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Original Article

Modulation of Glutathione and Glutathione Dependent Antioxidant Enzymes in Mouse Heart Following Doxorubicin Therapy

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Pages 111-120 | Received 12 May 1993, Published online: 07 Jul 2009

References

  • Carter S. K. Adriamycin-a review. Journal of the National Cancer Institute 1975; 55: 1265–1274
  • Von Hoff D. D., Rozencweig M., Piccart M. The cardiotoxicity of anticancer agents. Seminars in Oncology 1982; 9: 23–33
  • Myers C. E., McGuire W. P., Liss R. H., Grotzinger K., Young R. C. Adriamycin: the role of lipid peroxidation in cardiac toxicity and tumor response. Science 1977; 197: 165–167
  • Bachur N. R., Gordon S. L., Gee M. V. Anthracycline antibiotic augmentation of micro-somal electron transport and free radical formation. Molecular Pharmacology 1977; 13: 901–910
  • Mimnaugh E. G., Trush M. A., Gram T. E. Stimulation by Adriamycin of rat heart and liver microsomal NADH-dependent lipid peroxidation. Biochemical Pharmacology 1981; 30: 2797–2804
  • Olson R. D., Boerth R. C., Gerber J. G., Nies A. S. Mini-Review. Mechanism of Adriamycin cardiotoxicity: evidence of oxidative stress. Life Sciences 1981; 29: 1393–1401
  • Davies K. J.A., Doroshow J. H. Redox cycling of anthracyclines by cardiac mitochondria. I. Anthracycline radical formation by NADH dehydrogenase. The Journal of Biological Chemistry 1986; 261: 3060–3067
  • Doroshow J. H., Davies K. J.A. Redox cycling of anthracyclines by cardiac mitochondria. II. Formation of superoxide anion, hydrogen peroxide, and hydroxyl radical. The Journal of Biological Chemistry 1986; 261: 3068–3074
  • Bachur N. R., Gordon S. L., Gee M. V., Kon H. NADPH-cytochrome P-450 reductase activation of quinone anticancer agents to free radicals. Proceedings of the National Academy of Science, USA 1979; 76: 954–957
  • Bachur N. R., Gordon S. L., Gee M. V. A general mechanism for microsomal activation of quinone anticancer agents to free radicals. Cancer Research 1978; 38: 1745–1750
  • Harris R. N., Doroshow J. H. Effect of doxorubicin-enhanced hydrogen peroxide and hydroxyl radical formation on calcium sequestration by cardiac sarcoplasmic reticulum. Biochemical and Biophysical Research Communications 1985; 130: 739–745
  • Trimm J. L., Salama G., Abramson J. J. Sulfhydryl oxidation induces rapid calcium release from sarcoplasmic reticulum. The Journal of Biological Chemistry 1986; 261: 16092–16098
  • Vile G., Winterbourn C. Thiol oxidation and inhibition of Ca-ATPase by Adriamycin in rabbit heart microsomes. Biochemical Pharmacology 1990; 39: 769–774
  • Doroshow J. H., Akman S., Esworthy S., Chu F. F., Burke T. Doxorubicin resistance conferred by selective enhancement of intracellular glutathione peroxidase or superoxide dismutase content in human MCF-7 breast cancer cells. Free Radical Research Communications 1991; 12–13: 779–781
  • Doroshow J. H. Prevention of doxorubicin-induced killing of MCF-7 human breast cancer cells by oxygen radical scavengers and iron chelating agents. Biochemical and Biophysical Research Communications 1986; 135: 330–335
  • Doroshow J. H. Role of hydrogen peroxide and hydroxyl radical in the killing of Ehrlich tumor cells by anticancer quinones. Proceedings of the National Academy of Science, USA 1986; 83: 4514–4518
  • Muller A., Cadenes E., Graf P., Sies H. A novel biologically active seleno-organic compound-I: glutathione peroxidase-like activity in vitro and antioxidant capacity of PZ-51 (ebselen). Biochemical Pharmacology 1984; 33: 3235–3239
  • Dusre L., Mimnaugh E. G., Myers C. E., Sinha B. K. Potentiation of doxorubicin cytotoxicity by buthionine sulfoximine in multidrug-resistant human breast tumor cells. Cancer Research 1989; 49: 511–515
