Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1986 Jul 1;237(1):265–269. doi: 10.1042/bj2370265

Sickle cell membranes and oxidative damage.

C Rice-Evans, S C Omorphos, E Baysal
PMCID: PMC1146974  PMID: 3800879

Abstract

Sickle erythrocytes and their membranes are susceptible to endogenous free-radical-mediated oxidative damage which correlates with the proportion of irreversibly sickled cells. The suppression of incubation-induced oxidative stress by antioxidants, free radical scavengers and an iron chelator suggest that oxidation products of membrane-bound haemoglobin contribute towards the pathology of the disease.

Full text

PDF
265

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Asakura T., Minakata K., Adachi K., Russell M. O., Schwartz E. Denatured hemoglobin in sickle erythrocytes. J Clin Invest. 1977 Apr;59(4):633–640. doi: 10.1172/JCI108681. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. BARTLETT G. R. Phosphorus assay in column chromatography. J Biol Chem. 1959 Mar;234(3):466–468. [PubMed] [Google Scholar]
  3. BEUTLER E., DURON O., KELLY B. M. Improved method for the determination of blood glutathione. J Lab Clin Med. 1963 May;61:882–888. [PubMed] [Google Scholar]
  4. BLIGH E. G., DYER W. J. A rapid method of total lipid extraction and purification. Can J Biochem Physiol. 1959 Aug;37(8):911–917. doi: 10.1139/o59-099. [DOI] [PubMed] [Google Scholar]
  5. Ballas S. K., Burka E. R. Failure to demonstrate red cell membrane protein abnormalities in sickle cell anaemia. Br J Haematol. 1980 Dec;46(4):627–629. doi: 10.1111/j.1365-2141.1980.tb06022.x. [DOI] [PubMed] [Google Scholar]
  6. Bidlack W. R., Tappel A. L. Fluorescent products of phospholipids during lipid peroxidation. Lipids. 1973 Apr;8(4):203–207. doi: 10.1007/BF02544636. [DOI] [PubMed] [Google Scholar]
  7. Chiu D., Lubin B. Abnormal vitamin E and glutathione peroxidase levels in sickle cell anemia: evidence for increased susceptibility to lipid peroxidation in vivo. J Lab Clin Med. 1979 Oct;94(4):542–548. [PubMed] [Google Scholar]
  8. Chiu D., Lubin B., Shohet S. B. Erythrocyte membrane lipid reorganization during the sickling process. Br J Haematol. 1979 Feb;41(2):223–234. doi: 10.1111/j.1365-2141.1979.tb05851.x. [DOI] [PubMed] [Google Scholar]
  9. DODGE J. T., MITCHELL C., HANAHAN D. J. The preparation and chemical characteristics of hemoglobin-free ghosts of human erythrocytes. Arch Biochem Biophys. 1963 Jan;100:119–130. doi: 10.1016/0003-9861(63)90042-0. [DOI] [PubMed] [Google Scholar]
  10. Das S. K., Nair R. C. Superoxide dismutase, glutathione peroxidase, catalase and lipid peroxidation of normal and sickled erythrocytes. Br J Haematol. 1980 Jan;44(1):87–92. doi: 10.1111/j.1365-2141.1980.tb01186.x. [DOI] [PubMed] [Google Scholar]
  11. Diplock A. T. The role of vitamin E in biological membranes. Ciba Found Symp. 1983;101:45–55. doi: 10.1002/9780470720820.ch4. [DOI] [PubMed] [Google Scholar]
  12. ELLMAN G. L. Tissue sulfhydryl groups. Arch Biochem Biophys. 1959 May;82(1):70–77. doi: 10.1016/0003-9861(59)90090-6. [DOI] [PubMed] [Google Scholar]
  13. Eaton J. W., Skelton T. D., Swofford H. S., Kolpin C. E., Jacob H. S. Elevated erythrocyte calcium in sickle cell disease. Nature. 1973 Nov 9;246(5428):105–106. doi: 10.1038/246105a0. [DOI] [PubMed] [Google Scholar]
  14. Freedman R. B., Radda G. K. The interaction of 1-anilino-8-naphthalene sulphonate with erythrocyte membranes. FEBS Lett. 1969 Apr;3(2):150–152. doi: 10.1016/0014-5793(69)80121-3. [DOI] [PubMed] [Google Scholar]
  15. Glader B. E., Lux S. E., Muller-Soyano A., Platt O. S., Propper R. D., Nathan D. G. Energy reserve and cation composition of irreversibly sickled cells in vivo. Br J Haematol. 1978 Dec;40(4):527–532. doi: 10.1111/j.1365-2141.1978.tb05828.x. [DOI] [PubMed] [Google Scholar]
  16. Graf E., Mahoney J. R., Bryant R. G., Eaton J. W. Iron-catalyzed hydroxyl radical formation. Stringent requirement for free iron coordination site. J Biol Chem. 1984 Mar 25;259(6):3620–3624. [PubMed] [Google Scholar]
