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Volumn 267, Issue 2, 1997, Pages 129-142

Antioxidant defence of red blood cells and plasma in stored human blood

Author keywords

Antioxidant systems; Blood storage; Catalase; Glutathione dependent enzymes; Peroxidation; Superoxide dismutase; TRAP

Indexed keywords

ANTIOXIDANT; CATALASE; GLUTATHIONE; GLUTATHIONE DISULFIDE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; SUPEROXIDE DISMUTASE;

EID: 18544394874     PISSN: 00098981     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-8981(97)00148-4     Document Type: Article
Times cited : (66)

References (56)
  • 1
    • 0021873087 scopus 로고
    • The membrane and the lesions of storage in preserved red cells
    • Wolfe L.C. The membrane and the lesions of storage in preserved red cells. Transfusion. 25:1985;185-203.
    • (1985) Transfusion , vol.25 , pp. 185-203
    • Wolfe, L.C.1
  • 2
    • 0015057291 scopus 로고
    • The autoxidation of red cells
    • Dormandy T.L. The autoxidation of red cells. Br J Haematol. 20:1971;457-461.
    • (1971) Br J Haematol , vol.20 , pp. 457-461
    • Dormandy, T.L.1
  • 3
    • 0021351203 scopus 로고
    • Oxygen toxicity, oxygen radicals, transition metals and disease
    • Halliwell B., Gutteridge J.M.C. Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem J. 219:1984;1-14.
    • (1984) Biochem J , vol.219 , pp. 1-14
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 4
    • 0024468158 scopus 로고
    • Lipid peroxidation in human red cells
    • Chiu D., Kuypers F., Lubin B. Lipid peroxidation in human red cells. Semin Hematol. 26:1989;257-276.
    • (1989) Semin Hematol , vol.26 , pp. 257-276
    • Chiu, D.1    Kuypers, F.2    Lubin, B.3
  • 6
    • 0023853772 scopus 로고
    • Evidence for membrane lipid peroxidation during the in vivo aging of human erythrocytes
    • Jain S.K. Evidence for membrane lipid peroxidation during the in vivo aging of human erythrocytes. Biochim Biophys Acta. 937:1988;205-210.
    • (1988) Biochim Biophys Acta , vol.937 , pp. 205-210
    • Jain, S.K.1
  • 7
    • 0023201142 scopus 로고
    • Lipoperoxides in plasma as measured by liquid chromatographic separation of malonyldialdehyde-thiobarbituric acid adduct
    • Wong S.H.Y., Knight J.A., Hopfer S.M., Zacharia O., Leach C.N. Jr., Sunderman F.W. Jr. Lipoperoxides in plasma as measured by liquid chromatographic separation of malonyldialdehyde-thiobarbituric acid adduct. Clin Chem. 33:1987;214-220.
    • (1987) Clin Chem , vol.33 , pp. 214-220
    • Wong, S.H.Y.1    Knight, J.A.2    Hopfer, S.M.3    Zacharia, O.4    Leach C.N., Jr.5    Sunderman F.W., Jr.6
  • 9
    • 0015511913 scopus 로고
    • Intracellular pH of red cells stored in acid citrate dextrose medium
    • Tsuda S., Kakinuma K., Minarami S. Intracellular pH of red cells stored in acid citrate dextrose medium. Experientia. 28:1972;1481-1482.
    • (1972) Experientia , vol.28 , pp. 1481-1482
    • Tsuda, S.1    Kakinuma, K.2    Minarami, S.3
  • 10
    • 0015432442 scopus 로고
    • Red cell 2,3-diphosphoglycerate and intracellular arterial pH in acidosis and alkalosis
    • Desforges J.F., Slawski P. Red cell 2,3-diphosphoglycerate and intracellular arterial pH in acidosis and alkalosis. Blood. 40:1972;740-746.
    • (1972) Blood , vol.40 , pp. 740-746
    • Desforges, J.F.1    Slawski, P.2
  • 12
    • 0026704767 scopus 로고
    • The effect of metal chelators on lipid peroxidation in stored erythrocytes
    • Knight A., Voorhees R.P., Martin L. The effect of metal chelators on lipid peroxidation in stored erythrocytes. Ann Clin Lab Sci. 22:1992;207-213.
