Skip to main content
NCBI home page
British Journal of Cancer logoLink to British Journal of Cancer
. 1983 Jun;47(6):809–812. doi: 10.1038/bjc.1983.135

Activities of free radical metabolizing enzymes in tumours.

M J Tisdale, M B Mahmoud
PMCID: PMC2011368  PMID: 6860548

Abstract

The activity of enzymatic defences against free radical attack including superoxide dismutase (SOD), catalase, glutathione peroxidase and glutathione reductase have been compared in some experimental animal tumours with the corresponding normal mouse tissues. The activity of SOD in PC6 plasmacytoma and P388 lymphocytic leukaemia was lower than in normal lymphocytes and the activity in a mouse bladder carcinoma (MB) was one-half of that of the normal bladder tissue. Similarly PC6, P388, TLX5 lymphoma and MB showed lower catalase activity than the corresponding normal tissues. The activity of glutathione peroxidase in tumours was in general comparable with that of the normal tissues with the exception of MB, while TLX5, PC6 and P388 contained much lower glutathione reductase activity than normal lymphocytes. The results suggest that it may be possible to selectively destroy certain tumours by peroxidative attack, and that P388 leukaemia would be much more sensitive than L1210 leukaemia to free radical production.

Full text

PDF
809

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Beauchamp C., Fridovich I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem. 1971 Nov;44(1):276–287. doi: 10.1016/0003-2697(71)90370-8. [DOI] [PubMed] [Google Scholar]
  2. Crapo J. D., Tierney D. F. Superoxide dismutase and pulmonary oxygen toxicity. Am J Physiol. 1974 Jun;226(6):1401–1407. doi: 10.1152/ajplegacy.1974.226.6.1401. [DOI] [PubMed] [Google Scholar]
  3. Dionisi O., Galeotti T., Terranova T., Azzi A. Superoxide radicals and hydrogen peroxide formation in mitochondria from normal and neoplastic tissues. Biochim Biophys Acta. 1975 Oct 22;403(2):292–300. doi: 10.1016/0005-2744(75)90059-5. [DOI] [PubMed] [Google Scholar]
  4. Favaudon V. On the mechanism of reductive activation in the mode of action of some anticancer drugs. Biochimie. 1982 Jul;64(7):457–475. doi: 10.1016/s0300-9084(82)80162-4. [DOI] [PubMed] [Google Scholar]
  5. Fernandez-Pol J. A., Hamilton P. D., Klos D. J. Correlation between the loss of the transformed phenotype and an increase in superoxide dismutase activity in a revertant subclone of sarcoma virus-infected mammalian cells. Cancer Res. 1982 Feb;42(2):609–617. [PubMed] [Google Scholar]
  6. Goldin A., Venditti J. M., Macdonald J. S., Muggia F. M., Henney J. E., Devita V. T., Jr Current results of the screening program at the Division of Cancer Treatment, National Cancer Institute. Eur J Cancer. 1981 Feb;17(2):129–142. doi: 10.1016/0014-2964(81)90027-x. [DOI] [PubMed] [Google Scholar]
  7. Gutierrez P. L., Friedman R. D., Bachur N. R. Biochemical activation of AZQ [3,6-diaziridinyl-2,5-bis(carboethoxyamino)-1,4-benzoquinone] to its free radical species. Cancer Treat Rep. 1982 Feb;66(2):339–342. [PubMed] [Google Scholar]
  8. Ishida R., Takahashi T. Increased DNA chain breakage by combined action of bleomycin and superoxide radical. Biochem Biophys Res Commun. 1975 Oct 27;66(4):1432–1438. doi: 10.1016/0006-291x(75)90519-7. [DOI] [PubMed] [Google Scholar]
  9. Oberley L. W., Bize I. B., Sahu S. K., Leuthauser S. W., Gruber H. E. Superoxide dismutase activity of normal murine liver, regenerating liver, and H6 hepatoma. J Natl Cancer Inst. 1978 Aug;61(2):375–379. [PubMed] [Google Scholar]
  10. Oberley L. W., Buettner G. R. Role of superoxide dismutase in cancer: a review. Cancer Res. 1979 Apr;39(4):1141–1149. [PubMed] [Google Scholar]
  11. Olson R. D., Boerth R. C., Gerber J. G., Nies A. S. Mechanism of adriamycin cardiotoxicity: evidence for oxidative stress. Life Sci. 1981 Oct 5;29(14):1393–1401. doi: 10.1016/0024-3205(81)90001-1. [DOI] [PubMed] [Google Scholar]
  12. Pinto R. E., Bartley W. Glutathione reductase and glutathione peroxidase activities in hepatomous livers of rats treated with diethylnitrosamine. FEBS Lett. 1973 Jun 1;32(2):307–309. doi: 10.1016/0014-5793(73)80860-9. [DOI] [PubMed] [Google Scholar]
  13. Pinto R. E., Bartley W. The effect of age and sex on glutathione reductase and glutathione peroxidase activities and on aerobic glutathione oxidation in rat liver homogenates. Biochem J. 1969 Mar;112(1):109–115. doi: 10.1042/bj1120109. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Trush M. A., Mimnaugh E. G., Ginsburg E., Gram T. E. Studies on the in vitro interaction of mitomycin C, nitrofurantoin and paraquat with pulmonary microsomes. Stimulation of reactive oxygen-dependent lipid peroxidation. Biochem Pharmacol. 1982 Mar 1;31(5):805–814. doi: 10.1016/0006-2952(82)90467-1. [DOI] [PubMed] [Google Scholar]
  15. Worthington D. J., Rosemeyer M. A. Human glutathione reductase: purification of the crystalline enzyme from erythrocytes. Eur J Biochem. 1974 Oct 1;48(1):167–177. doi: 10.1111/j.1432-1033.1974.tb03754.x. [DOI] [PubMed] [Google Scholar]

Articles from British Journal of Cancer are provided here courtesy of Cancer Research UK

RESOURCES