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Antioxidant enzyme activities and oxidative stress in human breast cancer

  • Original Papers
  • Clinical Oncology
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Abstract

We have analysed products of lipid peroxidation reactions and activities of antioxidant enzymes in cancerous breast tissue and in corresponding reference tissue. In addition, the serum lipid peroxidation and peroxyl-radical-trapping capacity of breast cancer patients were compared to those of healthy subjects. A total of 23 patients with breast cancer participated in this study. In the cancerous tissue, catalase activity was lower than in the reference tissue, while the activities of superoxide dismutase, glutathione peroxidase and the hexose monophosphate shunt were elevated. The content of thiobarbituric-acid-reactive material was slightly lower in the cancerous tissues, but the levels in serum were found to be elevated in patients with breast cancer. The amounts of conjugated diene double bonds were essentially equal both in the cancerous and in the reference tissue. Moreover, in breast cancer patients the serum levels of diene conjugation and the peroxyl-radical-scavenging capacity did not differ from those measured in healthy subjects. This study indicates that the antioxidant defence system is altered in cancerous breast tissues, but does not support the hypothesis suggesting that formation of lipid peroxides in the tumour tissue itself is of primary importance in the carcinogenesis.

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References

  • Alanko J, Riutta A, Mucha I, Vapaatalo H, Metsä-Ketelä T (1993) Modulation of arachidonic acid metabolism by phenols: relation to positions of hydroxyl groups and peroxyl radical scavenging properties. Free Rad Biol Med 14: 19–25

    Google Scholar 

  • Armstrong B, Doll R (1975) Environmental factors and cancer incidence and mortality in different countries with special reference to dietary practices. Int J Cancer 15: 617–631

    Google Scholar 

  • Beers B, Sizer W (1952) A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem 195: 133–139

    Google Scholar 

  • Bird RP, Draper HH (1984) Comparative studies on different methods of malonaldehyde determination. Methods Enzymol 105: 299–305

    Google Scholar 

  • Carroll KK (1980) Lipids and carcinogenesis. J Environ Pathol Toxicol 3: 253–271

    Google Scholar 

  • Cerutti PA (1985) Prooxidant states and tumor promotion. Science 227: 375–381

    Google Scholar 

  • Cerutti PA (1991) Oxidant stress and carcinogenesis. Eur J Clin Invest 21: 1–5

    Google Scholar 

  • Cerutti P, Krupitza G, Larsson R, Muehlematter D, Crawford D, Amstad P (1988) Physiological and pathological effects of oxidants in mouse epidermal cells. Ann NY Acad Sci 551: 75–82

    Google Scholar 

  • Cheeseman KH, Collins M, Proudfoot K, Slater TF, Burton GW, Webb AC, Ingold KU (1986) Studies on lipid peroxidation in normal and tumor tissues. Biochem J 235: 507–514

    Google Scholar 

  • Copeland ES (1983) A National Institute of Health Workshop report: free radicals in promotion — a Chemical Pathology Study Section Workshop. Cancer Res 43: 5631–5637

    Google Scholar 

  • Cornwell DG, Morisaki N (1984) Fatty acid peroxides in the control of cell proliferation: prostaglandins, lipid peroxides, and cooxidation reactions. In: Pryor WA (ed) Free radicals in biology, vol 6. Academic Press, New York, pp 96–148

    Google Scholar 

  • Corongiou F, Lai M, Milia A (1983) Carbon tetrachloride, bromotrichloromethane and ethanol acute intoxication. Biochem J 212: 625–631

    Google Scholar 

  • Demopoulos HB, Pietronigro DD, Flamm ES, Seligman ML (1980) The possible role of free radical reactions in carcinogenesis. J Environ Pathol Toxicol 3: 273–303

    Google Scholar 

  • Dormandy TL, Wickens DG (1988) Diene conjugation and peroxidation in precancer. J Environ Pathol Toxicol 153–159

  • Esterbauer H, Koller E, Slee R, Koster J (1986) Possible involvement of lipid peroxidation product 4-hydroxynoneal in the formation of fluorescent chromolipids. Biochem J 239: 405–409

    Google Scholar 

  • Glock GE, McLean P (1953) Further studies on the properties and assay of glucose-6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase of rat liver. Biochem J 55: 400–408

    Google Scholar 

  • Habig WH, Pabst MJ, Jacoby WB (1974) Glutathione transferase. The first enzymatic step in mercapturic acid formation. J Biol Chem 249: 7130–7139

    Google Scholar 

  • Halliwell B, Gutteridge JM, Cross CM (1992) Free radicals, antioxidants, and human disease: Where are we now? J Lab Clin Med 119: 598–620