  17. Gutteridge J. M., Richmond R., Halliwell B. Inhibition of the iron-catalysed formation of hydroxyl radicals from superoxide and of lipid peroxidation by desferrioxamine. Biochem J. 1979 Nov 15;184(2):469–472. doi: 10.1042/bj1840469. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. HARLEY J. D., MAUER A. M. Studies on the formation of Heinz bodies. I. Methemoglobin production and oxyhemoglobin destruction. Blood. 1960 Dec;16:1722–1735. [PubMed] [Google Scholar]
  19. Halliwell B., Gutteridge J. M. Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem J. 1984 Apr 1;219(1):1–14. doi: 10.1042/bj2190001. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. 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 Lett. 1978 Aug 15;92(2):321–326. doi: 10.1016/0014-5793(78)80779-0. [DOI] [PubMed] [Google Scholar]
  21. Hebbel R. P., Eaton J. W., Balasingam M., Steinberg M. H. Spontaneous oxygen radical generation by sickle erythrocytes. J Clin Invest. 1982 Dec;70(6):1253–1259. doi: 10.1172/JCI110724. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Jain S. K., Shohet S. B. A novel phospholipid in irreversibly sickled cells: evidence for in vivo peroxidative membrane damage in sickle cell disease. Blood. 1984 Feb;63(2):362–367. [PubMed] [Google Scholar]
  23. Kennedy A., Rice-Evans C. A spectrofluorimetric study of the interaction of glycerol mono-oleate with human erythrocyte ghosts. FEBS Lett. 1976 Oct 15;69(1):45–50. doi: 10.1016/0014-5793(76)80650-3. [DOI] [PubMed] [Google Scholar]
  24. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  25. Lux S. E., John K. M., Karnovsky M. J. Irreversible deformation of the spectrin-actin lattice in irreversibly sickled cells. J Clin Invest. 1976 Oct;58(4):955–963. doi: 10.1172/JCI108549. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Muakkassah-Kelly S. F., Andresen J. W., Shih J. C., Hochstein P. Decreased [3H]serotonin and [3H]spiperone binding consequent to lipid peroxidation in rat cortical membranes. Biochem Biophys Res Commun. 1982 Feb 11;104(3):1003–1010. doi: 10.1016/0006-291x(82)91349-3. [DOI] [PubMed] [Google Scholar]
  27. O'Brien P. J. Intracellular mechanisms for the decomposition of a lipid peroxide. I. Decomposition of a lipid peroxide by metal ions, heme compounds, and nucleophiles. Can J Biochem. 1969 May;47(5):485–492. doi: 10.1139/o69-076. [DOI] [PubMed] [Google Scholar]
  28. Palek J. Red cell membrane injury in sickle cell anaemia. Br J Haematol. 1977 Jan;35(1):1–9. doi: 10.1111/j.1365-2141.1977.tb00556.x. [DOI] [PubMed] [Google Scholar]
  29. Platt O. S., Falcone J. F., Lux S. E. Molecular defect in the sickle erythrocyte skeleton. Abnormal spectrin binding to sickle inside-our vesicles. J Clin Invest. 1985 Jan;75(1):266–271. doi: 10.1172/JCI111684. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Rank B. H., Carlsson J., Hebbel R. P. Abnormal redox status of membrane-protein thiols in sickle erythrocytes. J Clin Invest. 1985 May;75(5):1531–1537. doi: 10.1172/JCI111857. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Rice-Evans C., Baysal E., Kontoghiorghes G. J., Flynn D. M., Hoffbrand A. V. Oxidative effects of iron on erythrocytes. Free Radic Res Commun. 1985;1(1):55–62. doi: 10.3109/10715768509056536. [DOI] [PubMed] [Google Scholar]
  32. Rice-Evans C., Baysal E., Pashby D. P., Hochstein P. t-butyl hydroperoxide-induced perturbations of human erythrocytes as a model for oxidant stress. Biochim Biophys Acta. 1985 May 28;815(3):426–432. doi: 10.1016/0005-2736(85)90370-0. [DOI] [PubMed] [Google Scholar]
  33. Rice-Evans C., Bruckdorfer K. R., Dootson G. Studies on the altered membrane characteristics of sickle cells. FEBS Lett. 1978 Oct 1;94(1):81–86. doi: 10.1016/0014-5793(78)80911-9. [DOI] [PubMed] [Google Scholar]
  34. Shaklai N., Sharma V. S., Ranney H. M. Interaction of sickle cell hemoglobin with erythrocyte membranes. Proc Natl Acad Sci U S A. 1981 Jan;78(1):65–68. doi: 10.1073/pnas.78.1.65. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Walls R., Kumar K. S., Hochstein P. Aging human erythrocytes. Differential sensitivity of young and old erythrocytes to hemolysis induced by peroxide in the presence of thyroxine. Arch Biochem Biophys. 1976 Jun;174(2):463–468. doi: 10.1016/0003-9861(76)90374-x. [DOI] [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES