The iron-binding and hydroxyl radical scavenging action of anti-inflammatory drugs

References

• Anbar M., Neta P. A compilation of specific bimolecular rate constants for the reactions of hydrated electrons, hydrogen atoms and hydroxyl radicals with inorganic and organic compounds in aqueous solution. International Journal of Applied Radiation and Isotopes 1967; 18: 495–523
   Google Scholar
• Aruoma O. I., Wasil M., Halliwell B., Hoey B. M., Butler J. The scavenging of oxidants by sulphasalazine and its metabolites. A possible contribution to their anti-inflammatory effects?. Biochemical Pharmacology 1987a; 36: 3739–3742
   PubMed Web of Science ®Google Scholar
• Aruoma O. I., Grootveld M., Halliwell B. The role of iron in ascorbate-dependent deoxyriboxe degradation. Evidence consistent with a site-specific hydroxyl radical generation caused by iron ions bound to the deoxyribose molecule. Journal of Inorganic Biochemistry 1987b; 29: 289–299
   Web of Science ®Google Scholar
• Biemond P., Swaak A. J. G., Penders J. M. A., Biendorff C. M., Koster J. F. Superoxide production by polymorphonuclear leukocytes in rheumatoid arthritis and osteoarthritis: in vivo inhibition by the antirheumatic drug piroxicam due to interference with the activation of the NADPH oxidase. Annals of the Rheumatic Diseases 1986; 45: 249–255
   PubMed Web of Science ®Google Scholar
• Borg D. C., Schaich K. M. Cytotoxicity from coupled redox cycling of autoxidizing xenobiotics and metals. Israel Journal of Chemistry 1984; 24: 38–53
   Web of Science ®Google Scholar
• Czapski G. On the use of OH scavengers in biological systems. Israel Journal of Chemistry 1984; 24: 29–32
   Web of Science ®Google Scholar
• Czapski G., Goldstein S. When do metal complexes protect the biological system from superoxide toxicity and when do they enhance it?. Free Radical Research Communications 1986; 1: 157–161
   PubMedGoogle Scholar
• Diguiseppi J., Fridovich I. The toxicology of molecular oxygen. CRC Critical Reviews in Toxicology 1984; 12: 315–342
   Web of Science ®Google Scholar
• Dowling E. J., Symons A. M., Parke D. V. Free radical production at the site of an acute inflammatory reaction as measured by chemiluminescence. Agents and Actions 1986; 19: 203–207
   PubMedGoogle Scholar
• Grootveld M., Halliwell B. An aromatic hydroxylation assay for hydroxyl radicals utilizing high-performance liquid chromatography. Use to investigate the effect of EDTA on the Fenton reaction. Free Radical Research Communications 1986a; 1: 243–250
   PubMedGoogle Scholar
• Grootveld M., Halliwell B. Aromatic hydroxylation as a potential measure of hydroxyl radical formation in vivo Identification of hydroxylated derivatives of salicylate in human body fluids. Biochemical Journal 1986b; 237: 499–504
   PubMed Web of Science ®Google Scholar
• Gutteridge J. M. C. Thiobarbituric acid-reactivity following iron-dependent free radical damage to amino acids and carbohydrates. FEBS Letters 1981; 128: 343–346
   PubMed Web of Science ®Google Scholar
• Gutteridge J. M. C. Reactivity of hydroxyl and hydroxyl-like radical discriminated by release of thiobarbituric-acid-reactive material from deoxyribose, nucleosides and benzoate. Biochemical Journal 1984; 224: 761–767
   PubMed Web of Science ®Google Scholar
• Gutteridge J. M. C. Ferrous-salt promoted damage to deoxyribose and benzoate. The increased effectiveness of hydroxyl-radical scavengers in the presence of EDTA. Biochemical Journal 1987; 243: 709–714
   PubMed Web of Science ®Google Scholar
• Gutteridge J. M. C., Halliwell B. Biology of superoxide and hydroxyl radicals. In vivo production and reactivity. Oxygen and Sulfur Radicals in Chemistry and Medicine, A. Breccia, M. A. J. Rodgers, G. Semerano. Lo Scarabeo Press, Bologna 1986; 47–52
   Google Scholar
• Gutteridge J. M. C., Beard A. P. C., Quinlan G. J. Catalase enhances damage to DNA by bleomycin-iron(II): the role of hydroxyl radicals. Biochemistry International 1985; 10: 441–449
   PubMedGoogle Scholar
• Halliwell B. Superoxide-dependent formation of hydroxyl radicals in the presence of iron chelates. Is it a mechanism for hydroxyl radical production in biochemical systems?. FEBS Letters 1978; 92: 321–326
   PubMed Web of Science ®Google Scholar
• Halliwell B., Gutteridge J. M. C. Formation of a thiobarbituric-acid-reactive substance from deoxyribose in the presence of iron salts. FEBS Letters 1981; 128: 347–352
