Inhibition of Microsomal Lipid Peroxidation and Cytochrome P-450-Catalyzed Reactions by Nitrofuran Compounds

References

• Marr J. J., Docampo R. Chemotherapy for Chagas' disease: a perspective of current therapy and considerations for future research. Reviews of Infectious Diseases 1986; 8: 884–903
   PubMedGoogle Scholar
• Stoppani A. O. M. Rational approaches to Chagas' disease chemotherapy. Rendicunti della Accademia Nazionale Delle Scienze Detta Dei XL 1986; 10: 125–139
   Google Scholar
• Docampo R., Stoppani A. O. M. Generation of superoxide anion hydrogen peroxide induced by nifurtimox in Trypanosoma cruzi. Archives of Biochemistry and Biophysics 1979; 197: 317–321
   PubMed Web of Science ®Google Scholar
• Docampo R., Moreno S. N. J., Stoppani A. O. M., Leon W., Cruz F. S., Villalta F., Munˆiz R. F. A. Mechanism of nifurtimox toxicity in different forms of Trypanosoma cruzi. Biochemical Pharmacology 1981; 30: 1947–1951
   PubMed Web of Science ®Google Scholar
• Docampo R., Moreno S. N. J., Stoppani A. O. M. Nitrofuran enhancement of microsomal electron transport, superoxide anion production and lipid peroxidation. Archives of Biochemistry and Biophysics 1981; 207: 316–324
   PubMed Web of Science ®Google Scholar
• Goijman S. G., Stoppani A. O. M. Effects of nitroheterocyclic drugs on macromolecule synthesis and degradation in Trypanosoma cruzi. Biochemical Pharmacology 1985; 34: 1331–1336
   PubMed Web of Science ®Google Scholar
• Goijman S. G., Frasch A. C. C., Stoppani A. O. M. Damage ofTrypanosoma cruzideoxyribonucleic acid by nitroheterocyclic drugs. Biochemical Pharmacology 1985; 34: 1457–1461
   PubMed Web of Science ®Google Scholar
• Goijman S. G., Stoppani A. O. M. Oxygen radicals and macromolecule turnover in Trypanosoma cruzi. Oxidative Damage and Related Enzymes, G. Rotillo, J. V. Bannister. Harwood Academic Publisher GMBH, Chur, London, New York 1984; 216–221
   Google Scholar
• Cataldi de Flombaum M. A., Stoppani A. O. M. Inactivation of mitochondrial adenosine triphosphatase fromTrypanosoma cruziby oxygen radicals. Biochemistry International 1986; 12: 785–793
   PubMedGoogle Scholar
• Dubin M., Moreno S. N. J., Martino E. E., Docampo R., Stoppani A. O. M. Increased biliary secretion and loss of hepatic glutathione in rat liver after nifurtimox treatment. Biochemical Pharmacology 1983; 32: 483–487
   PubMed Web of Science ®Google Scholar
• Dubin M., Goijman S. G., Stoppani A. O. M. Effect of nitroheterocyclic drugs on lipid peroxidation and glutathione content in rat liver extracts. Biochemical Pharmacology 1984; 33: 3419–3423
   PubMed Web of Science ®Google Scholar
• Dubin M., Grinblat L., Fernandez Villamil S. H., Stoppani A. O. M. Nitrofuran inhibition of microsomal lipid peroxidation. FEBS Letters 1987; 220: 197–200
   PubMed Web of Science ®Google Scholar
• Castro J. A., Diaz de Toranzo E. G. Toxic effects of nifurtimox and benzinidazole, two drugs used against American Trypanosomiasis (Chagas' disease). Biomedical and Environmental Sciences 1988; 1: 19–33
   PubMedGoogle Scholar
• Nagel R. Genotoxicity studies with two antichagasic drugs. Mutation Research 1987; 191: 17–20
   PubMed Web of Science ®Google Scholar
• Mester B., Elguero J., Claramunt R. M., Castanys S., Mascaro M. L., Osuna A., Vilaplana M. J., Molina P. Activity againstTrypanosoma cruziof new analogues of nifurtimox. Archives in Pharmacy (Weinheim) 1987; 320: 115–120
   PubMed Web of Science ®Google Scholar
• Alejandre-Duran E., Claramunt R. M., Sanz D., Vilaplana M. J., Molina P., Pueyo C. Study of the mutagenicity of nifurtimox and eight derivatives with the L-arabinose resistance test of Salmonella typhimurium. Mutation Research 1988; 206: 193–200
   PubMed Web of Science ®Google Scholar
• Grinblat L., Sreider C. M., Stoppani A. O. M. Nitrofuran inhibition of yeast and rat tissue glutathione reductases. Structure-activity relationships. Biochemical Pharmacology 1989; 38: 767–772
   PubMed Web of Science ®Google Scholar
• Sreider C. M., Grinblat L., Stoppani A. O. M. Catalysis of nitrofuran redox-cycling and superoxide anion production by heart lipoamide dehydrogenase. Biochemical Pharmacology 1990; 40: 1849–1857
   PubMed Web of Science ®Google Scholar
• Fernandez Villamil S. H., Dubin M., Brusa M. A., Duran R. P., Perissinotti L. J., Stoppani A. O. M. Generation of radical anions of nifurtimox and related nitrofuran compounds by ascorbate. Free Radical Research Communications 1990; 10: 351–360
   PubMed Web of Science ®Google Scholar
• Misra H. P., Fridovich I. The univalent reduction of oxygen by reduced flavins and quinones. Journal of Biological Chemistry 1972; 247: 188–192
   PubMed Web of Science ®Google Scholar
