Inhibition of Radiation-induced Changes of Glyoxalase I Activity in Mouse Spleen and Liver by Phenothiazines

References

• Alper T. Low oxygen enhancement ratios for radiosensitive bacterial strains and the probable interaction of two types of primary lesion. Nature 1968; 217: 862–863
   PubMed Web of Science ®Google Scholar
• Aust S.D. Sources of iron for lipid peroxidation in biological systems. Oxygen Radicals and Tissue Injury. Proceedings of an Upjohn Symposium, B. Halliwell. Upjohn, 1988; 27–33, In
   Google Scholar
• Bend J.R., Singh J.S. Xenobiotic metabolism by extrahepatic tissues. Drug Metabolism and Drug Toxicity, J.R. Mitchell, M.G. Horning. Raven, New York 1984; 110–110, In
   Google Scholar
• Bergonie J., Tribondeau L. Interpretation of some results of radiotherapy and an attempt at determining a logical technique of treatment. Radiation Research 1959; 11: 587–588
   PubMed Web of Science ®Google Scholar
• Bertsche U. Induction and repair of X-ray damage in mammalian cell cultures treated with membrane active drugs. British Journal of Cancer 1984; 49(Suppl. 6)121–127
   Google Scholar
• Bezkorovainy A. Biochemistry of nonheme iron in man. Iron proteins and cellular iron metabolism. Clinical Physiology and Biochemistry 1989; 7: 1–17
   PubMedGoogle Scholar
• Borg D.C., Schiach K.M. Cytotoxicity from coupled redox cycling of auto-oxidising xenobiotics and metals. Israel Journal of Chemistry 1984; 24: 38–53
   Web of Science ®Google Scholar
• Bradford M.M. A rapid and sensitive method of quantitation of microgram quantities of protein utilizing the principle of protein dye binding. Analytical Biochemistry 1976; 72: 248–254
   PubMed Web of Science ®Google Scholar
• Breyer U., Schmalzing G. Metabolism and disposition of trifluoperazine in rat. A thin layer chromatographic method for measurement of trifluoperazine and its metabolites in rat tissues. Drug Metabolism and Disposition 1977; 5: 97–103
   PubMedGoogle Scholar
• Cleare M.J., Hydes P.C. Antitumour properties of metal complexes. Metal Ions in Biological Systems, H. Sigel. Marcel Dekker, New York 1990; 11: 1–62, In
   Google Scholar
• Clelland J.D., Thornalley P.J. S-2-Hydroxyacylglutathione derivatives: enzyme preparation, purification and characterisation. Journal of the Chemical Society, Perkin Transactions 1991; 1: 3009–3015
   Google Scholar
• Cohen C., Shulman G., Budgeon L.R. Immunohistochemical ferritin in testicular seminoma. Cancer 1984; 54: 2190–2194
   PubMedGoogle Scholar
• Dunford H.B. Free radicals in iron containing systems. Free Radicals in Biology and Medicine 1987; 3: 405–421
   PubMed Web of Science ®Google Scholar
• Gutteridge J.M.C., Beard A.P.C., Quikin G.J. Superoxide dependent lipid peroxidation problems with the use of catalase as a specific probe for Fenton-derived hydroxyl radicals. Biochemical and Biophysical Research Communication 1983; 117: 901–901
   PubMedGoogle Scholar
• Gutteridge J.M.C. Bleomycin-detectable iron in knee-joint synovial fluid from arthritic patients and its relationship to the extracellular antioxidant activities of caeruloplasmin, transferrin and lactoferrin. Biochemical Journal 1988; 245: 415–421
   Google Scholar
• Halliwell B., Gutteridge J.M.C. Role of free radicals and catalytic metal ions in human disease: an overview. Methods in Enzymology 1990; 186: 1–67
   PubMed Web of Science ®Google Scholar
• Halliwell B., Aruoma O.I., Wasil M., Gutteridge J.M.C. The resistance of transferrin, lactoferrin and caeruloplasmin to oxidative damage. Biochemical Journal 1988; 256: 311–312
   PubMedGoogle Scholar
• Hooper N.I., Tisdale M.J., Thornalley P.J. Modification of the glyoxalase system in human HL60 promyeloctyic leukemia cells during differentiation to neutrophils in vitro. Biochimica et Biophysica Acta 1988; 966: 362–369
   PubMedGoogle Scholar
• Kojima N., Bates G.W. The reduction and release of iron from Fe3+-transferrin-Co32–. Journal of Biological Chemistry 1979; 254: 8847–8854
   PubMedGoogle Scholar
• Kozarich J.W., Deegan J.L. 7-Methylguanosine-dependent inhibition of globin mRNA translation by methylglyoxal. Journal of Biological Chemistry 1979; 254: 9345–9347
   PubMedGoogle Scholar
• Maniar H.S., Singh B.B. Modification of radiation response of E. coli B/r cells by phenothiazines. International Journal of Radiation Biology 1983; 44: 399–404
   Web of Science ®Google Scholar