    • (1992) Ann Clin Lab Sci , vol.22 , pp. 207-213
    • Knight, A.1    Voorhees, R.P.2    Martin, L.3
  • 13
    • 37049066149 scopus 로고
    • A scheme for the colorimetric determination of microgram amounts of thiols
    • Seville B. A scheme for the colorimetric determination of microgram amounts of thiols. Analyst. 33:1958;670-672.
    • (1958) Analyst , vol.33 , pp. 670-672
    • Seville, B.1
  • 14
    • 0014108436 scopus 로고
    • Studies on quantitative and qualitative characterisation of erythrocytes glutathione peroxidase
    • Paglia D.E., Valentine W.N. Studies on quantitative and qualitative characterisation of erythrocytes glutathione peroxidase. J Lab Clin Med. 70:1967;158-169.
    • (1967) J Lab Clin Med , vol.70 , pp. 158-169
    • Paglia, D.E.1    Valentine, W.N.2
  • 16
    • 0017293933 scopus 로고
    • Evaluation of method of coenzyme activation of erythrocytes for detection of vitamins B1, B2, and B6
    • Bayoumi R.A., Rosalki S.B. Evaluation of method of coenzyme activation of erythrocytes for detection of vitamins B1, B2, and B6. Clin Chem. 22:1976;327-335.
    • (1976) Clin Chem , vol.22 , pp. 327-335
    • Bayoumi, R.A.1    Rosalki, S.B.2
  • 17
    • 41049100518 scopus 로고
    • A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase
    • Beers R.F.J., Sizer J.W. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem. 195:1952;33-34.
    • (1952) J Biol Chem , vol.195 , pp. 33-34
    • Beers, R.F.J.1    Sizer, J.W.2
  • 18
    • 0023662410 scopus 로고
    • The relative contributions of vitamin E, urate, ascorbate and proteins to the total peroxyl radical-trapping antioxidant activity of human blood plasma
    • Wayner D.D.M., Burton G.W., Ingold K.U., Barclay R.L.C., Locke S.J. The relative contributions of vitamin E, urate, ascorbate and proteins to the total peroxyl radical-trapping antioxidant activity of human blood plasma. Biochim Biophys Acta. 924:1987;408-419.
    • (1987) Biochim Biophys Acta , vol.924 , pp. 408-419
    • Wayner, D.D.M.1    Burton, G.W.2    Ingold, K.U.3    Barclay, R.L.C.4    Locke, S.J.5
  • 19
    • 0025350138 scopus 로고
    • Experimental biology of cerebral hypoxia-ischemia: Relation to perinatal brain damage
    • Vannuci R.C. Experimental biology of cerebral hypoxia-ischemia: relation to perinatal brain damage. Pediatr Res. 27:1990;317-326.
    • (1990) Pediatr Res , vol.27 , pp. 317-326
    • Vannuci, R.C.1
  • 20
    • 0026349756 scopus 로고
    • Mechanisms of perinatal brain damage
    • Kjellmer I. Mechanisms of perinatal brain damage. Ann Med. 23:1991;675-679.
    • (1991) Ann Med , vol.23 , pp. 675-679
    • Kjellmer, I.1
  • 21
    • 0029015925 scopus 로고
    • Arachidonic acid supplementation enhances hydrogen peroxide induced injury of neonatal rat cardiac myocytes
    • Toraason M., Wey H., Woolery M., Plews P., Hoffman P. Arachidonic acid supplementation enhances hydrogen peroxide induced injury of neonatal rat cardiac myocytes. Cardiovasc Res. 29:1995;624-628.
    • (1995) Cardiovasc Res , vol.29 , pp. 624-628
    • Toraason, M.1    Wey, H.2    Woolery, M.3    Plews, P.4    Hoffman, P.5
  • 22
    • 0026803213 scopus 로고
    • Ischemia and reperfusion: Effect of fructose-1,6-bisphosphate
    • Lazzarino G., Tavazzi B., Di Pierro D. Ischemia and reperfusion: effect of fructose-1,6-bisphosphate. Free Radic Res Commun. 16:1992;325-339.
    • (1992) Free Radic Res Commun , vol.16 , pp. 325-339
    • Lazzarino, G.1    Tavazzi, B.2    Di Pierro, D.3
  • 24
    • 0024602827 scopus 로고
    • Tissue destruction by neutrophils
    • Weiss S.J. Tissue destruction by neutrophils. N Engl J Med. 320:1989;365-374.
