메뉴 건너뛰기




Volumn 27, Issue 3-4, 1999, Pages 401-410

Persistent oxidative stress in human colorectal carcinoma, but not in adenoma

Author keywords

3 Nitro L tyrosine; 4 Hydroxy 2 nonenal; 8 Hydroxy 2' deoxyguanosine; Adenoma; Colorectal carcinoma; Free radicals; Human; Oxidative stress; Proliferating cell nuclear antigen

Indexed keywords

4 HYDROXYNONENAL; 8 HYDROXYDEOXYGUANOSINE; ANTIBODY; CELL NUCLEUS ANTIGEN; FREE RADICAL; PEROXYNITRITE; REACTIVE OXYGEN METABOLITE; TYROSINE DERIVATIVE;

EID: 0032817402     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(99)00087-8     Document Type: Article
Times cited : (150)

References (38)
  • 2
    • 0026021362 scopus 로고
    • Production of large amounts of hydrogen peroxide by human tumor cells
    • Szatrowski T.P., Nathan C.F. Production of large amounts of hydrogen peroxide by human tumor cells. Cancer Res. 51:1991;794-798.
    • (1991) Cancer Res. , vol.51 , pp. 794-798
    • Szatrowski, T.P.1    Nathan, C.F.2
  • 3
    • 0025289049 scopus 로고
    • Free radicals, antioxidant enzymes, and carcinogenesis
    • Sun Y. Free radicals, antioxidant enzymes, and carcinogenesis. Free Radic. Biol. Med. 8:1990;583-599.
    • (1990) Free Radic. Biol. Med. , vol.8 , pp. 583-599
    • Sun, Y.1
  • 5
    • 0028270384 scopus 로고
    • Oxidative DNA base damage and antioxidant enzyme activities in human lung cancer
    • Jaruga P., Zastawny T.H., Skokowski J., Dizdaroglu M., Olinski R. Oxidative DNA base damage and antioxidant enzyme activities in human lung cancer. FEBS Lett. 341:1994;59-64.
    • (1994) FEBS Lett. , vol.341 , pp. 59-64
    • Jaruga, P.1    Zastawny, T.H.2    Skokowski, J.3    Dizdaroglu, M.4    Olinski, R.5
  • 7
    • 0028900690 scopus 로고
    • Hypothesis: Persistent oxidative stress in cancer
    • Toyokuni S., Okamoto K., Yodoi J., Hiai H. Hypothesis persistent oxidative stress in cancer . FEBS Lett. 358:1995;1-3.
    • (1995) FEBS Lett. , vol.358 , pp. 1-3
    • Toyokuni, S.1    Okamoto, K.2    Yodoi, J.3    Hiai, H.4
  • 8
    • 0021769722 scopus 로고
    • Hydroxylation of deoxyguanosine at the C-8 position by ascorbic acid and other reducing agents
    • Kasai H., Nishimura S. Hydroxylation of deoxyguanosine at the C-8 position by ascorbic acid and other reducing agents. Nucleic Acids Res. 12:1984;2137-2145.
    • (1984) Nucleic Acids Res. , vol.12 , pp. 2137-2145
    • Kasai, H.1    Nishimura, S.2
  • 9
    • 0025981359 scopus 로고
    • Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG
    • Shibutani S., Takeshita M., Grollman A.P. Insertion of specific bases during DNA synthesis past the oxidation-damaged base 8-oxodG. Nature. 349:1991;431-434.
    • (1991) Nature , vol.349 , pp. 431-434
    • Shibutani, S.1    Takeshita, M.2    Grollman, A.P.3
  • 10
    • 0026606054 scopus 로고
    • Modification of histidine residues in proteins by reaction with 4-hydroxynonenal
    • Uchida K., Stadtman E.R. Modification of histidine residues in proteins by reaction with 4-hydroxynonenal. Proc. Natl. Acad. Sci. USA. 89:1992;4544-4548.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4544-4548
    • Uchida, K.1    Stadtman, E.R.2
  • 11
