Skip to main content
SpringerLink
Log in

Iron-Mediated Oxidative Stress and Erythrocytes

  • Chapter
Erythroid Cells

Part of the book series: Blood Cell Biochemistry ((BLBI,volume 1))

Abstract

Iron in its labile, chelatable form has been implicated in the generation of radical species such as the hydroxyl radical, ferryl species [an Fe(IV)-oxygen complex], perferryl (Fe2+ −O2 ↔ Fe3+ −O −2 ∙), and Fe2+ /Fe3+ /O2 complexes (for reviews see Halliwell and Gutteridge, 1986; Czapski and Goldstein, 1986; Aust and White, 1986; Aust and Minotti, 1987; Gutteridge and Halliwell, 1989) and in the propagation of oxidative events.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 169.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 219.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 219.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Aisen, P., 1977, Some physicochemical aspects of iron metabolism, CIBA Found. Symp. 51: 1–17.

    CAS  Google Scholar 

  • Ames, B. N., Cathcart, R., Schwiers, E., and Hochstein, P., 1981, Uric acid provides an antioxidant defence in humans against oxidant-and radical-caused aging and cancer: A hypothesis, Proc. Natl. Acad. Sci. USA 78: 6858–6862.

    Article  PubMed  CAS  Google Scholar 

  • Arden, G. B., Wonke, B., Kennedy, C., and Huehns, E. R., 1984, Ocular changes in patients undergoing longterm desferrioxamine treatment, Br. J. Ophthalmol. 68: 873–877.

    Article  PubMed  CAS  Google Scholar 

  • Aruoma, O., Halliwell, B., Laughton, M. J., Quinlan, G. J., and Gutteridge, J. M. C., 1989, The mechanism of initiation of lipid peroxidation. Evidence against a requirement for iron(II)—iron(III) complex, Biochem. J. 258: 617–620.

    PubMed  CAS  Google Scholar 

  • Asakura, T., Minakata, K., Adachi, K., Russell, M. O., and Schwartz, E., 1977, Denatured haemoglobin in sickle erythrocytes, J. Clin. Invest. 59: 633–640.

    Article  PubMed  CAS  Google Scholar 

  • Aust, S. D., and White, B. C., 1986, The role of iron in lipid peroxidation, in: Free Radicals, Cell Damage and Disease ( C. Rice-Evans, ed.), pp. 15–27, Richelieu Press, London.

    Google Scholar 

  • Aust, S. D. and Minotti, G., 1987, The role of iron in the inhibition of lipid peroxidation, Chem. and Physics of Lipids 44: 141–207.

    Google Scholar 

  • Bauminger, E. R., Cohen, S. G., Offer, S., Racmilewitz, E. A., 1979, Quantitative studies of ferritin-like iron in erythrocytes of thalassaemia, sickle cell anemia and haemoglobin Hammersmith by Mossbauer spectroscopy, Proc. Natl. Acad. Sci. USA 76: 939–943.

    Article  PubMed  CAS  Google Scholar 

  • Blake, D. R., Winyard, P., and Lunec, J., 1985, Cerebral and ocular toxicity induced by desferrioxamine, Q. J. Med. 219: 345–355.

    Google Scholar 

  • Brunori, M., Wyman, J., Antonini, E., and Rossi-Fanelli, A., 1965, Studies on the oxidation—reduction potentials of haem proteins, J. Biol. Chem. 240: 3317–3324.

    PubMed  CAS  Google Scholar 

  • Brunori, M., Falcioni, G., Fioreti, E., Giardina, B., and Rotilio, G., 1975, Formation of superoxide in the autoxidation of isolated a and ß chains of human haemoglobin and its involvement in haemichrome precipitation, Eur. J. Biochem. 53: 99–104.

    Article  CAS  Google Scholar 

  • Bunn, F., and Jandl, J., 1966, Exchange of haem among haemoglobin molecules, Proc. Natl. Acad. Sci. USA 56: 974–978.

    Article  PubMed  CAS  Google Scholar 

  • Butler, J., Hoey, B. M., Lea, J. S., 1988, The measurement of radicals by pulse radiolysis, in: Free Radicals, Methodology and Concepts ( C. Rice-Evans, and B. Halliwell, eds.), pp. 457–479, Richelieu Press, London.

    Google Scholar 

  • Bessis, M., 1983, Red cell shapes, in Red Cell Shape ( M. Bessis, R. I. Weed, P. F. Leblond, eds.), Springer, New York.

    Google Scholar 

  • Chidambaram, M. V., Barnes, G., and Frieden, E., 1983, Caeruloplasmin and the reactions forming diferric transferrin, FEBS Lett. 159: 137–140.