  • Revis N. W., Marusic N. Glutathione peroxidase activity and selenium concentration in the hearts of doxorubicin-treated rabbits. Journal of Molecular and Cellular Cardiology 1978; 10: 945–951
  • Doroshow J. H., Locker G. Y., Myers C. E. Enzymatic defenses of the mouse heart against reactive oxygen metabolites: Alterations produced by doxorubicin. Journal of Clinical Investigations 1980; 65: 128–135
  • Porta E. A., Joun N. S., Matsumura L., Nakasone B., Sablan H. Acute adriamycin cardiotoxicity in rats. Research Communications in Chemical Pathology and Pharmacology 1983; 41: 125–137
  • Jackson J. A., Reeves J. P., Muntz K. H., Kruk D., Prough R. A., Willerson J. T., Buja L. M. Evaluation of free radical effects and catecholamine alterations in adriamycin cardiotoxicity. American Journal of Pathology 1984; 117: 140–153
  • Olson R. D., Mac J. S., Donald C., vanBoxtel J., Boerth R. C., Harbison R. D., Slonim A. E., Freeman R. W., Gates J. A. Regulatory role of glutathione and soluble sulfhydryl groups in the toxicity of adriamycin. Journal of Pharmacology and Experimental Therapeutics 1980; 215: 450–454
  • Bertazzoli C., Bellini O., Magrini U., Tosana M. G. Quantitative experimental evaluation of adriamycin cardiotoxicity in the mouse. Cancer Treatment Reports 1979; 63: 1877–1883
  • Doroshow J. H., Locker G. Y., Ifrim I., Meyers C. E. Prevention of doxorubicin cardiac toxicity in the mouse by N-acetylcysteine. Journal of Clinical Investigations 1981; 68: 1053–1064
  • McCord J. M., Fridovich I. Superoxide dismutase: An enzymatic function for erythro-cuprein (hemocuprein). The Journal of Biological Chemistry 1969; 244: 6049–6055
  • Oberley L. W., Spitz D. R. Assay of superoxide dismutase in tumor tissue. Methods in Enzymology 1984; 105: 457–464
  • Aebi H. Catalase in vitro. Methods in Enzymology 1984; 105: 121–126
  • Racker E. Glutathione reductase (liver and yeast). Methods in Enzymology 1955; 2: 722–725
  • Strauss R. S., Snyder E. L., Wallace P. D., Rosenberger T. G. Oxygen detoxifying enzymes in neutrophils of infants in their mothers. Journal of Laboratory and Clinical Medicine 1980; 95: 897–902
  • Fariss M. W., Reed D. J. High-performance liquid chromatography of thiols and disulfides: Dinitrophenol derivatives. Methods in Enzymology 1987; 143: 101–109
  • Roe C. R., Limbird L. E., Wagner G. S., Nerenberg S. T. Combined isoenzyme analysis in the diagnosis of myocardial injury: Application of electrophoretic methods for the detection and quantitiation of the creatinine phosphokinase MB isoenzyme. Journal of Laboratory and Clinical Medicine 1972; 80: 577–590
  • Wills E. D. Evaluation of lipid peroxidation in lipids and biological membranes. Biochemical Toxicology, K. Snell, B. Mullock. IRL Press, Washington, DC 1987; 127–152
  • Gustafson D. L., Swanson J. D., Pritsos C. A. Role of xanthine oxidase in the potentiation of doxorubicin-induced cardiotoxicity by mitomycin C. Cancer communications 1991; 3: 299–304
  • Pritsos C. A., Sokoloff M., Gustafson D. L. PZ-51 (Ebselen) in vivo protection against adriamycin-induced mouse cardiac and hepatic lipid peroxidation and toxicity. Biochemical Pharmacology 1992; 44: 839–841
  • Paraidathathu T., Combs A. B., Kehrer J. P. In vivo effects of 1,3-bis(2-chloroethyl)-1-nitrosurea and doxorubicin on the cardiac and hepatic glutathione systems. Toxicology 1985; 35: 113–124
  • Rajagopalan S., Politi P. M., Sinha B. K., Myers C. E. Adriamycin-induced free radical formation in the perfused rat heart: Implications for cardiotoxicity. Cancer Research 1988; 48: 4766–4769

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