    Google Scholar 

  • Hietanen E, Punnonen K, Punnonen R, Auvinen O (1986) Fatty acid composition and lipid peroxidation in human breast cancer and lipoma tissue. Carcinogenesis 7: 1965–1969

    Google Scholar 

  • Hietanen E, Bartsch H, Bereziat J-C, Ahotupa M, Camus A-M, Cabral JRP, Laitinen M (1990) Quantity and saturation degree of dietary fats as modulators of oxidative stress and chemically-induced liver tumours in rats. Int J Cancer 46: 640–647

    Google Scholar 

  • Ip C, Carter CA, Ip MM (1985) Requirement of essential fatty acids for mammary tumorigenesis in the rat. Cancer Res 45: 1997–2001

    Google Scholar 

  • Kensler TW, Taffe BG (1986) Free radicals in tumor promotion. Adv Free Radical Biol Med 2: 347–387

    Google Scholar 

  • Kumar K, Thangarju M, Sachdanandam P (1991) Changes observed in antioxidant system in the blood of postmenopausal women with breast cancer. Biochem Int 25: 371–380

    Google Scholar 

  • Lane HW, Butcl JS, Howard C, Shepherd F, Halligan R, Medina D (1985) The role of high levels of dietary fat in 7, 12-dimethylbenzanthracene-induced mammary tumorigenesis: lack of an effect on lipid peroxidation. Carcinogenesis 6: 403–407

    Google Scholar 

  • Layne EK (1957) Spectrophotometric and turbidimetric methods for measuring protein. Methods Enzymol 3: 447–454

    Google Scholar 

  • Logani MK, Solanki V, Slaga TJ (1982) Effect of tumor promoters on lipid peroxidation in mouse skin. Carcinogenesis 3: 1303–1308

    Google Scholar 

  • Misra HP, Fridovich I (1972) The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase. J Biol Chem 247: 3170–3175

    Google Scholar 

  • Nakashima R, Scott LJ, Pedersen PL (1986) The role of mitochondrial hexokinase binding in the abnormal energy metabolism of tumor cell lines. Ann NY Acad Sci 488: 438–450

    Google Scholar 

  • Otamiri T, Sjödahl R (1989) Increased lipid peroxidation in malignant tissues of patients with colorectal cancer. Cancer 64: 422–425

    Google Scholar 

  • Paglia D, Valentine W (1967) Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. J Lab Clin Med 70: 158–169

    Google Scholar 

  • Perchellet J-P, Perchellet EM (1989) Antioxidants and multistage carcinogenesis in mouse skin. Free Radical Biol Med 7: 377–408

    Google Scholar 

  • Petruzzelli S, Hietanen E, Bartsch H, Camus A-M, Mussi A, Angletti CA, Saracci R, Giuntini C (1990) Pulmonary lipid peroxidation in cigarette smokers and lung cancer patients. Chest 98: 930–935

    Google Scholar 

  • Punnonen K, Hietanen E, Auvinen O, Punnonen R (1989) Phospholipids and fatty acids in breast cancer tissue. J Cancer Res Clin Oncol 115: 575–578

    Google Scholar 

  • Punnonen R, Kudo R, Punnonen K, Hietanen E, Kuoppala T, Kainulainen H, Sato K, Ahotupa M (1993) Activities of antioxidant enzymes and lipid peroxidation in endometrial cancer. Eur J Cancer 29A: 266–269

    Google Scholar 

  • Sakai K, Okuyama H, Yura J, Takeyama H, Shinagawa H, Tsuruga N, Kato K, Miura K, Kawase K, Tsujimura T, Naruse T, Koike K (1992) Composition and turnover of phospholipids and neutral lipids in human breast cancer and reference tissues. Carcinogenesis 13: 579–584

    Google Scholar 

  • Sato K, Ito K, Koharada H, Yamaguchi Y, Adachi K, Endo H (1992) Negative regulation of catalase gene expression in hepatoma cells. Mol Cell Biol 12: 2525–2533

    Google Scholar 

  • Slater TF (1988) Lipid peroxidation and cell division in normal and tumour tissues. In: Nigam SK, McBrien DCH, Slater TF (eds) Eicosanoids, lipid peroxidation and cancer. Springer, Berlin Heidelberg New York, pp 137–142

    Google Scholar 

  • World Health Organization (1992) WHO Health Statistics Annual 1991, WHO, Geneva

    Google Scholar 

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Punnonen, K., Ahotupa, M., Asaishi, K. et al. Antioxidant enzyme activities and oxidative stress in human breast cancer. J Cancer Res Clin Oncol 120, 374–377 (1994). https://doi.org/10.1007/BF01247464

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  • DOI: https://doi.org/10.1007/BF01247464

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