    Article  PubMed  CAS  Google Scholar 

  • Chiu, D., and Lubin, B., 1979, Abnormal vitamin E and glutathione peroxidase levels in sickle cell anaemia: Evidence for increased susceptibility to lipid peroxidation in vivo, J. Lab. Clin. Med. 94: 542–548.

    PubMed  CAS  Google Scholar 

  • Chiu, D., Lubin, B., and Shohet, S., 1982, Peroxidative reactions in red cell biology, in: Free Radicals in Biology ( W. A. Pryor, ed.), Volume V, pp. 115–160, Academic Press, New York.

    Google Scholar 

  • Chung, J., and Wood, J. L., 1971, Oxidation of thiocyanate to cyanide catalysed by haemoglobin, J. Biol. Chem. 246: 555–560.

    PubMed  CAS  Google Scholar 

  • Clark, M. R., Mohandas, N., and Shohet, S. B., 1980, The deformability of oxygenated irreversibly sickled cells, J. Clin. Invest. 65: 185–196.

    Article  Google Scholar 

  • Cohen, G., and Hochstein, P., 1963, Glutathione peroxidase, the primary agent for the elimination of hydrogen peroxide in erythrocytes, Biochemistry 2: 1420–1428.

    Article  PubMed  CAS  Google Scholar 

  • Czapski, G., and Goldstein, S., 1986, When do metal complexes protect biological systems from superoxide toxicity and when do they enhance it? Free Radical Res. Commun. 1: 157–161.

    Article  CAS  Google Scholar 

  • Darley-Usmar, V. M., Hersey, A., and Garland, L. G., 1989, A method for the comparative assessment of antioxidants as peroxyl radical scavengers, Biochem. Pharmacol. 38: 1465–1467.

    Article  PubMed  CAS  Google Scholar 

  • Das, S. K., and Nair, R. C., 1980, Superoxide dismutase, glutathione peroxidase, catalase and lipid peroxidation of normal and sickled erythrocytes, Br. J. Haematol. 44: 87–92.

    Article  PubMed  CAS  Google Scholar 

  • Davies, K. J. A., and Goldberg, A. L., 1987, Oxygen radicals stimulate intracellular proteolysis and lipid peroxidation by independent mechanisms in erythrocytes, J. Biol. Chem. 262: 8220–8226.

    PubMed  CAS  Google Scholar 

  • Davies, K. J. A., Sevanian, A., Mukkassah-Kelly, S. F., and Hochstein, P., 1986, Uric acid—iron ion complexes, Biochem. J. 235: 747–754.

    PubMed  CAS  Google Scholar 

  • Davies, M. J., and Slater, T. F., 1987, Studies on the metal ion and lipoxygenase-catalysed breakdown of hydroepoxides using electron spin resonance spectroscopy, Biochem J. 245: 167–173.

    PubMed  CAS  Google Scholar 

  • Davies, M. J., Donkor, R. E., Dunster, A., Gee, C. A., Jonas, S., and Willson, R. L., 1987, Desferrioxamine and superoxide free radicals: Formation of an enzyme-damaging nitroxide, Biochem. J. 246: 725–729.

    PubMed  CAS  Google Scholar 

  • Davies, S. C., Marcus, R. E., Hungerford, J. L., Miller, M. H., Arden, G. B., and Huehns, E. R., 1983, Ocular toxicity of high dose intravenous desferrioxamine, Lancet 2: 181–184.

    Article  PubMed  CAS  Google Scholar 

  • Diplock, A. T., 1983, The role of vitamin E in biological membranes, CIBA Found. Symp. 101: 45–53.

    CAS  Google Scholar 

  • Doly, M., Bonhomme, B., and Vennat, J. C., 1986, Experimental study of the retinal toxicity of haemoglobin iron, Ophthalmic Res. 18: 21–27.

    Article  PubMed  CAS  Google Scholar 

  • Eaton, J. W., Skelton, T. O., Swofford, H. S., Kaplin, C. E., and Jacobs, H. S., 1974, Elevated calcium in sickle cell disease, Nature 246: 105–106.

    Article  Google Scholar 

  • Esterbauer, H., 1985, Lipid peroxidation products: Formation, chemical properties and biological activities, in: Free Radicals in Liver Injury ( G. Poli, K. Cheeseman, M. U. Dianzani, and T. F. Slater, eds.), pp. 29–47, IRL Press, Oxford, England.

    Google Scholar 

  • Eylar, E. H., and Matioli, G., 1965, Apoferritin synthesis in human erythroid cells in thalassaemia, Nature 208: 661–664.