   PubMed Web of Science ®Google Scholar
• Halliwell B., Gutteridge J. M. C. The importance of free radicals and catalytic metal ions in human diseases. Molecular Aspects of Medicine 1985; 8: 89–193
   PubMed Web of Science ®Google Scholar
• Halliwell B., Gutteridge J. M. C. Oxygen free radicals and iron in relation to biology and medicine; some problems and concepts. Archives of Biochemistry and Biophysics 1986; 246: 501–514
   PubMed Web of Science ®Google Scholar
• Halliwell B., Gutteridge J. M. C., Blake D. Metal ions and oxygen radical reactions in human inflammatory joint disease. Philosophical Transactions of the Royal Society of London, series B 1985; 311: 659–671
   PubMed Web of Science ®Google Scholar
• Halliwell B., Gutteridge J. M. C., Aruoma O. I. The deoxyribose method: a simple -test tube’ assay for determination of rate constants for reactions of hydroxyl radicals. Analytical Biochemistry 1987; 165: 215–219
   PubMed Web of Science ®Google Scholar
• Halliwell B., Gutteridge J. M. C., Grootveld M. Methods for the measurement of hydroxyl radicals in biochemical systems. Deoxyribose degradation and aromatic hydroxylation. Methods of Biochemical Analysis 1988, accepted for publication
   PubMedGoogle Scholar
• Hicks M., Gebicki J. M. Rate constants for reaction of hydroxyl radicals with Tris, Tricine and Hepes buffers. FEBS Letters 1986; 199: 92–94
   Web of Science ®Google Scholar
• Hiller K. O., Hodd P. L., Willson R. L. Antiinflammatory drugs: protection of a bacterial virus as an in vitro biological measure of free radical activity. Chemico-Biological Interactions 1983; 47: 293–305
   PubMed Web of Science ®Google Scholar
• Hirst N. P., French J. K., Bell A. L., Nuki G., O'Donnell M. L., Betts W. H., Cleland L. G. Differential effects of mepacrine, chloroquine and hydroxychloroquine on superoxide anion generation, phospholipid methylation and arachidonic acid release by human blood monocytes. Biochemical Pharmacology 1986; 35: 3083–3089
   PubMed Web of Science ®Google Scholar
• Martin R. B. Citrate binding of A13+ and Fe3+. Journal of Inorganic Biochemistry 1986; 28: 181–187
   PubMed Web of Science ®Google Scholar
• Filho Mello A. C., Meneghini R. In vivo formation of single-strand breaks in DNA by hydrogen peroxide is mediated by the Haber-Weiss reaction. Biochimica et Biophysica Acta 1984; 781: 56–63
   PubMedGoogle Scholar
• Moorhouse C. P., Halliwell B., Grootveld M., Gutteridge J. M. C. Cobalt(II) ion as a promoter of hydroxyl radical and possible -crypto-hydroxyl’ radical formation under physiological conditions. Differential effects of hydroxyl radical scavengers. Biochimica Biophysica Acta 1985; 843: 261–268
   PubMed Web of Science ®Google Scholar
• Muller-Peddinghaus R., Wurl M. The amplified chemiluminescence test to characterize antirheumatic drugs as oxygen radical scavengers. Biochemical Pharmacology 1987; 36: 1125–1132
   PubMed Web of Science ®Google Scholar
• Oyanagui Y. Inhibition of superoxide anion production in non-stimulated guinea pig peritoneal exudate cells by anti-inflammatory drugs. Biochemical Pharmacology 1978; 27: 777–782
   PubMed Web of Science ®Google Scholar
• Sausville E. A., Peisach J., Horwitz S. B. Effect of chelating agents and metal ions on the degradation of DNA by bleomycin. Biochemistry 1978; 17: 2740–2745
   PubMed Web of Science ®Google Scholar
• Schraufstatter I. U., Hinshaw D. B., Hyslop P. A., Spragg R. G., Cochrane C. G. Oxidant injury of cells. DNA strand-breaks activate polyadenosine diphosphate-ribose polymerase and lead to depletion of nicotinamide adenine dinucleotide. Journal of Clinical Investigation 1986; 77: 1312–1320
   PubMed Web of Science ®Google Scholar
• Wasil M., Halliwell B., Moorhouse C. P., Hutchison D. C. S., Baum H. Biologically-significant scavenging of the myeloperoxidase-derived oxidant hypochlorous acid by some anti-inflammatory drugs. Biochemical Pharmacology 1987; 36: 3847–3850
   PubMed Web of Science ®Google Scholar
• Weiss S. J. Oxygen, ischemia and inflammation. Acta Physiologica Scandinavica 1986; 548: 9–37, supplement
   Google Scholar
• Winterbourn C. C., Sutton H. C. Iron and xanthine oxidase catalyse formation of an oxidant species distinguishable from OH: comparison with the Haber-Weiss reaction. Archives of Biochemistry and Biophysics 1986; 244: 27–34
   PubMed Web of Science ®Google Scholar