• McLellan A.C., Thornalley P.J. Glyoxalase activity in human RBC fractionated by age. Mechanism of Ageing and Development 1989; 48: 63–71
   PubMed Web of Science ®Google Scholar
• O'Connell M.J., Ward R.J., Baum H., Peters T.J. The role of iron in ferritin and hemosiderin-mediated lipid peroxidation in liposomes. Biochemical Journal 1985; 229: 135–139
   PubMed Web of Science ®Google Scholar
• Papahadijopoulos D., Jacobson K., Poste G., Shepherd G. Effects of local anesthetics on membrane properties. I. Changes in the fluidity of phospholipid bilayers. Biochimica et Biophysica Acta 1975; 394: 504–519
   PubMedGoogle Scholar
• Saito M., Morehouse L.A., Aust S.D. Transferrin dependent lipid peroxidation. Free Radicals in Biology of Medicine 1986; 2: 99–105
   Google Scholar
• Seeman P. The membrane action of anesthetics and tranquillizers. Pharmacological Review 1972; 24: 139–159
   Google Scholar
• Sharma R., Kale R.K. Effect of radiation on glyoxalase I and glyoxalase II activities in spleen and liver of mice. International Journal of Radiation Biology 1993; 63: 233–238
   PubMed Web of Science ®Google Scholar
• Sheetz M.P., Singer S.J. Biological membrane as bilayer couples. A molecular mechanism of drug-erythrocyte interaction. Proceedings of the National Academy of Sciences, USA 1974; 71: 4457–4461
   PubMed Web of Science ®Google Scholar
• Sitasawad S.L. Investigation into radiation-induced lipid peroxidation. Jawaharlal Nehru University, New Delhi 1992, PhD thesis
   Google Scholar
• Shenoy M.A., Singh B.B. Non-nitro radiation sensitizers. International Journal of Radiation Biology 1985; 48: 315–326
   Web of Science ®Google Scholar
• Shenoy M.A., Blaglow J.W., Varnes M.E., Daniael J.W. A biochemical basis for the radiosensitizing and cytotoxic effects of chlorpromazine hydrochloride in vitro and in vivo. International Journal of Radiation Oncology, Biology and Physics 1982; 8: 725–728
   PubMed Web of Science ®Google Scholar
• Sieman D.W. New trends in improving oxygen delivery to tumour tissues. Proceedings of the Eighth International Congress of Radiation Research, E.M. Fielden, J.F. Fowler, J.H. Hendry, D. Scott, 1987; 2: 713–718, In
   Google Scholar
• Sigel H. Metal Ions in Biological Systems: Metal Complexes as Antitumour Agents. Marcel Dekker, New York 1980
   Google Scholar
• Sutrave P. Role of glycoxalase I in biological systems. Jawaharlal Nehru University, New Delhi 1979, PhD thesis
   Google Scholar
• Sutrave P., Rao A.R. Studies in glyoxalase I in regenerating mouse spleen. Life Sciences Advances 1982; 1: 141–145
   Google Scholar
• Song C.W., Kang M.S., Rhee J.G., Levitt S.H. The effect of hyperthermia on vascular function, pH and cell survival. Radiology 1980; 137: 795–795
   PubMed Web of Science ®Google Scholar
• Thornalley P.J. Review: The glyoxalase system: New developments towards functional characterization of metabolic pathway fundamental to biological life. Biochemistry Journal 1990; 269: 1–11
   PubMed Web of Science ®Google Scholar
• Thornalley P.J. The glyoxalase system in health and disease. Molecular Aspects of Medicine 1993; 14: 287–371
   PubMed Web of Science ®Google Scholar
• U R., Engler M.J. Introductory synopsis on heat generation and temperature measuring systems. Fundamentals of Cancer Therapy by Hyperthermia, Radiation and Chemicals, E. Kano. Mozg Bros, Tokyo 1983; 9–32, In
   Google Scholar
• VanderJagt D.L., Daub F., Krahn J.A., Han L.P.B. Effect of pH and thiols on the kinetics of yeast glyoxalase I. An evaluation of the random pathway mechanism. Biochemistry 1975; 14: 3669–3675
   PubMedGoogle Scholar
• Varshney R., Kale R.K. Effect of calmodulin antagonists on radiation induced lipid peroxidation in microsomes. International Journal of Radiation Biology 1990; 58: 733–743
   PubMed Web of Science ®Google Scholar
• Wilson R.L. Organic peroxy free radicals as ultimate agents in oxygen toxicity. Oxidative Stress, H. Sies. Academic, London 1985; 41–72, In
   Google Scholar
• Yatvin M.B., Schmitz B.J., Dennis W.H. Radiation Killing of E. coli K. 1060: role of membrane fluidity, hypothermia and local anaesthetics. International Journal of Radiation Biology 1980; 37: 513–519
   Web of Science ®Google Scholar
• Yau T.M., Kim S.C. Radioprotection of mammalian cells by procaine. British Journal of Radiology 1978; 51: 551–552
   PubMedGoogle Scholar