    Article  CAS  Google Scholar 

  • Fischer, S., Nagel, R. L., Bookchin, R. M., Roth, E. F., and Tellez-Nagel, I., 1975, The binding of haemoglobin to membranes of normal and sickle erythrocytes, Biochim. Biophys. Acta 375: 422–433.

    Article  PubMed  CAS  Google Scholar 

  • Fortier, N. L., Snyder, L. M., Ganver, F., Kiefer, C., McKenney, J., and Mohandas, N., 1988, The relationship between in vivo generated haemoglobin skeletal protein complex and increased cell and membrane rigidity, Blood 71: 1427–1431.

    PubMed  CAS  Google Scholar 

  • George, P., and Irvine, D. H., 1952, The interaction between metmyoglobin and hydrogen peroxide, Biochem. J. 52: 511–515.

    PubMed  CAS  Google Scholar 

  • Girotti, A. W., 1985, Mechanism of lipid peroxidation, J. Free Radical Biol. Med. 1: 87–95.

    Article  CAS  Google Scholar 

  • Goldberg, B., Stern, A., and Peisach, J., 1976, The mechanism of superoxide generation by the interaction of phenylhydrazine with haemoglobin, J. Biol. Chem. 251: 3045–3051.

    PubMed  CAS  Google Scholar 

  • Griffiths, H., Unsworth, J., Blake, D. R., and Lunec, J., 1988, Oxidation of amino acids within serum proteins, in: Free Radicals, Chemistry, Pathology and Medicine (C. Rice-Evans and T. Dormandy, eds.), pp. 439454, Richelieu Press, London.

    Google Scholar 

  • Guerini, A., London, G., Marchais, S., Metivier, F., and Relisse, J. M., 1985, Acute deafness and desferrioxamine, Lancet 2: 39–40.

    Article  Google Scholar 

  • Gutteridge, J. M. C., 1986, Iron promoters of the Fenton reaction and lipid peroxidation can be released from haemoglobin by peroxides, FEBS Lett. 201: 291–295.

    Article  PubMed  CAS  Google Scholar 

  • Gutteridge, J. M. C., 1987, The antioxidant activity of haptoglobin towards haemoglobin-stimulated lipid peroxidation, Biochim. Biophys. Acta 917: 219–223.

    Article  PubMed  CAS  Google Scholar 

  • Gutteridge, J. M. C., and Halliwell, B., 1989, Iron toxicity and oxygen radicals, Bailliere’s Clin. Haematol. 2: 195–256.

    Article  PubMed  CAS  Google Scholar 

  • Halliwell, B., and Gutteridge, J. M. C., 1984, Oxygen toxicity, oxygen radicals, transition metals and disease, Biochem. J. 219: 1–14.

    PubMed  CAS  Google Scholar 

  • Halliwell, B., and Gutteridge, J. M. C., 1986, Oxygen free radicals and iron in relation to biology and medicine. Some problems and concepts, Arch. Biochem. Biophys. 246: 501–514.

    Article  PubMed  CAS  Google Scholar 

  • Hartley, A., and Rice-Evans, C., 1989a, Membrane-associated iron species and membrane oxidation in sickle cell disease, Biochem. Soc. Trans. 17: 116–118.

    CAS  Google Scholar 

  • Hartley, A., and Rice-Evans, C., 1989b, The nature of membrane-bound iron species involved in radical-mediated damage to sickle erythrocytes, Biochem. Soc. Trans. 17: 488–489.

    CAS  Google Scholar 

  • Hartley, A., Davies, M. J., and Rice-Evans, C., 1990, Desferrioxamine as a lipid chain-breaking antioxidant in sickle erythrocyte membranes, FEBS Lett (in press).

    Google Scholar 

  • Hebbel, R. P., Yamada, O., Moldow, C. F., Jacob, H. S., White, J. G., and Eaton, J. W., 1980, Abnormal adherence of sickle erythrocytes to cultured vascular endothelium. Possible mechanisms for microvascular occlusion in sickle cell disease, J. Clin. Invest. 65: 154–158.

    Article  PubMed  CAS  Google Scholar 

  • Hebbel, R. P., Eaton, J. W., Balasingham, M., Steinberg, M. H., 1982, Spontaneous oxygen radical generation by sickle erythrocytes, J. Clin. Invest. 70: 1253–1259.

    Article  PubMed  CAS  Google Scholar 

  • Hershko, C., Graham, G., Bates, G. W., and Rachmilewitz, E. A., 1978, Nonspecific serum iron in thalassaemia: An abnormal serum iron fraction of potential toxicity, Br. J. Haematol. 49: 255–263.