    • (1989) N Engl J Med , vol.320 , pp. 365-374
    • Weiss, S.J.1
  • 26
    • 0021503754 scopus 로고
    • A controversy on the mechanism of autoxidation of oxymyoglobin and oxyhemoglobin
    • Shikama K. A controversy on the mechanism of autoxidation of oxymyoglobin and oxyhemoglobin. Biochem J. 223:1984;279-284.
    • (1984) Biochem J , vol.223 , pp. 279-284
    • Shikama, K.1
  • 27
    • 0022272178 scopus 로고
    • Free-radical production and oxidative reactions of hemoglobin
    • Winterbourn C.C. Free-radical production and oxidative reactions of hemoglobin. Environ Health Perspect. 64:1985;321-330.
    • (1985) Environ Health Perspect , vol.64 , pp. 321-330
    • Winterbourn, C.C.1
  • 28
    • 0001540685 scopus 로고
    • Generation of superoxide radicals during the autoxidation of mammalian oxyhemoglobin
    • Wever R., Oudega B., Van Gelder B.F. Generation of superoxide radicals during the autoxidation of mammalian oxyhemoglobin. Biochim Biophys Acta. 302:1973;475-478.
    • (1973) Biochim Biophys Acta , vol.302 , pp. 475-478
    • Wever, R.1    Oudega, B.2    Van Gelder, B.F.3
  • 29
    • 0015502066 scopus 로고
    • The generation of superoxide radical during the autoxidation of hemoglobin
    • Misra H.P., Fridovich I. The generation of superoxide radical during the autoxidation of hemoglobin. J Biol Chem. 247:1972;6960-6962.
    • (1972) J Biol Chem , vol.247 , pp. 6960-6962
    • Misra, H.P.1    Fridovich, I.2
  • 30
    • 0017113866 scopus 로고
    • Reactions involving superoxide and normal and unstable hemoglobins
    • Winterbourn C.C., McGrath B.M., Carrel R.W. Reactions involving superoxide and normal and unstable hemoglobins. Biochem J. 155:1976;493-502.
    • (1976) Biochem J , vol.155 , pp. 493-502
    • Winterbourn, C.C.1    McGrath, B.M.2    Carrel, R.W.3
  • 31
    • 0017238249 scopus 로고
    • Inhibition by superoxide dismutase of methemoglobin formation from oxyhemoglobin
    • Lynch R.E., Lee G.R., Cartwright G.E. Inhibition by superoxide dismutase of methemoglobin formation from oxyhemoglobin. J Biol Chem. 251:1976;1015-1019.
    • (1976) J Biol Chem , vol.251 , pp. 1015-1019
    • Lynch, R.E.1    Lee, G.R.2    Cartwright, G.E.3
  • 32
    • 0017359334 scopus 로고
    • Direct generation of superoxide anions by flash photolysis of human oxyhemoglobin
    • Demma L.S., Salhany J.M. Direct generation of superoxide anions by flash photolysis of human oxyhemoglobin. J Biol Chem. 252:1977;1226-1230.
    • (1977) J Biol Chem , vol.252 , pp. 1226-1230
    • Demma, L.S.1    Salhany, J.M.2
  • 33
    • 0000448117 scopus 로고
    • Oxidation of myoglobin by oxygen
    • George P., Stratmann C.J. Oxidation of myoglobin by oxygen. Biochem J. 51:1952;418-425.
    • (1952) Biochem J , vol.51 , pp. 418-425
    • George, P.1    Stratmann, C.J.2
  • 35
    • 0014959041 scopus 로고
    • Heme transfer from hemoglobin and ferrihemoglobin to some new ligands and its implication in the mechanism of oxidation of ferrohemoglobin by air
    • Banerjee R., Stetzkowski F. Heme transfer from hemoglobin and ferrihemoglobin to some new ligands and its implication in the mechanism of oxidation of ferrohemoglobin by air. Biochim Biophys Acta. 221:1970;636-639.