• Azzi A., Montecuoco C., Richter C. The use of acetylated ferricytochrome c for the detection of superoxide radicals produced in biological membranes. Biochemical Biophysical Research Communications 1975; 65: 597–603
   PubMed Web of Science ®Google Scholar
• Lake B. G. Determination of aniline 4-hydroxylase. Biochemical Toxicology, K. Snell, B. Mullock. IRL Press, Oxford 1987; 206–207
   Google Scholar
• Lake B. G. Determination of NADPH-cytochrome c (P450) reductase. Biochemical Toxicology, K. Snell, B. Mullock. IRL Press, Oxford 1987; 200–201
   Google Scholar
• Rogers M. J., Strittmatter P. The interaction of NADH-cytochromeb5reductase and cytochromeb5bound to egg lecithin liposomes. Journal of Biological Chemistry 1975; 250: 5713–5718
   PubMed Web of Science ®Google Scholar
• Misra P. H., Fridovich T. The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase. Journal of Biological Chemistry 1972; 247: 3170–3175
   PubMed Web of Science ®Google Scholar
• Aebi H. Catalase. Methods of Enzymatic Analysis, H. U. Bergmeyer. Verlag Chemie International, Deerfield Beach, Florida 1981; 22: 673–684
   Google Scholar
• Placer Z. A., Cushman L., Johnson B. C. Estimation of product of lipid peroxidation (malonyl dialdehyde) in biochemical systems. Analytical Biochemistry 1966; 16: 359–364
   PubMed Web of Science ®Google Scholar
• Gornall A. G., Bardawill C. J., David M. M. Determination of serum proteins by means of the biuret reaction. Journal of Biological Chemistry 1949; 177: 751–766
   PubMed Web of Science ®Google Scholar
• Omura T., Sato R. Isolation of cytochrome P-450 and P-420. Methods in Enzymology, R. W. Estabrook, M. E. Pullman. Academic Press, New York 1967; 10: 556–561
   Google Scholar
• Lake B. G. Determination of cytochromeb5. Biochemical Toxicology, K. Snell, B. Mullock. IRL Press, Oxford 1987; 194
   Google Scholar
• Stewart J. J. P. Optimization of parameters for semiempirical methods (I). Journal of Computational Chemistry 1989; 10: 209–220
   Web of Science ®Google Scholar
• Stewart J. J. P. Optimization of parameters for semiempirical methods (II). Applications. Journal of Computational Chemistry 1989; 10: 221–264
   Web of Science ®Google Scholar
• Dewar M. J. S., Zoebisch E. G., Healy E. F., Stewart J. J. P. AMI: a new general purpose quantum mechanical molecular model. Journal of the American Chemical Society 1985; 107: 3902–3909
   Web of Science ®Google Scholar
• Dubin M., Fernandez Villamil S. H., Stoppani A. O. M. Inhibition of microsomal lipid peroxidation and cytochrome P-450-catalyzed reactions by zˆ-lapachone and related naphthoquinones. Biochemical Pharmacology 1990; 39: 1151–1160
   PubMed Web of Science ®Google Scholar
• Mason R. P., Holtzman J. L. The mechanism of microsomal and mitochondrial nitroreductase. Electron spin resonance evidence for nitroaromatic free radical intermediates. Biochemistry 1975; 14: 1626–1632
   PubMed Web of Science ®Google Scholar
• Gutteridge J. M. C. Lipid peroxidation: some problems and concepts. Oxygen Radicals and Tissue Injury, B. Halliwell. The Upjohn Company and FASEB, Bathesda, Maryland 1987; 9–19
   Google Scholar
• Minotti G., Aust S. D. The role of iron in oxygen radical mediated lipid peroxidation. Chemical Biological Interactions 1989; 71: 1–19
   PubMed Web of Science ®Google Scholar
• Iba M. M., Mannering G. P. NADPH- and linoleic acid hydroperoxide-induced lipid peroxidation and destruction of cytochrome P-450 in hepatic microsomes. Biochemical Pharmacology 1987; 36: 1447–1455
   PubMed Web of Science ®Google Scholar
• Lane M. W., Segall H. J. In vitroeffects oftrans-4-hydroxy-2-alkenals on mouse liver cytochrome P-450. Chemical Biological Interactions 1987; 62: 59–74
   PubMed Web of Science ®Google Scholar
• Karuzina I. I., Varenitsa A. I., Archakov A. I. Comparative inhibitor analysis of the hydroxylation of aniline by cytochrome P-450 in NADPH-, cumene hydroperoxide-, and H2 O 2-dependent systems. Biokhimiia 1983; 48: 1788–1793
   PubMedGoogle Scholar
• Lopez de Compadre R. L., Debnath A. K., Shusterman A. J., Hansch C. LUMO energies and hydrophobicity as determinants of mutagenicity by nitroaromatic compounds in Salmonella typhimurium. Environmental and Molecular Mutagenesis 1990; 15: 44–55
   PubMed Web of Science ®Google Scholar
• Meisel D., Neta P. One-electron redox potentials of nitro compounds and radiosensitizers. Correlation with spin densities of their radical anions. Journal of the American Chemical Society 1975; 97: 5198–5203
   Web of Science ®Google Scholar
• Taniguchi H., Imai Y., Sato R. Protein-protein and lipid interactions in a reconstituted cytochrome P-450 dependent microsomal monoxygenase. Biochemistry 1987; 26: 7084–7090
   PubMed Web of Science ®Google Scholar