Thiol Compounds as Protective Agents in Erythrocytes Under Oxidative Stress

References

• Cotgreave I., Moldeus P., Schuppe I. The metabolism of N-acetylcysteine by human endothelial cells. Biochemical Pharmacology 1991; 42: 13–16
   PubMed Web of Science ®Google Scholar
• Aruoma O.I., Halliwell B., Hoey B.M., Butler J. The antioxidant action of N-acetylcysteine: its reaction with hydrogen peroxide. Free Radical Biology and Medicine 1989; 6: 593–597
   PubMed Web of Science ®Google Scholar
• Turner J.J.O., Rice-Evans C., Davies M.J., Newman E.S.R. The formation of free radicals by cardiac myocytes under oxidative stress and the effects of electron-donating drugs. Biochemical Journal 1991; 277: 833–837
   PubMed Web of Science ®Google Scholar
• Zimmer G., Evers J. 2-Mercaptopropionyl glycine improves aortic flow after reoxygenation in working rat hearts. Basic Research in Cardiology 1988; 83: 445–451
   PubMedGoogle Scholar
• Bolli R., Jeroudi M.O., Patel B.S., Aruoma O.I., Halliwell B., Lau E.K., McCay B.P. Marked reduction of free radical generation and contractile dysfunction of antioxidant therapy begun at the time of reperfusion. Evidence that myocardial stunning is a manifestation of reperfusion injury. Circulation Research 1989; 65: 607–622
   PubMed Web of Science ®Google Scholar
• Chaudiere J., Wihelmensen E.C., Tappel A.L. Mechanism of selenium glutathione peroxidase and its inhibition by mercaptocarboxylic acids and other mercaptans. Journal of Biological Chemistry 1984; 259: 1043–1050
   PubMed Web of Science ®Google Scholar
• Hebbel R.P. The sickle erythrocyte in double jeopardy: autoxidation and iron decompartmentalisation. Seminars in Haematology 1990; 27: 51–69
   PubMed Web of Science ®Google Scholar
• Rice-Evans C., Omorphos S.C., White J. The effects of hydrazine on erythrocytes. Biochimica Biophysica Acta 1982; 691: 367–371
   PubMedGoogle Scholar
• Rice-Evans C., Omorphos S.C., Baysal E. Sickle cell membranes and oxidative damage. Biochemical Journal 1986; 237: 265–267
   PubMed Web of Science ®Google Scholar
• Hebbel R.P., Eaton J.W., Balasingam M. Spontaneous oxygen radical generation by sickle erythrocytes. Journal of Clinical Investigation 1982; 70: 1253–1259
   PubMed Web of Science ®Google Scholar
• Hebbel R.P., Eaton J.W. Pathology of heme interaction with the erythrocyte membrane. Seminars in Haematology 1989; 26: 136–140
   PubMed Web of Science ®Google Scholar
• Hartley A., Davies M., Rice-Evans C. Desferrioxamine as a lipid chainbreaking antioxidant in sickle erythrocyte membranes. FEBS Letters 1990; 264: 145–148
   PubMed Web of Science ®Google Scholar
• Kuross S.A., Hebbel R.P. Non-heme iron in sickle erythrocyte membranes: association with phospholipids and potential role in lipid peroxidation. Blood 1988; 72: 1278–1285
   PubMed Web of Science ®Google Scholar
• Hartley A., Rice-Evans C. The nature of membrane-bound iron species involved in radical-mediated damage in sickle erythrocytes. Biochemical Society Transactions 1989; 17: 488–489
   Google Scholar
• Rice-Evans C. Iron-mediated oxidative stress in erythrocytes in. Blood cell Biochemistry, J.R. Harris. Plenum Press, New York and London 1990; 429–453
   Google Scholar
• Beutler E., Duron D., Kelly B.M. Improved method for the determination of blood glutathione. Journal of Laboratory and Clinical Medicine 1963; 61: 882–886
   PubMed Web of Science ®Google Scholar
• Dodge J.T., Mitchell C., Hanhanan D.J. The preparation and chemical characteristics of haemoglobin-free ghosts of human erythrocytes. Archives of Biochemistry and Biophysics 1963; 100: 119–128
   PubMed Web of Science ®Google Scholar
• Lowry O.H., Rosebrough N.J., Farr A.L., Randall R.J. Protein measurement with the folin phenol reagent. Journal of Biological Chemistry 1951; 193: 265–275
   PubMed Web of Science ®Google Scholar
• Walls R., Kumar K.S., Hochstein P. Aging human erythrocytes. Differential sensitivity of young and old erythrocytes to haemolysis induced by peroxide in the presence of thyroxine. Archives of Biochemistry and Biophysics 1976; 174: 463–468
   PubMed Web of Science ®Google Scholar
• Gutteridge J.M.C. Aspects to consider when detecting and measuring lipid peroxidation. Free Radical Research Communications 1986; 1: 173–184
   PubMedGoogle Scholar
• Haest C., Plasa G., Kays P., Deuticke B. Spectrin as a stabiliser of phospholipid asymmetry in the human erythrocyte membrane. Biochimica Biophysica Acta 1978; 509: 21–32
   PubMedGoogle Scholar
• Lachant N.A., Davidson W.B., Tanika K.R. Impaired pentose phosphate shunt function in sickle cell disease: a potential mechanism for increased Heinz body formation and membrane lipid peroxidation. American Journal of Haematology 1983; 15: 1–13
   PubMed Web of Science ®Google Scholar
• Wettersroem W., Brewer G.J., Warth J.A., Mitchinson A., Near K. Relationship of glutathione levels and Heinz body formation to irreversibly sickled cell in sickle cell anaemia. Journal of Laboratory and Clinical Medicine 1984; 103: 589–596
   PubMedGoogle Scholar
• Sullivan S.G., Stern A. Membrane protein changes induced by t-butyl hydroperoxide in red blood cells. Biochimica Biophysica Acta 1984; 774: 215–220
   PubMedGoogle Scholar
• Puppo A., Cecchini R., Aruoma O.I., Bolli R., Halliwell B. Scavenging of hypochlorous acid and of myoglobin-derived oxidants by the cardio-protective agent mercaptopropionyl glycine. Free Radical Research Communications 1990; 10: 371–381
   PubMed Web of Science ®Google Scholar
• Rice-Evans C., Okunade G., Khan R. The suppression of iron release from activated myoglobin by physiological electron donors and desferoxamine. Free Radical Research Communications 1989; 7: 45–54
   PubMed Web of Science ®Google Scholar