    • (1970) Biochim Biophys Acta , vol.221 , pp. 636-639
    • Banerjee, R.1    Stetzkowski, F.2
  • 36
    • 0022394280 scopus 로고
    • The importance of free radicals and catalytic metal ions in human diseases
    • Halliwell B., Gutteridge J.M.C. The importance of free radicals and catalytic metal ions in human diseases. Mol Aspects Med. 8:1985;189-193.
    • (1985) Mol Aspects Med , vol.8 , pp. 189-193
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 37
    • 0022529172 scopus 로고
    • Oxygen free radicals and iron in relation to biology and medicine: Some problems and concepts
    • Halliwell B., Gutteridge J.M.C. Oxygen free radicals and iron in relation to biology and medicine: some problems and concepts. Arch Biochem Biophys. 246:1986;501-504.
    • (1986) Arch Biochem Biophys , vol.246 , pp. 501-504
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 38
    • 0023759565 scopus 로고
    • The potential diagram for oxygen at pH 7.0
    • Wood P. The potential diagram for oxygen at pH 7.0. Biochem J. 253:1988;287-289.
    • (1988) Biochem J , vol.253 , pp. 287-289
    • Wood, P.1
  • 39
    • 0023779695 scopus 로고
    • Formation of hydroxyl radicals from hydrogen peroxide in the presence of iron
    • Puppo A., Halliwell B. Formation of hydroxyl radicals from hydrogen peroxide in the presence of iron. Biochem J. 249:1988;185-190.
    • (1988) Biochem J , vol.249 , pp. 185-190
    • Puppo, A.1    Halliwell, B.2
  • 40
    • 0025342010 scopus 로고
    • The hepatic glutathione system - Influence of xenobiotics
    • Kretzschmar M., Klinger W. The hepatic glutathione system - influence of xenobiotics. Exp Pathol. 38:1990;145-164.
    • (1990) Exp Pathol , vol.38 , pp. 145-164
    • Kretzschmar, M.1    Klinger, W.2
  • 41
    • 0023389164 scopus 로고
    • The enzymes of glutathione metabolism: An overview
    • Mannervik B. The enzymes of glutathione metabolism: an overview. Biochem Soc Trans. 15:1987;717-719.
    • (1987) Biochem Soc Trans , vol.15 , pp. 717-719
    • Mannervik, B.1
  • 42
    • 0021240616 scopus 로고
    • Glutathione depletion and susceptibility
    • Reed D.J., Fariss M.W. Glutathione depletion and susceptibility. Pharmacol Rev. 36:1984;25-33.
    • (1984) Pharmacol Rev , vol.36 , pp. 25-33
    • Reed, D.J.1    Fariss, M.W.2
  • 43
    • 0024432603 scopus 로고
    • Regulation of cellular glutathione
    • Deneke S.M., Fanburg B.L. Regulation of cellular glutathione. Am J Physiol. 257:1989;L163-L173.
    • (1989) Am J Physiol , vol.257
    • Deneke, S.M.1    Fanburg, B.L.2
  • 44
    • 0025298097 scopus 로고
    • Glutathione-dependent protection against oxidative injury
    • Shan X.Q., Aw T.Y., Jones D.P. Glutathione-dependent protection against oxidative injury. Pharmacol Ther. 47:1990;61-71.
    • (1990) Pharmacol Ther , vol.47 , pp. 61-71
    • Shan, X.Q.1    Aw, T.Y.2    Jones, D.P.3
  • 45
    • 0025259693 scopus 로고
    • Lipid peroxidation and antioxidant systems in the liver injury produced by glutathione depleting agents
    • Maellaro E., Casini A.F., Del Bello B., Comporti M. Lipid peroxidation and antioxidant systems in the liver injury produced by glutathione depleting agents. Biochem Pharmacol. 9:1990;1513-1521.
    • (1990) Biochem Pharmacol , vol.9 , pp. 1513-1521
    • Maellaro, E.1    Casini, A.F.2    Del Bello, B.3    Comporti, M.4
  • 46
    • 0026712171 scopus 로고
    • Lipid peroxidation - A common pathogenetic mechanism?
    • Dargel R. Lipid peroxidation - a common pathogenetic mechanism? Exp Toxicol Pathol. 44:1992;169-181.
