Significance of superoxide dismutase (SOD) in human colorectal cancer tissue: Correlation with malignant intensity
Tóm tắt
The significance of superoxide dismutase (SOD) activity in colorectal cancer tissue was determined from the aspect of the antioxidant defense system. SOD activity and thiobarbituric acid reactive substance were measured in the tumor, in tissues adjacent to the tumor, and in regions that appeared normal, and the results were analyzed in terms of various histopathological factors (stage of disease, depth of invasion, venous invasion, etc.). DNA ploidy pattern and cell proliferation in cancer tissue were also measured, and the results analyzed in relation to SOD activity. SOD activity in cancer tissue was higher than in the other two regions. SOD activity in cancer tissue increased with the progression of stage, and changed with the depth of invasion. There was a significant difference in SOD activity between patients with venous invasion and those in whom this was absent. Stepwise regression analysis suggested that venous invasion was the most significant factor influencing SOD activity. The proliferation index was high in cancer tissue with low SOD activity. The incidence of aneuploidy was high in cancer with high SOD activity, whereas the incidence of diploidy was high in cancer with low SOD activity. These results suggest that elucidation of the antioxidant system in cancer tissue can provide us with a better strategy for cancer treatment.
Tài liệu tham khảo
McCord JM, Fridovich I. Superoxide dismutase: An enzymic function for erythrocuprein (hemocuprein). J Biol Chem 1969; 244:6049–6055.
Nakamura Y, Gindhart TD, Winterstein D, et al. Early superoxide dismutase-sensitive event promotes neoplastic transformation in mucose epidermal JB6 cells. Carcinogenesis 1988;9: 203–207.
Hoffman CEJ, Webster NR, Wiggins PA, et al. Free radical detoxifying systems in human colorectal cancer. Br J Cancer 1985;51:127–129.
Sykes JA, McCormack FX Jr, O'Brien TJ. A preliminary study of the superoxide dismutase content of some human tumors. Cancer Res 1978;38:2759–2762.
Sinha BK, Mimnaugh EG, Rajagopalan S, et al. Adriamycine activation and oxygen free radical formation in human breast tumor cells: Protective role of glutathione peroxidase in adriamycine resistance. Cancer Res 1989;49:3844–3848.
Japanese Research Society for Cancer of Colon and Rectum. General rules for clinical and pathological studies on cancer of colon, rectum and anus. 4th ed. Tokyo: Kanehara, 1985.
Sonoda M, Asakuno G, Matsuki M, et al. Radical trapping by PBN during reperfusion in rabbit gastric mucosa. Free Rad Res Commun 1993;19:185–191.
Nagata O. Macintosh medical statistical manual. Tokyo: Shinko-koueki, 1994.
Marklund SL, Westman NG, Lundgren E, et al. Copper and zinc containing superoxide dismutase, manganese containing superoxide dismutase, catalase, and glutathione peroxidase in normal and neoplastic human cell lines and normal human tissues. Cancer Res 1982;42:1955–1961.
Bize IB, Oberley LW, Morris HP. Superoxide radical in Morris hepatoma. Cancer Res 1980;40:3686–3693.
Dionisi O, Galeotti T, Terranova T, et al. Superoxide radicals and hydrogen peroxide formation in mitochondria from normal and neoplastic tissues. Biochem Biophys Acta 1975;403:292–300.
Loven DP, Oberley LW, Rousseau FM, et al. Superoxide dismutase activity in 1,2-dimethylhydrazine-induced rat colon adenocarcinoma. JNCI 1980;65:377–381
Mukai M, Shinkai K, Tateish R, et al. Macrophage potentiation of invasive capacity of ascites hepatoma cells. Cancer Res 1987; 47:2167–2171.
Weitzman SA. Phagocytes as carcinogens: Malignant transformation produced by human neurtrophils. Science 1985,227:1231–1233.
Sinkai K, Mukai M, Imamura F, et al. Potentiation of invasive capacity of rat ascites hepatoma cells by free radicals. J Act Oxyg Free Rad 1991;2:330–336.
Szatrowski TP, Nathan CF. Production of large amounts of hydrogen peroxide by human tumor cells. Cancer Res 1991;51:794–798.
Iizuka H, Hashimoto Y, Kobayashi T. Oxygen and superoxide dismutase in epidermis: Its relation to keratinocyte proliferation. J Act Oxyg Free Rad 1992;3:313–321.
Blum J, Fridovich I. Inactivation of glutathione peroxidase by superoxide radical. Arch Biochem Biophys 1985;240:500–508.
Fridovich I, Superoxide dismutase. Ann Rev Biochem 1975;44:147–159.
Armato U, Andreis PG, Romano F. Exogenous Cu, Zn-superoxide dismutase suppresses the stimulation of neonatal rat hepatocyte growth by tumor promoters. Carcinogenesis 1984;5:1547–1554.
Rana RS, Hokin LE. Role of phosphoinositides in transmembrane signaling. Physiol Rev 1990;70:115–124.
Honda S, Senshu T, Matsuno M. The oxygen susceptibility of cultured Hela cells and the cell cycle. Cell Biol Internal Rep 1981;5:553–558.
Iwagaki H, Kashino H, Matsubara N, et al. Free radicals and lipid peroxidation in gastrointestinal tumors. Magn Reson Med 1993;4:71–74.
Cheeseman KH, Emery S, Maddix SP, et al. Studies on lipid peroxidation in normal and tumour tissues. Biochem J 1988; 250:247–252.
Wolley RC, Schreiber K, Koss LG, et al. DNA distribution in human colon carcinomas and its relationship to clinical behavior. JNCI 1982;69:15–22.
Armitage NC, Ballantyne KG, Evans DF, et al The influence of tumour cell DNA content on survival in colorectal cancer: A detailed analysis. Br J Cancer 1990;62:852–856.
Kouri M, Pyrhonen S, Mecklin JP, et al. The prognostic value of DNA ploidy in colorectal carcinoma: A prospective study. Br J Cancer 1990;62:976–981.
Hatsuda K. SOD and peroxidase activities in endometrial cancer and their effects on sensitivity to ADM. J Kyoto Pref Univ Med 1990;99:595–605.
Doroshow JH. Role of hydrogen peroxide and hydroxyl radical formation in the killing of Ehrlich tumor cells by anticancer quinones. Proc Natl Acad Sci USA 1986;83:4515–4518.
Iwagaki H, Matsubara N, Mizukawa K, et al. The possible involvement of free radical scavenging properties in interferon-γ. Magn Reson Med 1993;4:75–78.
Cerutti PA. Prooxidant states and tumor promotion. Science 1981;227:375–381.