    Article  Google Scholar 

  • Hochstein, P., Jain, S. K., and Rice-Evans, C., 1981, The physiological significance of oxidative perturbations in erythrocyte membrane lipids and proteins, in: The Red Cell ( G. Brewer, ed.), pp. 449–459, Liss, New York.

    Google Scholar 

  • Jackson, M. E., Brenton, D. P., and Modell, B., 1983, DTPA in management of iron overload in thalassaemia, J. Inher. Metab. Dis. 6: 97–98.

    Article  Google Scholar 

  • Jacobs, A., 1977, Low molecular weight intracellular iron transport compounds, Blood 50: 433–439.

    PubMed  CAS  Google Scholar 

  • Kahane, I., and Rachmilewitz, E. A., 1976, Alteration of the red blood cell membrane and the effect of vitamin E on osmotic fragility in thalassaemia major, Jar. J. Med. Sci. 12: 11–15.

    CAS  Google Scholar 

  • Kappus, H., 1985, Lipid peroxidation: Mechanisms, analysis, enzymology and biological relevance, in: Oxidative Stress ( H. Sies, ed.), pp. 273–310, Academic Press, New York.

    Google Scholar 

  • Keberle, H., 1964, The biochemistry of desferrioxamine and its relation to iron metabolism, Ann. N.Y. Acad. Sci. 119: 758–768.

    Article  PubMed  CAS  Google Scholar 

  • Kim, H. C., Friedman, S., Asakura, T., and Schwartz, E., 1980, Inclusions in red blood cells containing HbS or HbC, Br. J. Haematol. 44: 547–554.

    Article  PubMed  CAS  Google Scholar 

  • Kuross, S. A., and Hebbel, R. P., 1988, Nonhaem iron in sickle erythrocyte membranes: Association with phospholipids and potential role in lipid peroxidation, Blood 72: 1278–1285.

    PubMed  CAS  Google Scholar 

  • Kuross, S. A., Rank, B. H., and Hebbel, R. P., 1988, Excess haem in sickle erythrocyte inside-out membranes: Possible role in thiol oxidation, Blood 71: 876–882.

    PubMed  CAS  Google Scholar 

  • Labeque, R., and Mainett, L., 1988, Reaction of haematin with allylic fatty acid hydroepoxides, Biochemistry 27: 7060–7070.

    Article  PubMed  CAS  Google Scholar 

  • Lessin, L. S., Kuranstin-Mills, J., Wallas, C., and Weems, H., 1978, Membrane alterations in irreversibly sickled cells: Haemoglobin—membrane interactions, J. Supramol. Struct. 9: 537–543.

    Article  PubMed  CAS  Google Scholar 

  • Levine, R. L., Oliver, C. N., Fulks, R. M., and Stadtman, E. R., 1981, Turnover of bacterial glutamate synthetase: Oxidative inactivation precedes proteolysis, Proc. Natl. Acad. Sci. USA 78: 2120–2124.

    Article  PubMed  CAS  Google Scholar 

  • Liu, S. C., Zhai, S., and Palek, J., 1988, Detection of haemin release during haemoglobin S denaturation, Blood 71: 1755–1758.

    PubMed  CAS  Google Scholar 

  • Lubin, B., Chiu, D., Bastacky, J., Roelofsen, B., and Van Deenen, L. L. M., 1981, Abnormalities in the membrane phospholipid organisation in sickled erythrocytes, J. Clin. Invest. 67: 1643–1649.

    Article  PubMed  CAS  Google Scholar 

  • Lux, S. E., John, K. M., and Karnovsky, M. J., 1976, Irreversible deformation of the spectrin—actin lattice in irreversibly sickled cells, J. Clin. Invest. 58: 955–963.

    Article  PubMed  CAS  Google Scholar 

  • McCord, J. M., and Fridovich, I., 1969, Superoxide dismutase an enzymic function for erythrocuprein (haemocuprein), J. Biol. Chem. 244: 6049–6055.

    PubMed  CAS  Google Scholar 

  • Marklund, S. L., 1984, Extracellular superoxide dismutase and other superoxide dismutase isoenzymes in tissues from nine mammalian species, Biochem. J. 222: 649–655.

    PubMed  CAS  Google Scholar 

  • Minotti, G., and Aust, S. D., 1987a, Role of iron in the initiation of lipid peroxidation, Chem. Phys. Lipids 44: 191–208.

    Article  PubMed  CAS  Google Scholar 

  • Minotti, G., and Aust, S. D., 1987b, The requirement for iron (IV) in the initiation of lipid peroxidation by iron (II) and hydrogen peroxide, J. Biol. Chem. 262: 1098–1104.

