkin A, and Farber E. Gamma-glutamyltransferase in putative premalignant liver cell populations during hepatocarcinogenesis. Cancer Res. 38: 823-829. 1978.
    • (1978) Cancer Res , vol.38 , pp. 823-829
    • Cameron, R.1    Kellen, J.2    Kolin, A.3    Malkin, A.4    Farber, E.5
  • 11
    • 20144372038 scopus 로고    scopus 로고
    • Enzymatic detection of precursor cell populations of preneoplastic foci positive for gamma-glutamyltranspeptidase in rat liver
    • Satoh K, Takahashi G, Miura T, Hayakari M, and Hatayama I. Enzymatic detection of precursor cell populations of preneoplastic foci positive for gamma-glutamyltranspeptidase in rat liver. Int J Cancer. 115: 711-716. 2005.
    • (2005) Int J Cancer , vol.115 , pp. 711-716
    • Satoh, K.1    Takahashi, G.2    Miura, T.3    Hayakari, M.4    Hatayama, I.5
  • 12
    • 15744390110 scopus 로고    scopus 로고
    • Contribution of mitochondrial DNA repair to cell resistance from oxidative stress
    • Grishko VI, Rachel LI, Spitz DR, Wilson GL, and LeDoux SP. Contribution of mitochondrial DNA repair to cell resistance from oxidative stress. J Biol Chem. 280: 8901-8905. 2005.
    • (2005) J Biol Chem , vol.280 , pp. 8901-8905
    • Grishko, V.I.1    Rachel, L.I.2    Spitz, D.R.3    Wilson, G.L.4    LeDoux, S.P.5
  • 13
    • 0020188453 scopus 로고
    • Oxidase and oxygenase function of the microsomal cytochrome P450 monooxygenase system
    • Kuthan H and Ulrich V. Oxidase and oxygenase function of the microsomal cytochrome P450 monooxygenase system. Eur J Biochem. 126: 583-588. 1982.
    • (1982) Eur J Biochem , vol.126 , pp. 583-588
    • Kuthan, H.1    Ulrich, V.2
  • 14
    • 0025087596 scopus 로고
    • Sensitive and rapid quantitation of oxygen reactive species formation in rat synaptosomes
    • LeBel CP and Bondy SC. Sensitive and rapid quantitation of oxygen reactive species formation in rat synaptosomes. Neurochem. Int. 17: 435-440. 1990.
    • (1990) Neurochem. Int , vol.17 , pp. 435-440
    • LeBel, C.P.1    Bondy, S.C.2
  • 16
    • 33750711768 scopus 로고    scopus 로고
    • Molecular pathological analysis for determining the possible mechanism of piperonyl butoxide-induced hepatocarcinogenesis in mice
    • Muguruma M, Nishimura J, Jin M, Kashida Y, Moto M, Takahashi M, Yokouchi Y, and Mitsumori K. Molecular pathological analysis for determining the possible mechanism of piperonyl butoxide-induced hepatocarcinogenesis in mice. Toxicology. 228: 178-187. 2006.
    • (2006) Toxicology , vol.228 , pp. 178-187
    • Muguruma, M.1    Nishimura, J.2    Jin, M.3    Kashida, Y.4    Moto, M.5    Takahashi, M.6    Yokouchi, Y.7    Mitsumori, K.8
  • 17
    • 0030474051 scopus 로고    scopus 로고
    • Thiol regulation of endotoxin-induced release of tumour necrosis factor alpha from isolated rat Kupffer cells
    • Neuschwander-Tetri BA, Bellezzo JM, Britton RS, Bacon BR, and Fox ES. Thiol regulation of endotoxin-induced release of tumour necrosis factor alpha from isolated rat Kupffer cells. Biochem. J. 320: 1005-1010. 1996.
    • (1996) Biochem. J , vol.320 , pp. 1005-1010
    • Neuschwander-Tetri, B.A.1    Bellezzo, J.M.2    Britton, R.S.3    Bacon, B.R.4    Fox, E.S.5
  • 18
    • 0037763721 scopus 로고    scopus 로고
    • Regulatory mechanisms controlling gene expression mediated by the antioxidant response element
    • Nguyen T, Sherrat PJ, and Pickett CB. Regulatory mechanisms controlling gene expression mediated by the antioxidant response element. Annu Rev Pharmacol Toxicol. 43: 233-260. 2003.
    • (2003) Annu Rev Pharmacol Toxicol , vol.43 , pp. 233-260
    • Nguyen, T.1    Sherrat, P.J.2    Pickett, C.B.3
  • 19
    • 0029561598 scopus 로고
    • The glutathione S-transferase supergene family: Regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance
    • Hayes JD and Pulford DJ. The glutathione S-transferase supergene family: regulation of GST and the contribution of the isoenzymes to cancer chemoprotection and drug resistance. Crit Rev Biochem Mol Biol. 30: 445-600. 1995.
    • (1995) Crit Rev Biochem Mol Biol , vol.30 , pp. 445-600
    • Hayes, J.D.1    Pulford, D.J.2
  • 20
    • 0023506857 scopus 로고
    • The effects of selenium and copper deficiencies on glutathione S-transferase and glutathione peroxidase in rat liver
    • Arthur JR, Morrice PC, Nicol F, Beddows SE, Boyd R, Hayes JD, and Beckett GJ. The effects of selenium and copper deficiencies on glutathione S-transferase and glutathione peroxidase in rat liver. Biochem. J. 248: 539-544. 1987.
    • (1987) Biochem. J , vol.248 , pp. 539-544
    • Arthur, J.R.1    Morrice, P.C.2    Nicol, F.3    Beddows, S.E.4    Boyd, R.5    Hayes, J.D.6    Beckett, G.J.7
  • 21
    • 0028171293 scopus 로고    scopus 로고
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response. Cell. 79: 583-593. 1994.
    • 2 from the oxidative burst orchestrates the plant hypersensitive disease resistance response. Cell. 79: 583-593. 1994.
  • 22
    • 0036840585 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase regulates nuclear translocation of NF-E2-related factor 2 through actin rearrangement in response to oxidative stress
    • Kang KW, Lee SJ, Park JW, and Kim SG., Phosphatidylinositol 3-kinase regulates nuclear translocation of NF-E2-related factor 2 through actin rearrangement in response to oxidative stress. Mol Pharmacol. 62: 1001-1010. 2002.
    • (2002) Mol Pharmacol , vol.62 , pp. 1001-1010
    • Kang, K.W.1    Lee, S.J.2    Park, J.W.3    Kim, S.G.4
  • 23
    • 5444240961 scopus 로고    scopus 로고
    • Contribution of NAD(P)H:quinone oxidoreductase 1 to protection against carcinogenesis, and regulation of its gene by the Nrf2 basic-region leucine zipper and the arylhydrocarbon receptor basic helix-loop-helix transcription factors
    • Nioi P and Hayes JD. Contribution of NAD(P)H:quinone oxidoreductase 1 to protection against carcinogenesis, and regulation of its gene by the Nrf2 basic-region leucine zipper and the arylhydrocarbon receptor basic helix-loop-helix transcription factors. Mutat Res. 555: 149-171. 2004.
    • (2004) Mutat Res , vol.555 , pp. 149-171
    • Nioi, P.1    Hayes, J.D.2
  • 24
    • 0033655446 scopus 로고    scopus 로고
    • Regulation of glutathione synthesis
    • Lu SC. Regulation of glutathione synthesis. Curr Top Cell Regul. 36: 95-116. 2000.
    • (2000) Curr Top Cell Regul , vol.36 , pp. 95-116
    • Lu, S.C.1
  • 26
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh K, Wakabayashi N, Katoh Y, Ishii T, Igarashi K, Engel JD, and Yamamoto M. Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev. 13: 76-86. 1999.
    • (1999) Genes Dev , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 27
    • 0036708902 scopus 로고    scopus 로고
    • Antioxidants and oxidants regulated signal transduction pathways
    • Owuor ED and Kong AN. Antioxidants and oxidants regulated signal transduction pathways. Biochem Pharmacol. 64: 765-770. 2002.
    • (2002) Biochem Pharmacol , vol.64 , pp. 765-770
    • Owuor, E.D.1    Kong, A.N.2
  • 30
    • 0034213842 scopus 로고    scopus 로고
    • Nrf2 and c-Jun regulation of antioxidant response element (ARE)-mediated expression and induction of gamma-glutamylcysteine synthetase heavy subunit gene
    • Jeyapaul J and Jaiswal AK. Nrf2 and c-Jun regulation of antioxidant response element (ARE)-mediated expression and induction of gamma-glutamylcysteine synthetase heavy subunit gene. Biochem Pharmacol. 59: 1433-1439. 2000.
    • (2000) Biochem Pharmacol , vol.59 , pp. 1433-1439
    • Jeyapaul, J.1    Jaiswal, A.K.2
  • 31
    • 0032542213 scopus 로고    scopus 로고
    • Nrf2 and Nrf1 in association with Jun proteins regulate antioxidant response element-mediated expression and coordinated induction of genes encoding detoxifying enzymes
    • Venugopal R and Jaiswal AK. Nrf2 and Nrf1 in association with Jun proteins regulate antioxidant response element-mediated expression and coordinated induction of genes encoding detoxifying enzymes. Oncogene. 17: 3145-3156. 1998.
    • (1998) Oncogene , vol.17 , pp. 3145-3156
    • Venugopal, R.1    Jaiswal, A.K.2
  • 32
    • 0029906134 scopus 로고    scopus 로고
    • Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:quinone oxidoreductase1 gene
    • Venugopal R and Jaiswal AK. Nrf1 and Nrf2 positively and c-Fos and Fra1 negatively regulate the human antioxidant response element-mediated expression of NAD(P)H:quinone oxidoreductase1 gene. Proc Natl Acad Sci USA. 93: 14960-14965. 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14960-14965
    • Venugopal, R.1    Jaiswal, A.K.2
  • 33
    • 33644501791 scopus 로고    scopus 로고
    • Activation of the Nrf2-ARE signaling pathway: A promising strategy in cancer prevention
    • Giudice A, and Montella M. Activation of the Nrf2-ARE signaling pathway: a promising strategy in cancer prevention. Bioessays. 28: 169-181. 2006.
    • (2006) Bioessays , vol.28 , pp. 169-181
    • Giudice, A.1    Montella, M.2
  • 34
    • 32444433202 scopus 로고    scopus 로고
    • Free radicals, metals and antioxidants in oxidative stress-induced cancer
    • Valko M, Rhodes CJ, Moncol J, Izakovic M, and Mazur M. Free radicals, metals and antioxidants in oxidative stress-induced cancer. Chem Biol Interact. 160: 1-40. 2006.
    • (2006) Chem Biol Interact , vol.160 , pp. 1-40
    • Valko, M.1    Rhodes, C.J.2    Moncol, J.3    Izakovic, M.4    Mazur, M.5
  • 35
    • 0034190272 scopus 로고    scopus 로고
    • Activator protein 1 (AP-1)- and nuclear factor kappaB (NF-kappaB)-dependent transcriptional events in carcinogenesis
    • Hsu TC, Young MR, Cmarik J, and Colburn NH. Activator protein 1 (AP-1)- and nuclear factor kappaB (NF-kappaB)-dependent transcriptional events in carcinogenesis. Free Radic Biol Med. 28: 1338-1348. 2000.
    • (2000) Free Radic Biol Med , vol.28 , pp. 1338-1348
    • Hsu, T.C.1    Young, M.R.2    Cmarik, J.3    Colburn, N.H.4
  • 36
    • 0025806587 scopus 로고
    • Ha-Ras augments c-Jun activity and stimulates phosphorylation of its activation domain
    • Binetruy B, Smeal T, Karin M. Ha-Ras augments c-Jun activity and stimulates phosphorylation of its activation domain. Nature. 351: 122-127. 1991.
    • (1991) Nature , vol.351 , pp. 122-127
    • Binetruy, B.1    Smeal, T.2    Karin, M.3
  • 37
    • 0025788098 scopus 로고
    • Oncogenic and transcriptional cooperation with Ha-Ras requires phosphorylation of c-Jun on serines 63 and 73
    • Smeal T, Binetruy B, Mercola DA, Birrer M, and Karin M. Oncogenic and transcriptional cooperation with Ha-Ras requires phosphorylation of c-Jun on serines 63 and 73. Nature. 354: 494-496. 1991.
    • (1991) Nature , vol.354 , pp. 494-496
    • Smeal, T.1    Binetruy, B.2    Mercola, D.A.3    Birrer, M.4    Karin, M.5
  • 38
    • 0025973702 scopus 로고
    • Assays for 8-hydroxy-2′-deoxyguanosine: A biomarker of in vivo oxidative DNA damage
    • Shigenaga MK and Ames BN. Assays for 8-hydroxy-2′-deoxyguanosine: a biomarker of in vivo oxidative DNA damage. Free Radic Biol Med. 10: 211-216. 1991.
    • (1991) Free Radic Biol Med , vol.10 , pp. 211-216
    • Shigenaga, M.K.1    Ames, B.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.