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Original Article

Protoporphyrin IX and oxidative stress

, &
Pages 161-170 | Received 01 Dec 1998, Published online: 07 Jul 2009

References

  • Moore M.R., McColl K.E.L., Rimington C., Goldberg A. Disorders of Porphyrin Metabolism. Plenum Publishing Corporation, London, New YorkUK, USA 1987
  • Didier S., Boboc B., Bernuau J., Bismuth H., Benhamou J.P. Liver transplantation for protoporphyria: Evidence for the predominant role of the erythropoietic tissue in protoporphyrin overproduction. Gastroenterology 1988; 95: 816–819
  • Morehouse K.M., Moreno S.N.J., Mason R.P. The one-electron reduction of uroporphyrin I by rat hepatic microsomes. Archives of Biochemistry and Biophysics 1987; 257: 276–284
  • van Steveninck, J., Boegheim, J.P.J., Dubbelman, T.M.A.R., et al. The mechanism of potentiation of horseradish peroxidase-catalyzed oxidation of NADPH by porphyrins. Biochemical Journal 1987; 242: 611–613
  • van Steveninck, J., Boegheim, J.P.J., Dubbelman, T.M.A.R., et al. The influence of porphyrins on iron-catalysed generation of hydroxyl radicals. Biochemical Journal 1988; 250: 197–201
  • Comporti M. Lipid peroxidation and cellular damage in toxic liver injury. Laboratory Investigation 1985; 53: 599–623
  • Tribble D.L., Tak Y.A., Jones D.P. The pathophysiological significance of lipid peroxidative cell injury. Hepatology 1987; 7: 377–387
  • Marver H., Tschudy D., Perlroth M., Collins A. δ-aminolevulinic acid synthetase I. Studies in liver homogenates. Journal of Biological Chemistry 1966; 241: 2803–2809
  • Batlle A., Ferramola A.M., Grinstein M. Purification and general properties of δ-aminolevulinate dehydratase from cow liver. Biochemical Journal 1967; 104: 244–249
  • Batlle A., Wider de Xifra E., Stella A.M. A simple method for measuring erythrocyte porphobilinogenase and its use in the diagnosis of acute intermittent porphyria. International Journal of Biochemistry 1978; 9: 871–875
  • Chance B., Maehly A. Asssay of catalases and peroxidases. Methods in Enzymology, B. Chance, A. Maehly. Acad. Press N.Y. 1955; II: 764–768, In
  • Pinto R., Bartley W. The effect of age and sex on glutathione peroxidase activities and on aerobic glutathione oxidation in rat liver homogenates. Biochemical Journal 1969; 112: 109–115
  • Paglia D.E., Valentine W.N. Studies on the quantitative and qualitative characterization of erythrocyte glutathione peroxidase. Journal of Laboratory and Clinical Medicine 1967; 70: 158–169
  • Paoletti F., Aldinucci D., Mocali A., Caparrini A. A sensitive spectrophotometric method for the determination of superoxide dismutase activity in tissue extracts. Analytical Biochemistry 1986; 154: 536–541
  • Habig W., Pabst M., Jakoby W. Glutathione-S-Transferase. The first enzymatic step in mercapturic acid formation. Journal of Biological Chemistry 1974; 249: 7130–7139
  • Rossi R., Cardaioli E., Scaloni A., Amiconi G., Di Simplicio P. Thiol groups in proteins as endogenous reductants to determine glutathione protein mixed disulphides in biological systems. Biochimica et Biophysica Acta 1995; 1243: 230–238
  • Niehaus W., Samuelson D. Formation of malondialdehyde from phospholipids arachidonate during microsomal lipid peroxidation. European Journal of Biochemistry 1968; 6: 126–130
  • Polo C., Frisardi A., Resnik E., Schoua A.E., Batlle A. Factors influencing fluorescence spectra of free porphyrins. Clinical Chemistry 1988; 34: 757–760
  • Polo C., Afonso S., Batlle A. Un método simplificado para la determinación y la extracción de esteres metílicos de porfirinas. Acta Bioquímica Clínica Latinoamericana 1988; XXII: 439–441
  • Rimington C., Sveinson S. The spectrophotometric determination of uroporphyrin. Scandinavian Journal of Clinical and Laboratory Investigation 1950; 2: 209–216
  • Lowry O., Rosebrough N., Farr A., Randall R. Protein measurement with the Folin-phenol reagent. Journal of Biochemistry 1951; 193: 265–275
  • Lamola A.A., Asher I., Muller-Eberhard U., Poh-Fitzpatrick M.B. Fluorometric study of the binding of protoporphyrin to haemopexin and albumin. Biochemical Journal 1981; 196: 693–698
  • Sandberg S., Brun A. Light-induced protoporphyrin release from erythrocytes in erythropoietic protoporphyria. Journal of Clinical Investigation 1982; 70: 693–697
  • Brun A., Sandberg S. Photodynamic release of protoporphyrin from intact erythrocytes in erythropoietic protoporphyria. The effect of small repetitive light doses. Photochemistry and Photobiology 1985; 41: 535–541
  • Bloomer J.R. The liver in protoporphyria. Hepatology 1988; 8: 402–407
  • Wolfson S.J., Bartczak A., Bloomer J.R. Effect of endogenous heme generation on δ-aminolevulinic acid synthase activity in rat liver mitochondria. Journal of Biological Chemistry 1979; 254: 3543–3546
  • Halliwell B., Gutteridge J.M.C. Free Radicals in Biology and Medicine2nd edition. Clarendon Press, Oxford, UK 1989
  • Michiels C., Raes M., Toussaint O., Remacle J. Importance of glutathione peroxidase, catalase and Cu/Zn-SOD for cell survival against oxidative stress. Free Radicals, Biology and Medicine 1994; 17: 235–248
  • Sahu S.C., Gray G.C. Pro-oxidant activity of flavonoids effects on glutathione and glutathione S-transferase in isolated rat liver nuclei. Cancer Letters 1996; 104: 193–196
  • Sheen L.Y., Lii C.K., Sheu S.F., Meng R.H., Tsai S.J. Effect of the active principle of garlic (diallyl sulfide) on cell viability, detoxication capability and the antioxidation system of primary rat hepatocytes. Food and Chemical Toxicology 1996; 34: 971–972
  • Fridovich I. Superoxide dismutases. An adaptation to a paramagnetic gas. Journal of Biological Chemistry 1989; 264: 7761–7764
  • McCord J.M. Superoxide radical: controversies, contradictions, and paradoxes. Proceedings of the Society for Experimental Biology and Medicine 1995; 209: 112–117
  • Honda S., Matsuo M. Lack of recovery from oxygen-induced damage to colony formation and DNA synthesis in senescent human diploid fibroblasts. Mechanisms of Ageing and Development 1987; 40: 81–87
  • Martin W.J., Kachel D.L. Oxygen-mediated impairment of human pulmonary endothelial cell growth: Evidence for a specific threshold of toxicity. Journal of Laboratory and Clinical Medicine 1989; 113: 413–421
  • Michiels C., Raes M., Pigeolet E., Corbisier P., Lambert D., Remacle J. Importance of a threshold for error accumulation in cell degeneration processes. I. Modulation of the threshold in a model of free radial induced cell degeneration. Mechanisms of Ageing and Development 1990; 51: 41–54

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