    PubMed  CAS  Google Scholar 

  • Misra, H. P., and Fridovich, I., 1972, The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase, J. Biol. Chem. 247: 3170–3175.

    PubMed  CAS  Google Scholar 

  • Modell, B., and Berdoukas, V., 1984, The Clinical Approach to Thalassaemia, Grune and Stratton, New York.

    Google Scholar 

  • Morehouse, K. M., Flitter, W. D., and Mason, R. P., 1987, The enzymatic oxidation of desferal to a nitroxide radical, FEBS Lett. 222: 246–250.

    Article  PubMed  CAS  Google Scholar 

  • Moser, U., 1987, Uptake of ascorbic acid by leukocytes, Ann. N.Y. Acad. Sci. 498: 200–215.

    Article  PubMed  CAS  Google Scholar 

  • O’Brien, P. J., 1969, Intracellular mechanisms for the decomposition of a lipid hydroperoxide, Can. J. Biochem. 47: 485–492.

    Article  PubMed  Google Scholar 

  • Osaki, S., Johnson, D. A., and Frieden, E., 1966, Possible significance of the ferrous oxidase activity of caeruloplasmin in normal human serum, J. Biol. Chem. 241: 2746–2751.

    PubMed  CAS  Google Scholar 

  • Palek, J., 1977, Red cell membrane injury in sickle cell anaemia, Br. J. Haematol. 35: 1–9.

    Article  PubMed  CAS  Google Scholar 

  • Panter, S. S., Sadrzadeh, S. M., Hallaway, P. E., Haines, J. L., Anderson, V. E., and Eaton, J. W., 1985, Hypohaptoglobinaemia associated with familial epilepsy, J. Exp. Med. 161: 748–754.

    Article  PubMed  CAS  Google Scholar 

  • Pearson, H. A., and O’Brien, R. T., 1975, The management of thalassaemia major, Semin. Haematol. 12: 255–265.

    CAS  Google Scholar 

  • Peisach, J., Blumberg, W. E., Wittenberg, B. A., and Wittenberg, J. B., 1968, The electronic structure of protohaem proteins. III. The configuration of the haem and its ligands, J. Biol. Chem. 243: 1871–1880.

    PubMed  CAS  Google Scholar 

  • Peisach, J., Blumberg, W. E., and Rachmilewitz, E. A., 1975, The demonstration of ferrihaemochrome intermediates in Heinz body formation following the oxidation of oxyhaemoglobin by acetylphenylhydrazinc, Biochem. Biophys. Acta 393: 404–418.

    Article  PubMed  CAS  Google Scholar 

  • Perutz, M., 1989, Myoglobin and haemoglobin: Role of distal residues in reactions with haem ligands, Trends Biochem. Sci. 14: 42–44.

    Article  PubMed  CAS  Google Scholar 

  • Petersen, R. I., Symons, M. C. R., and Taiwo, F. A., 1989, Application of irradiation and ESR spectroscopy to the study of ferryl haemoglobin and myoglobin, J. Chem. Soc. Faraday Trans. 85: 2435–2443.

    Article  CAS  Google Scholar 

  • Platt, O. S., Falcone, J. F., and Lux, S. E., 1985, Molecular defect in the sickle erythrocyte cytoskeleton. Abnormal spectrin binding to sickle inside-out vesicles, J. Clin. Invest. 75: 266–271.

    Article  PubMed  CAS  Google Scholar 

  • Poli, G., Ramenghi, U., David, O., Biasi, F., Cecchini, G., Carini, R., Chiarpotto, E., and Dianzani, M. U., 1986, Lipid peroxidation in red blood cells obtained from thalassaemic subjects and exposed to oxidative stress, in: Free Radicals, Cell Damage and Disease ( C. Rice-Evans, ed.), pp. 449–459, Richelieu Press, London.

    Google Scholar 

  • Polliack, A., and Rachmilewitz, E. A., 1973, Ultrastructural studies in thalassaemia major, Br. J. Haematol. 24: 319–326.

    Article  PubMed  CAS  Google Scholar 

  • Polliack, A., Yataganas, X., Thorell, B., and Rachmilewitz, E. A., 1974, An electron microscopic study of the nuclear abnormalities in erythroblasts in beta-thalassaemia major, Br. J. Haematol. 26: 201–204.

    Article  PubMed  CAS  Google Scholar 

  • Puppo, A., and Halliwell, B., 1988, Formation of hydroxyl radicals from hydrogen peroxide in the presence of iron: Is haemoglobin a biological Fenton reagent? Biochem. J. 249: 185–190.

    PubMed  CAS  Google Scholar 

  • Rachmilewitz, E. A., 1985, Erythrocyte membrane alterations in beta-thalassaemia, Clin. Haematol. 14: 163–182.