    • 0025814980 scopus 로고
    • Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes
    • Esterbauer H., Schauur J.S., Zollner H. Chemistry and biochemistry of 4-hydroxynonenal, malonaldehyde and related aldehydes. Free Radic. Biol. Med. 11:1991;81-128.
    • (1991) Free Radic. Biol. Med. , vol.11 , pp. 81-128
    • Esterbauer, H.1    Schauur, J.S.2    Zollner, H.3
  • 12
    • 0030948596 scopus 로고    scopus 로고
    • Quantitative immunohistochemical determination of 8-hydroxy-2′-deoxyguanosine by a monoclonal antibody N45.1: Its application to ferric nitrilotriacetate-induced renal carcinogenesis model
    • Toyokuni S., Tanaka T., Hattori Y., Nishiyama Y., Ochi H., Hiai H., Uchida K., Osawa T. Quantitative immunohistochemical determination of 8-hydroxy-2′-deoxyguanosine by a monoclonal antibody N45.1 its application to ferric nitrilotriacetate-induced renal carcinogenesis model . Lab. Invest. 76:1997;365-374.
    • (1997) Lab. Invest. , vol.76 , pp. 365-374
    • Toyokuni, S.1    Tanaka, T.2    Hattori, Y.3    Nishiyama, Y.4    Ochi, H.5    Hiai, H.6    Uchida, K.7    Osawa, T.8
  • 15
    • 0023091627 scopus 로고
    • Cyclin/PCNA is the auxiliary protein of DNA polymerase-delta
    • Bravo R., Frank R., Blundell P.A., Macdonald-Bravo H. Cyclin/PCNA is the auxiliary protein of DNA polymerase-delta. Nature. 326:1987;515-517.
    • (1987) Nature , vol.326 , pp. 515-517
    • Bravo, R.1    Frank, R.2    Blundell, P.A.3    Macdonald-Bravo, H.4
  • 19
    • 0003652868 scopus 로고    scopus 로고
    • Tokyo: Foundation of Promotion for Cancer Research
    • Cancer statistics in Japan-1997. 1997;Foundation of Promotion for Cancer Research, Tokyo.
    • (1997) Cancer Statistics in Japan-1997
  • 20
    • 0025938226 scopus 로고
    • Major alterations in the nucleotide structure of DNA in cancer of the female breast
    • Malins D.C., Haimanot R. Major alterations in the nucleotide structure of DNA in cancer of the female breast. Cancer Res. 51:1991;5430-5432.
    • (1991) Cancer Res. , vol.51 , pp. 5430-5432
    • Malins, D.C.1    Haimanot, R.2
  • 23
    • 0029932905 scopus 로고    scopus 로고
    • Overexpression of human mutT homologue gene messenger RNA in renal-cell carcinoma: Evidence of persistent oxidative stress in cancer
    • Okamoto K., Toyokuni S., Kim J.-W., Ogawa O., Kakehi Y., Arao S., Hiai H., Yoshida O. Overexpression of human mutT homologue gene messenger RNA in renal-cell carcinoma evidence of persistent oxidative stress in cancer . Int. J. Cancer. 65:1996;437-441.
    • (1996) Int. J. Cancer , vol.65 , pp. 437-441
    • Okamoto, K.1    Toyokuni, S.2    Kim, J.-W.3    Ogawa, O.4    Kakehi, Y.5    Arao, S.6    Hiai, H.7    Yoshida, O.8
  • 24
    • 0032486359 scopus 로고    scopus 로고
    • Overexpression of hMTH1 mRNA: A molecular marker of oxidative stress in lung cancer cells
    • Kennedy C.H., Cueto R., Belinsky S.A., Lechner J.F., Pryor W.A. Overexpression of hMTH1 mRNA a molecular marker of oxidative stress in lung cancer cells . FEBS Lett. 429:1998;17-20.
    • (1998) FEBS Lett. , vol.429 , pp. 17-20
    • Kennedy, C.H.1    Cueto, R.2    Belinsky, S.A.3    Lechner, J.F.4    Pryor, W.A.5
  • 25
    • 0028089905 scopus 로고
    • Metabolism of 4-hydroxynonenal, a cytotoxic lipid peroxidation product, in Ehrlich mouse ascites cells at different proliferation stages
    • Grune T., Siems W.G., Zollner H.G., Esterbauer H. Metabolism of 4-hydroxynonenal, a cytotoxic lipid peroxidation product, in Ehrlich mouse ascites cells at different proliferation stages. Cancer Res. 54:1994;5231-5235.
    • (1994) Cancer Res. , vol.54 , pp. 5231-5235
    • Grune, T.1    Siems, W.G.2    Zollner, H.G.3    Esterbauer, H.4
  • 26
    • 0030795737 scopus 로고    scopus 로고
    • Induction and nuclear translocation of thioredoxin by oxidative damage in the mouse kidney: Independence of tubular necrosis and sulfhydryl depletion
    • Tanaka T., Nishiyama Y., Okada K., Hirota K., Matsui M., Yodoi J., Hiai H., Toyokuni S. Induction and nuclear translocation of thioredoxin by oxidative damage in the mouse kidney independence of tubular necrosis and sulfhydryl depletion . Lab. Invest. 77:1997;145-155.
    • (1997) Lab. Invest. , vol.77 , pp. 145-155
    • Tanaka, T.1    Nishiyama, Y.2    Okada, K.3    Hirota, K.4    Matsui, M.5    Yodoi, J.6    Hiai, H.7    Toyokuni, S.8
  • 28
    • 0028223268 scopus 로고
    • Formation of 4-hydroxy-2-nonenal-modified proteins in the renal proximal tubules of rats treated with a renal carcinogen, ferric nitrilotriacetate
    • Toyokuni S., Uchida K., Okamoto K., Hattori-Nakakuki Y., Hiai H., Stadtman E.R. Formation of 4-hydroxy-2-nonenal-modified proteins in the renal proximal tubules of rats treated with a renal carcinogen, ferric nitrilotriacetate. Proc. Natl. Acad. Sci. USA. 91:1994;2616-2620.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2616-2620
    • Toyokuni, S.1    Uchida, K.2    Okamoto, K.3    Hattori-Nakakuki, Y.4    Hiai, H.5    Stadtman, E.R.6
  • 29
    • 0002906058 scopus 로고    scopus 로고
    • Structure of a fluorescent compound formed from 4-hydroxy-2-nonenal and Nα-hippuryllysine: A model study for fluorophore derived from protein modification by lipid peroxidation
    • Itakura K., Osawa T., Uchida K. Structure of a fluorescent compound formed from 4-hydroxy-2-nonenal and Nα-hippuryllysine a model study for fluorophore derived from protein modification by lipid peroxidation . J. Org. Chem. 63:1998;185-187.
    • (1998) J. Org. Chem. , vol.63 , pp. 185-187
    • Itakura, K.1    Osawa, T.2    Uchida, K.3
  • 30
    • 0031028437 scopus 로고    scopus 로고
    • Immunohistochemical detection of 4-hydroxy-2-nonenal adducts in Alzheimer's disease is associated with inheritance of APOE4
    • Montine K.S., Olson S.J., Amarnath V., Whetsell W.O. Jr, Graham D.G., Montine T.J. Immunohistochemical detection of 4-hydroxy-2-nonenal adducts in Alzheimer's disease is associated with inheritance of APOE4. Am. J. Pathol. 150:1997;437-443.
    • (1997) Am. J. Pathol. , vol.150 , pp. 437-443
    • Montine, K.S.1    Olson, S.J.2    Amarnath, V.3    Whetsell W.O., Jr.4    Graham, D.G.5    Montine, T.J.6
  • 31
    • 0032493431 scopus 로고    scopus 로고
    • Structural characterization and immunochemical detection of a fluorophore derived from 4-hydroxy-2-nonenal and lysine
    • Tsai L., Szweda P.A., Vinogradova O., Szweda L.I. Structural characterization and immunochemical detection of a fluorophore derived from 4-hydroxy-2-nonenal and lysine. Proc. Natl. Acad. Sci. USA. 95:1998;7975-7980.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7975-7980
    • Tsai, L.1    Szweda, P.A.2    Vinogradova, O.3    Szweda, L.I.4
  • 32
    • 0031925544 scopus 로고    scopus 로고
    • Structural characterization of a 4-hydroxy-2-alkenal-derived fluorophore that contributes to lipoperoxidatiopn-dependent protein cross-linking in aging and degenerative disease
    • Xu G., Sayre L.M. Structural characterization of a 4-hydroxy-2-alkenal-derived fluorophore that contributes to lipoperoxidatiopn-dependent protein cross-linking in aging and degenerative disease. Chem. Res. Toxicol. 11:1998;247-251.
    • (1998) Chem. Res. Toxicol. , vol.11 , pp. 247-251
    • Xu, G.1    Sayre, L.M.2
  • 33
    • 0032054970 scopus 로고    scopus 로고
    • Role of nitric oxide and superoxide anion in elimination of low metastatic human colorectal carcinomas by unstimulated hepatic sinusoidal endothelial cells
    • Edmiston K.H., Shoji Y., Mizoi T., Ford R., Nachman A., Jessup J.M. Role of nitric oxide and superoxide anion in elimination of low metastatic human colorectal carcinomas by unstimulated hepatic sinusoidal endothelial cells. Cancer Res. 58:1998;1524-1531.
    • (1998) Cancer Res. , vol.58 , pp. 1524-1531
    • Edmiston, K.H.1    Shoji, Y.2    Mizoi, T.3    Ford, R.4    Nachman, A.5    Jessup, J.M.6
  • 35
    • 0024215330 scopus 로고
    • Disturbance of cell proliferation by two model compounds of peroxidation contradicts causative role in proliferative senescence
    • Martin P., Hermann E., Peter S.R., Holger H. Disturbance of cell proliferation by two model compounds of peroxidation contradicts causative role in proliferative senescence. J. Cell. Physiol. 137:1988;421-429.
    • (1988) J. Cell. Physiol. , vol.137 , pp. 421-429
    • Martin, P.1    Hermann, E.2    Peter, S.R.3    Holger, H.4
  • 37
    • 0027229929 scopus 로고
    • Glutathione metabolism by gamma-glutamyl transpeptidase leads to lipid peroxidation - Characterization of the system and relevance to hepatocarcinogenesis
    • Stark A.-A., Zeiger E., Pagano D.A. Glutathione metabolism by gamma-glutamyl transpeptidase leads to lipid peroxidation - Characterization of the system and relevance to hepatocarcinogenesis. Carcinogenesis. 14:1993;183-189.
    • (1993) Carcinogenesis , vol.14 , pp. 183-189
    • Stark, A.-A.1    Zeiger, E.2    Pagano, D.A.3
  • 38
    • 0031018546 scopus 로고    scopus 로고
    • Gamma-glutamyl transpeptidase-dependent lipid peroxidation in isolated hapatocytes and HepG2 hepatoma cells
    • Paolicchi A., Tongiani R., Tonarelli P., Comporti M., Pompella A. Gamma-glutamyl transpeptidase-dependent lipid peroxidation in isolated hapatocytes and HepG2 hepatoma cells. Free Radic. Biol. Med. 22:1997;853-860.
    • (1997) Free Radic. Biol. Med. , vol.22 , pp. 853-860
    • Paolicchi, A.1    Tongiani, R.2    Tonarelli, P.3    Comporti, M.4    Pompella, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.