Summary
The enzymatic destruction of oxidizing products produced during metabolic reduction of oxygen in the cell (such as singlet oxygen, H2O2 and OH radical) involves the concerted action of superoxide dismutase-which removes O -2 and yields H2O2-and H2O2 removing enzymes such as catalase and glutathione peroxidase. A difference in distribution or ratio of these enzymes in various tissues may result in a different reactivity of oxygen radicals.
It was found that in red blood cells superoxide dismutase and catalase are extracted in the same fraction as hemoglobin, while glutathione peroxidase appears to be “loosely” bound to the cellular structure. This suggests that in red blood cells catalase acts in series with superoxide dismutase against bursts of oxygen radicals formed from oxyhemoglobin, while glutathione & peroxidase may protect the cell membrane against low concentrations of H2O2. On the other hand, catalase activity is absent in various types of ascites tumor cells, while glutathione peroxidase and superoxide dismutase are found in the cytoplasm. However, the peroxidase/dismutase ratio is lower than in liver cells, and this may provide an explanation for the higher susceptibility of tumor cells to treatments likely to involve oxygen radicals.
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References
Fridovich, I., Acc. Chem. Res. 5, 321–326, 1972.
Rotilio, G., Calabrese, L., Finazzi Agro, A., Argento-Cerù, M. P., Autuori, F. and Mondovl, B., Biochim. Biophys. Acta, 321, 98–102, 1973.
McCord, J. M., and Fridovich, I., J. Biol. Chem. 244, 6049, 1969.
McCord, J. M., Keele, B. B. and Fridovich, I., Proc. Natl. Acad. Sci. U.S.A. 68, 1024–1027, 1971.
Fee, J. A. and Teitelbaum, H. D., Biochem. Biophys. Res. Comm. 49, 150–158, 1972.
Finazzi Agro, A., Giovagnoli, C., De Sole, P., Calabrese, L., Rotilio, G., Mondovì, B., FEBS Letters 21, 183–185, 1972.
Finazzi Agrò, A., De Sole, P., Rotilio, G. and Mondovì, B., Ital. J. Biochem. 22, 217–231, 1973.
Pederson, T. C. and Aust, S. D., Biochem. Biophys. Res. Comm. 52, 1071–1078, 1973.
Lavelle, F., Michelson, A. M. and Dimitrijevic, L. Biochem. Biophys. Res. Comm. 55, 350–357, 1973.
Weser, U. and Paschen, W., FEBS Letters 27, 248–250, 1972.
Porter, D. J. T. and Ingraham, L. L., Biochim. Biophys. Acta 334, 97–102, 1974.
Cohen, G. and Hochstein, P., Biochemistry 2, 1420–1428, 1963.
Wever, R., Oudega, B. and Van Gelder, B. F., Biochim. Biophys. Acta 302, 475–478, 1973.
Errera, M. and Forssberg, eds. Mechanism in Radiobiology, Vol. I, Academic Press, 1961.
Gilbert, D. L., Gerschuman, R., Cohen, T. and Sherwood, W., J. Am. Chem. Soc. 79, 5677–5686, 1957.
Allen, J. E., Goodman, D. B. P., Besarab, A. and Rasmussen, H., Biochim. Biophys. Acta 320, 708–728, 1973.
Schowoch, G. and Passow, H. Mol. Cell. Biochem. 2, 197–218, 1973.
Klein, G. and Klein, Eva, Cancer Res. 11, 466–470, 1951.
Cavaliere, R. Ciocatto, E. C., Giovanella, B. C., Heidelberger, C., Johnson, R. O., Margottini, M., Mondovì, B., Moricca, C., and Rossi Fanelli, A., Cancer 20, 1351–1381, 1967.
Kvetina, J. and Guaitani, A., Pharmacology 2, 65–68, 1969.
Tennant, J. R. Transplantation 2, 685–694, 1964.
Nishikimi, M., Rao, N. A. and Yagi, K. Biochem. Biophys. Res. Comm. 46, 849–853, 1972.
Misra, H. P. and Fridovich, I., J. Biol. Chem. 247, 188–192, 1972.
Lück, H. in Methods of Enzymatic Analysis, 2° Ed. (ed. Bergmayer, M. U.) p. 886–888, Verlag Chemic. Acad. Press New York.
Paglia, E. D. and Valentine, W. N., J. Lab. Clin. Med. 70, 158–169, 1967.
Ellman, G. L. and Callaway, E., Nature 192, 1216, 1961.
Pocker, Y. and Stone, J. T., Biochemistry 6, 628–678, 1967.
Goa, J., J. Clin. Lab. Invest. 5, 218–222, 1953.
Rossi Fanelli, A., Antonini, E. and Caputo, A., Biochim. Biophys. Acta 30, 608–615, 1958.
DeDuve, C., Acta Chem. Scand. 2, 264–273, 1948.
Horejsi, J., in Red Cell Metabolism and Function (Brewer, G. J. Ed.), pl. 9–20, Plenum Press, New York, 1970.
Hanahan, D. J., Biochim. Biophys. Acta 300, 319–340, 1973.
Hosod, S. and Natamura, W., Biochim. Biophys. Acta 222, 53–64, 1970.
Hochstein, P. and Utley, N., Mol. Pharmacol. 4, 574–579, 1968.
Misra, H. P. and Fridovich, I., J. Biol. Chem. 247, 6960–6962, 1972.
Brunori, M., Falcioni, G., Fioretti, E., Giardina, B. and Rotilio, G., Europ. J. Biochem., 53, 99–104, 1975.
Nicholls, P., Biochem. Biophys. Acta 279, 306–308, 1972.
Christophersen, B. O., Biochim. Biophys. Acta 176, 463–470, 1969.
Cohen, G. and Heikkila, R. F., J. Biol. Chem. 249, 2447–2454, 1974.
Dalton, H. J., In Cellular Control Mechanism and Cancer (ed. by P. Emmelot and O. Mühlbock) pp. 211–225, Elsevier, Amsterdam, 1964.
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Bozzi, A., Mavelli, I., Finazzi Agrò, A. et al. Enzyme defense against reactive oxygen derivatives. II. Erythrocytes and tumor cells. Mol Cell Biochem 10, 11–16 (1976). https://doi.org/10.1007/BF01731676
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DOI: https://doi.org/10.1007/BF01731676