    PubMed  CAS  Google Scholar 

  • Rachmilewitz, E. A., Peisach, J., and Blumberg, W. E., 1971, Studies on the stability of oxyhaemoglobin A and its constituent chains and their derivatives, J. Biol. Chem. 246: 3356–3366.

    PubMed  CAS  Google Scholar 

  • Rachmilewitz, E. A., Lubin, B. H., and Shohet, S. B., 1976, Lipid membrane peroxidation in betathalassaemia major, Blood 47: 495–505.

    PubMed  CAS  Google Scholar 

  • Rank, B. H., Carlsson, J., and Hebbel, R. P., 1985, Abnormal redox status of membrane: Protein thiols in sickle erythrocytes, J. Clin. Invest. 75: 1531–1537.

    Article  PubMed  CAS  Google Scholar 

  • Rice-Evans, C., 1987, Oxidative modifications in erythrocytes induced by iron, in: Free Radicals, Oxidant Stress and Drug Action ( C. Rice-Evans, ed.), pp. 307–330, Richelieu Press, London.

    Google Scholar 

  • Rice-Evans, C., 1989, Iron chelators and the suppression of oxidative damage in erythrocytes: Extracellular and intracellular responses, in: Free Radicals, Metal Ions and Biopolymers ( P. Beaumont, D. Deeble, B. Parsons, and C. Rice-Evans, eds.), pp. 283–301, Richelieu Press, London.

    Google Scholar 

  • Rice-Evans, C., 1990, Decompartmentalised, microbleeding and membrane oxidation, in: Free Radicals, Lipoproteins and Membrane Lipids (A. Crastes de Paulet, L. Douste Blazy, and R. Paoletti, eds.), in press.

    Google Scholar 

  • Rice-Evans, C., and Baysal, E., 1987a, Role of membrane-bound haemoglobin products in oxidative damage in sickle cell membranes, Acta Haematol. 78: 105–108.

    Article  PubMed  CAS  Google Scholar 

  • Rice-Evans, C., and Baysal, E., 1987b, Iron-mediated oxidative stress in erythrocytes, Biochem. J. 244: 19 1196.

    Google Scholar 

  • Rice-Evans, C., and Chapman, D., 1981, Red blood cell biomembrane structure and deformability, Scand. J. Clin. Lab. Invest. 156: 99–110.

    Article  CAS  Google Scholar 

  • Rice-Evans, C., and Dunn, M. J., 1982, Erythrocyte deformability and disease, Trends Biochem. Sci. 7: 282–286.

    Article  CAS  Google Scholar 

  • Rice-Evans, C., and Hartley, A., 1989, Free radicals erythrocyte disorders and iron decompartmentalisation, in: Medical, Biochemical and Chemical Aspects of Free Radicals ( O. Hayaishi, E. Niki, M. Kondo, and T. Yoshikawa, eds.), Elsevier, Amsterdam, pp. 1185–1194.

    Google Scholar 

  • Rice-Evans, C., and Omorphos, S., 1983, Hydrazine and sickle cells, Biochem. Soc. Trans. 11: 180–181.

    CAS  Google Scholar 

  • Rice-Evans, C., and Omorphos, S. C., 1986, Free radical-induced membrane damage in sickle erythrocytes, in: Approaches to the Therapy of Sickle Cell Anaemia ( Y. Beuzard, S. Charache, and F. Galacteros, eds.), pp. 329–336, INSERM, Paris.

    Google Scholar 

  • Rice-Evans, C., Bruckdorfer, K. R., and Dootson, G., 1978, Studies on the altered membrane characteristics of sickle cells, FEBS Lett. 94: 81–86.

    Article  PubMed  CAS  Google Scholar 

  • Rice-Evans, C., Johnson, A., and Flynn, D. M., 1980, Red cell membrane abnormalities in beta-thalassaemia major, FEBS Lett. 119: 53–57.

    Article  PubMed  CAS  Google Scholar 

  • Rice-Evans, C., Omorphos, S., and White, J. M., 1982, The effects of hydrazine on sickle cells, Biochim. Biophys. Acta 691: 367–371.

    Article  PubMed  CAS  Google Scholar 

  • Rice-Evans, C., Baysal, E., Flynn, D., and Kontoghiorghes, G., 1986a, Iron-mediated free radical effects on erythrocytes: The role of desferrioxamine, Biochem. Soc. Trans. 14: 368–369.