    • (1992) Exp Toxicol Pathol , vol.44 , pp. 169-181
    • Dargel, R.1
  • 47
    • 0021777064 scopus 로고
    • The role of aspartic acid and asparagine residues in the aging of erythrocyte proteins: Cellular metabolism of racemized and isomerised forms by methylation reactions
    • Clarke S. The role of aspartic acid and asparagine residues in the aging of erythrocyte proteins: Cellular metabolism of racemized and isomerised forms by methylation reactions. Prog Clin Biol Res. 195:1985;91-107.
    • (1985) Prog Clin Biol Res , vol.195 , pp. 91-107
    • Clarke, S.1
  • 48
    • 0021891879 scopus 로고
    • Protein carboxyl methyltransferases: Two distinct classes of enzymes
    • Clarke S. Protein carboxyl methyltransferases: two distinct classes of enzymes. Ann Rev Biochem. 54:1985;479-506.
    • (1985) Ann Rev Biochem , vol.54 , pp. 479-506
    • Clarke, S.1
  • 49
    • 0020057229 scopus 로고
    • The effect of malonyldialdehyde on erythrocyte deformability
    • Pfafferot C., Meiselman H.J., Hochstein P. The effect of malonyldialdehyde on erythrocyte deformability. Blood. 59:1982;12-15.
    • (1982) Blood , vol.59 , pp. 12-15
    • Pfafferot, C.1    Meiselman, H.J.2    Hochstein, P.3
  • 51
    • 0019474177 scopus 로고
    • Association of lipid peroxidation and polymerization of membrane proteins with erythrocyte aging
    • Hochstein P., Jain S.K. Association of lipid peroxidation and polymerization of membrane proteins with erythrocyte aging. Fed Proc. 40:1981;183-188.
    • (1981) Fed Proc , vol.40 , pp. 183-188
    • Hochstein, P.1    Jain, S.K.2
  • 52
    • 0029311236 scopus 로고
    • Cell damage in inflammatory and infectious sites might involve a coordinated 'cross-talk' among oxidants, microbial haemolysins and ampiphiles, cationic proteins, phospholipases, fatty acids, proteinases and cytokines (an overview)
    • Ginsburg I., Kohen R. Cell damage in inflammatory and infectious sites might involve a coordinated 'cross-talk' among oxidants, microbial haemolysins and ampiphiles, cationic proteins, phospholipases, fatty acids, proteinases and cytokines (an overview). Free Radic Res Commun. 22:1995;489-517.
    • (1995) Free Radic Res Commun , vol.22 , pp. 489-517
    • Ginsburg, I.1    Kohen, R.2
  • 53
    • 0021719627 scopus 로고
    • Neutrophils mediate lipid peroxidation in human red cells
    • Claster S., Chiu D.T.Y., Quintanilha A., Lubin B. Neutrophils mediate lipid peroxidation in human red cells. Blood. 64:1984;1079-1084.
    • (1984) Blood , vol.64 , pp. 1079-1084
    • Claster, S.1    Chiu, D.T.Y.2    Quintanilha, A.3    Lubin, B.4
  • 54
    • 0019389783 scopus 로고
    • Role of hydrogen peroxide in neutrophil-mediated destruction of cultured endothelial cells
    • Weiss S.J., Young J., Lobuglio A.F., Slivka A., Nimen N.F. Role of hydrogen peroxide in neutrophil-mediated destruction of cultured endothelial cells. J Clin Invest. 68:1981;714-721.
    • (1981) J Clin Invest , vol.68 , pp. 714-721
    • Weiss, S.J.1    Young, J.2    Lobuglio, A.F.3    Slivka, A.4    Nimen, N.F.5
  • 55
    • 0019161779 scopus 로고
    • The role of superoxide in the destruction of erythrocyte targets by human neutrophils
    • Weiss S.J. The role of superoxide in the destruction of erythrocyte targets by human neutrophils. J Biol Chem. 255:1980;9912-9917.
    • (1980) J Biol Chem , vol.255 , pp. 9912-9917
    • Weiss, S.J.1
  • 56
    • 0022516690 scopus 로고
    • Effects of blood storage on red cell antioxidative systems
    • Webster N.R., Toothil C. Effects of blood storage on red cell antioxidative systems. Acta Haematol. 75:1986;30-33.
    • (1986) Acta Haematol , vol.75 , pp. 30-33
    • Webster, N.R.1    Toothil, C.2


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