    CAS  Google Scholar 

  • Rice-Evans, C., Baysal, E., Flynn, D., and Kontoghiorghes, G., 1986b, The effects of desferrioxamine and ascorbate on haemoglobin from thalassaemic erythrocytes, in: Superoxide and Superoxide Dismutase in Chemistry, Pathology and Medicine ( G. Rotilio, ed.), pp. 662–666, Elsevier, Amsterdam.

    Google Scholar 

  • Rice-Evans, C., Omorphos, S. C., and Baysal, E., 1986c, Sickle cell membranes and oxidative damage, Biochem. J. 237: 265–269.

    PubMed  CAS  Google Scholar 

  • Rice-Evans, C., Omorphos, S. C., and Baysal, E., 1986d, Sickle cell pathology: Is the membrane important? in: Free Radicals, Cell Damage and Disease (C. Rice-Evans, ed.), pp. 149–166

    Google Scholar 

  • Richelieu Press, London. Rice-Evans, C., Okunade, G., and Khan, R., 1989, The suppression of iron release from activated myoglobin by physiological electron donors and by desferrioxamine, Free Radical Res. Commun. 7: 45–54.

    Google Scholar 

  • Risdon, R. A., Barry, M., and Flynn, D., 1975, Transfusional iron overload: Hepatic fibrosis in thalassaemia, J. Pathol. 116: 83–95.

    Article  CAS  Google Scholar 

  • Romeo, M. A., DiGregorio, F., and Schiliro, G., 1984, Allergy to desferrioxamine, J. Inher. Metab. Dis. 7: 121–124.

    Article  PubMed  CAS  Google Scholar 

  • Roshchupkin, D. I., Talitsky, V. V., and Peleritsyn, A. N., 1979, Fluorescence study of tryptophan photolysis, Photochem. Photobiol. 30: 635–641.

    Article  CAS  Google Scholar 

  • Rowland, I., and Symons, M. C. R., 1988, Tumours and iron: The use of electron spin resonance, in: Free Radicals, Methodology and Concepts ( C. Rice-Evans and B. Halliwell, eds.), pp. 169–184, Richelieu Press, London.

    Google Scholar 

  • Rowley, D. A., and Halliwell, B., 1982a, Superoxide-dependent formation of hydroxyl radicals in the presence of thiol compounds, FEBS Leu. 138: 33–36.

    Article  CAS  Google Scholar 

  • Rowley, D. A., and Halliwell, B., 1982b, Superoxide-dependent formation of hydroxyl radicals from NADH and NADPH in the presence of iron salts, FEBS Lett. 142: 39–41.

    Article  PubMed  CAS  Google Scholar 

  • Rowley, D. A., and Halliwell, B., 1983, Formation of hydroxyl radicals from hydrogen peroxide and iron salts by superoxide-and ascorbate-dependent mechanisms: Relevance to the pathology of rheumatoid disease, Clin. Sci. 64: 649–653.

    PubMed  CAS  Google Scholar 

  • Schwartz, R., Rybicki, A. C., Heath, R. H., and Lubin, B. H., 1987, Protein 4.1 in sickle erythrocytes, J. Biol. Chem. 262: 15666–15672.

    PubMed  CAS  Google Scholar 

  • Searle, A., and Tomasi, A., 1982, Hydroxyl free radical production in iron-cysteine solutions and protection by zinc, J. lnorg. Chem. 17: 161–166.

    CAS  Google Scholar 

  • Shaklai, N., Sharma, V. S., and Ranney, H. M., 1981, Interaction of sickle cell haemoglobin with erythrocyte membranes, Proc. Natl. Acad. Sci. USA 78: 65–68.

    Article  PubMed  CAS  Google Scholar 

  • Shaklai, N., Shviro, Y., Rabizadeh, E., and Kirscher-Zilbe, I., 1985, Accumulation and drainage of haemin in the red cell membrane, Biochim. Biophys. Acta 821: 355–356.

    Article  PubMed  CAS  Google Scholar 

  • Sies, H., 1986, Biochemistry of oxidative stress, Angew. Chem. Int. Ed. Engl. 25: 1058–1071.

    Article  Google Scholar 

  • Singh, A., Koroll, G. W., and Cundall, R. B., 1982, Pulse radiolysis of aqueous solutions of sodium azide: Reactions of azide radical, tryptophan and tyrosine, Radiat. Phys. Chem. 19: 137–146.

    CAS  Google Scholar 

  • Snyder, L. M., Fortier, N. L., Leb, L., McKenney, J., Trainor, J., Sheerin, H., and Mohandas, N., 1988, The role of membrane protein sulphydryl groups in hydrogen peroxide-mediated membrane damage in human erythrocytes, Biochim. Biophys. Acta 937: 229–240.

    Article  PubMed  CAS  Google Scholar 

  • Stocks, J., Offerman, E. L., Modell, C. B., and Dormandy, T. L., 1972, The susceptibility to autoxidation of human red cell lipids in health and disease, Br. J. Haematol. 23: 713–724.

    Article  PubMed  CAS  Google Scholar 

  • Tappel, A. L., 1962, Vitamin E as the biological lipid antioxidant, Vitam. Horm. (N.Y.) 20: 493–510.

    Article  CAS  Google Scholar 

  • Tappel, A. L., 1980, Measurement of and protection from in vivo lipid peroxidation, in: Free Radicals in Biology ( W. A. Pryor, ed.), Volume IV, pp. 1–45, Academic Press, New York.

    Google Scholar 

  • Tillman, W., and Schroter, W., 1979, Rheological properties of erythrocytes in homozygous and heterozygous thalassaemia, Br.J. Haematol. 41: 401–411.

    Article  Google Scholar 

  • Waugh, S. M., Willardson, B. M., Kannan, R., Labotka, R. J., and Low, P. S., 1986, Heinz bodies induce clustering of band 3, glycophorin and ankyrin in sickle cell erythrocytes, J. Clin. Invest. 78: 1155–1160.

    Article  PubMed  CAS  Google Scholar 

  • Weiss, J., 1964, The nature of iron bound in oxyhaemoglobin, Nature 202: 83–84.

    Article  PubMed  CAS  Google Scholar 

  • Whitburn, K., 1987, The interaction of oxymyoglobin with hydrogen peroxide: The formation of ferryl myo-globin at moderate excess of hydrogen peroxide, Arch. Biochem. Biophys. 253: 419–430.

    Article  PubMed  CAS  Google Scholar 

  • White, J. G., 1974, Ultrastructural features of erythrocyte and haemoglobin sickling, Arch. Intern. Med. 133: 545–562.

    Article  PubMed  CAS  Google Scholar 

  • Williams, D. R., 1971, The Metals of Life, Van Nostrand—Rheinhold, Princeton, N.J.

    Google Scholar 

  • Winterboum, C. C., 1979, Comparison of superoxide with other reducing agents in the biological production of hydroxyl radicals, Biochem. J. 182: 625–628.

    Google Scholar 

  • Winterboum, C. C., 1981, Hydroxyl radical production in body fluids. Roles of metal ions, ascorbate and superoxide, Biochem. J. 198: 125–131.

    Google Scholar 

  • Winterboum, C. C., McGrath, B. N. M., and Carrell, R. W., 1976, Reactions involving superoxide and normal and unstable haemoglobins, Biochem. J. 155: 493–502.

    Google Scholar 

  • Wittenberg, J. B., Wittenberg, B. A., Peisach, J., and Blumberg, W. E., 1970, On the state of iron and the nature of the ligand in oxyhaemoglobin, Proc. Natl. Acad. Sci. USA 67: 1846–1853.

    Article  PubMed  CAS  Google Scholar 

  • Wolff, S. P., and Dean, R. T., 1986, Fragmentation of proteins by free radicals and its effect on their susceptibility to enzymic hydrolysis, Biochem. J. 234: 399–403.

    PubMed  CAS  Google Scholar 

  • Wolff, S. P. Garner, A., and Dean, R. T., 1986, Free radicals, lipids and protein degradation, Trends Biochem. Sci. 11: 27–31.

    Article  CAS  Google Scholar 

  • Worwood, M. J., 1983, Iron and haemochromatosis, J. Inher. Metab. Dis. 6: 63–69.

    Article  PubMed  Google Scholar 

  • Yoshino, S., Blake, D. R., Hewitt, S., Morris, C., and Bacon, P. A., 1985, Effect of blood on the activity and persistence of antigen reduced inflammation in the rat air pouch, Ann. Rheum. Dis. 44: 495–490.

    Article  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Biochemistry and Chemistry, Royal Free Hospital School of Medicine, London, NW3 2PF, England

    Catherine Rice-Evans

Authors
  1. Catherine Rice-Evans
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. North East Thames Regional Transfusion Centre, CM15 8DP, Brentwood, Essex, England

    J. Robin Harris

Rights and permissions

Reprints and permissions

Copyright information

© 1990 Springer Science+Business Media New York

About this chapter

Cite this chapter

Rice-Evans, C. (1990). Iron-Mediated Oxidative Stress and Erythrocytes. In: Harris, J.R. (eds) Erythroid Cells. Blood Cell Biochemistry, vol 1. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9528-8_14

Download citation

  • DOI: https://doi.org/10.1007/978-1-4757-9528-8_14

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4757-9530-1

  • Online ISBN: 978-1-4757-9528-8

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation