메뉴 건너뛰기




Volumn 51, Issue 4, 1999, Pages 341-350

Effect of oxidative stress and erythropoietin on cytoskeletal protein and lipid organization in human erythrocytes

Author keywords

Erythropoietin; Lipid peroxidation; Oxidative damage; Phenylhydrazine

Indexed keywords

ADENOSINE TRIPHOSPHATE; BEE VENOM; CYTOSKELETON PROTEIN; HYDROXYL RADICAL; MEMBRANE PHOSPHOLIPID; PHENYLHYDRAZINE; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLETHANOLAMINE; PHOSPHATIDYLSERINE; PHOSPHOLIPASE A2; PROTEINASE; RECOMBINANT ERYTHROPOIETIN; TYROSINE;

EID: 0032885056     PISSN: 12306002     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (11)

References (51)
  • 1
    • 0001457369 scopus 로고
    • The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid
    • Ames B. N., Dubin D. T.: The role of polyamines in the neutralization of bacteriophage deoxyribonucleic acid. J. Biol. Chem., 1960, 235, 769-775.
    • (1960) J. Biol. Chem. , vol.235 , pp. 769-775
    • Ames, B.N.1    Dubin, D.T.2
  • 2
    • 0022993070 scopus 로고
    • Phenylhydrazine-induced changes in erythrocyte membrane surface lipid packing
    • Arduini A., Chen Z., Stern A.: Phenylhydrazine-induced changes in erythrocyte membrane surface lipid packing. Biochim. Biophys. Acta, 1986, 862, 65-71.
    • (1986) Biochim. Biophys. Acta , vol.862 , pp. 65-71
    • Arduini, A.1    Chen, Z.2    Stern, A.3
  • 3
    • 0022341309 scopus 로고
    • Spectrin degradation in intact red blood cell by phenylhydrazine
    • Arduini A., Stern A.: Spectrin degradation in intact red blood cell by phenylhydrazine. Biochem. Pharmacol., 1985, 34, 4283-4289.
    • (1985) Biochem. Pharmacol. , vol.34 , pp. 4283-4289
    • Arduini, A.1    Stern, A.2
  • 6
    • 0025166591 scopus 로고
    • Pathophysiology of hemolysis in glucose-6-phosphate dehydrogenase deficiency
    • Arese P., De Flora A.: Pathophysiology of hemolysis in glucose-6-phosphate dehydrogenase deficiency. Semin. Hematol., 1990, 27, 1-12.
    • (1990) Semin. Hematol. , vol.27 , pp. 1-12
    • Arese, P.1    De Flora, A.2
  • 7
    • 0015607096 scopus 로고
    • Fluorescent products of phospholipid during lipid peroxidation
    • Bidlack W. R., Tappel A. L.: Fluorescent products of phospholipid during lipid peroxidation. Lipids, 1973, 8, 203-207.
    • (1973) Lipids , vol.8 , pp. 203-207
    • Bidlack, W.R.1    Tappel, A.L.2
  • 8
    • 0020073779 scopus 로고
    • Role of the adenosine triphosphate dependent proteolytic pathway in reticulocyte maturation
    • Boches F. S., Goldberg A. L.: Role of the adenosine triphosphate dependent proteolytic pathway in reticulocyte maturation. Science, 1982, 215, 978-980.
    • (1982) Science , vol.215 , pp. 978-980
    • Boches, F.S.1    Goldberg, A.L.2
  • 9
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye-binding
    • Bradford M. M.: A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye-binding. Anal. Biochem., 1976, 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 0024986495 scopus 로고
    • Phenylhydrazine mediated degradation of bovine serum albumin and membrane proteins of human erythrocytes
    • Chakrabarti S., Naik A. A., Reddy G. R.: Phenylhydrazine mediated degradation of bovine serum albumin and membrane proteins of human erythrocytes. Biochim. Biophys. Acta, 1990, 1028, 89-94.
    • (1990) Biochim. Biophys. Acta , vol.1028 , pp. 89-94
    • Chakrabarti, S.1    Naik, A.A.2    Reddy, G.R.3
  • 15
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals
    • Davies K. J. A.: Protein damage and degradation by oxygen radicals. J. Biol. Chem., 1987, 262, 9895-9901.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9895-9901
    • Davies, K.J.A.1
  • 16
    • 0021189414 scopus 로고
    • Protein damaged by hydroxyl radicals can be recognized and degraded by erythrocytes and reticulocyte proteolytic systems
    • Davies K. J. A., Goldberg A. L.: Protein damaged by hydroxyl radicals can be recognized and degraded by erythrocytes and reticulocyte proteolytic systems. Fed. Proc., 1984, 43, 606.
    • (1984) Fed. Proc. , vol.43 , pp. 606
    • Davies, K.J.A.1    Goldberg, A.L.2
  • 17
    • 0023655258 scopus 로고
    • Oxygen radicals stimulate intracellular proteolysis and lipid peroxidation by independent mechanisms in erythrocytes
    • Davies K. J. A., Goldberg A. L.: Oxygen radicals stimulate intracellular proteolysis and lipid peroxidation by independent mechanisms in erythrocytes. J. Biol. Chem., 1987, 262, 8220-8226.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8220-8226
    • Davies, K.J.A.1    Goldberg, A.L.2
  • 18
    • 0023655050 scopus 로고
    • Proteins damaged by oxygen radicals are rapidly degraded in extracts of red blood cells
    • Davies K. J. A., Goldberg A. L.: Proteins damaged by oxygen radicals are rapidly degraded in extracts of red blood cells. J. Biol. Chem., 1987, 262, 8227-8234.
    • (1987) J. Biol. Chem. , vol.262 , pp. 8227-8234
    • Davies, K.J.A.1    Goldberg, A.L.2
  • 19
    • 0019831686 scopus 로고
    • Alterations in erythrocyte membrane fluidity by phenylhydrazine-induced peroxidation of lipids
    • Evans C. R., Hochstein P.: Alterations in erythrocyte membrane fluidity by phenylhydrazine-induced peroxidation of lipids. Biochem. Biophys. Res. Commun., 1981, 100, 1537-1542.
    • (1981) Biochem. Biophys. Res. Commun. , vol.100 , pp. 1537-1542
    • Evans, C.R.1    Hochstein, P.2
  • 20
    • 0022975889 scopus 로고
    • Red blood cells contain a pathway for the degradation of oxidant damaged hemoglobin that does not require atp or ubiquitin
    • Fagan J. M., Waxman L., Goldberg A. L.: Red blood cells contain a pathway for the degradation of oxidant damaged hemoglobin that does not require ATP or ubiquitin. J. Biol. Chem., 1986, 261, 5705-5713.
    • (1986) J. Biol. Chem. , vol.261 , pp. 5705-5713
    • Fagan, J.M.1    Waxman, L.2    Goldberg, A.L.3
  • 21
    • 0344710499 scopus 로고
    • Inactivation of key metabolic enzymes by mixed function oxidation reactions: Possible implication in protein turnover and aging
    • Fucci L., Oliver C. N., Coon M. J., Stadman E. R.: Inactivation of key metabolic enzymes by mixed function oxidation reactions: possible implication in protein turnover and aging. Proc. Nat. Acad. Sci. USA, 1983, 80, 1521-1525.
    • (1983) Proc. Nat. Acad. Sci. USA , vol.80 , pp. 1521-1525
    • Fucci, L.1    Oliver, C.N.2    Coon, M.J.3    Stadman, E.R.4
  • 22
    • 0020031293 scopus 로고
    • Oxidized proteins in erythrocytes are rapidly degraded by the adenosine-triphosphate-dependent proteolytic system
    • Goldberg A. L., Boches F. S.: Oxidized proteins in erythrocytes are rapidly degraded by the adenosine-triphosphate-dependent proteolytic system. Science, 1982, 215, 1107-1109.
    • (1982) Science , vol.215 , pp. 1107-1109
    • Goldberg, A.L.1    Boches, F.S.2
  • 23
    • 0018091301 scopus 로고
    • Spectrin as a stabilizer of the phospholipid asymmetry in the human erythrocyte membrane
    • Haest C. W. M., Plasa G., Kamp D., Deuticke B.: Spectrin as a stabilizer of the phospholipid asymmetry in the human erythrocyte membrane. Biochim. Biophys. Acta, 1978, 509, 21-32.
    • (1978) Biochim. Biophys. Acta , vol.509 , pp. 21-32
    • Haest, C.W.M.1    Plasa, G.2    Kamp, D.3    Deuticke, B.4
  • 24
    • 0020022916 scopus 로고
    • Mechanisms of intracellular protein breakdown
    • Hershko A., Ciechanover A.: Mechanisms of intracellular protein breakdown. Annu. Rev. Biochem., 1982, 51, 335-364.
    • (1982) Annu. Rev. Biochem. , vol.51 , pp. 335-364
    • Hershko, A.1    Ciechanover, A.2
  • 25
    • 0024286763 scopus 로고
    • Hydroperoxide-mediated fragmentation of proteins
    • Hunt J. V., Simpson J. A., Dean R. T.: Hydroperoxide-mediated fragmentation of proteins. Biochem. J., 1988, 250, 87-93.
    • (1988) Biochem. J. , vol.250 , pp. 87-93
    • Hunt, J.V.1    Simpson, J.A.2    Dean, R.T.3
  • 26
    • 0021324990 scopus 로고
    • The accumulation of malonyldialdehyde, a product of fatty acid peroxidation, can disturb amino phospholipid organization in the membrane bilayer of human erythrocytes
    • Jain S. K.: The accumulation of malonyldialdehyde, a product of fatty acid peroxidation, can disturb amino phospholipid organization in the membrane bilayer of human erythrocytes. J. Biol. Chem., 1984, 259, 3391-3394.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3391-3394
    • Jain, S.K.1
  • 27
    • 0022390631 scopus 로고
    • In vivo externalization of phosphatidylserine and phosphatidylethanolamine in the membrane bilayer and hydrocoagulability by the lipid peroxidation of erythrocyte in rats
    • Jain S. K.: In vivo externalization of phosphatidylserine and phosphatidylethanolamine in the membrane bilayer and hydrocoagulability by the lipid peroxidation of erythrocyte in rats. J. Clin. Invest., 1985, 76, 281-286.
    • (1985) J. Clin. Invest. , vol.76 , pp. 281-286
    • Jain, S.K.1
  • 28
    • 0019272262 scopus 로고
    • Membrane alterations in phenylhydrazine-induced reticulocytes
    • Jain S. K., Hochstein P.: Membrane alterations in phenylhydrazine-induced reticulocytes. Arch. Biochem. Biophys., 1980, 201, 683-687.
    • (1980) Arch. Biochem. Biophys. , vol.201 , pp. 683-687
    • Jain, S.K.1    Hochstein, P.2
  • 29
    • 0019450954 scopus 로고
    • Calcium potentiates the peroxidation of erythrocyte membrane lipids
    • Jain S. K., Sohet S. B.: Calcium potentiates the peroxidation of erythrocyte membrane lipids. Biochim. Biophys. Acta, 1981, 642, 46-54.
    • (1981) Biochim. Biophys. Acta , vol.642 , pp. 46-54
    • Jain, S.K.1    Sohet, S.B.2
  • 30
    • 0030966961 scopus 로고    scopus 로고
    • Oxidative damage does not alter membrane phospholipid asymmetry in human erythrocytes
    • Jong K. de, Geldwerth D., Kuypers F. A.: Oxidative damage does not alter membrane phospholipid asymmetry in human erythrocytes. Biochemistry, 1997, 36, 6768-6776.
    • (1997) Biochemistry , vol.36 , pp. 6768-6776
    • De Jong, K.1    Geldwerth, D.2    Kuypers, F.A.3
  • 31
    • 0344042245 scopus 로고
    • Exposure of erythrocytes to peroxide or superoxide stimulates the degradation of cellular protein
    • Kirschner R. J., Goldberg A. L.: Exposure of erythrocytes to peroxide or superoxide stimulates the degradation of cellular protein. Fed. Proc., 1982, 41, 865.
    • (1982) Fed. Proc. , vol.41 , pp. 865
    • Kirschner, R.J.1    Goldberg, A.L.2
  • 32
    • 0020569163 scopus 로고
    • Red cell membrane abnormalities in chronic myeloid leukaemia
    • Kumar A., Gupta C. M.: Red cell membrane abnormalities in chronic myeloid leukaemia. Nature, 1983, 303, 632-633.
    • (1983) Nature , vol.303 , pp. 632-633
    • Kumar, A.1    Gupta, C.M.2
  • 34
    • 0019555585 scopus 로고
    • Turnover of bacterial glutaminisynthetase: Oxidative inactivation precedes proteolysis
    • Levine R. L., Oliver C. N., Fulks R. N., Stadtman E. R.: Turnover of bacterial glutaminisynthetase: oxidative inactivation precedes proteolysis. Proc. Nat. Acad. Sci. USA, 1981, 78, 2120-2124.
    • (1981) Proc. Nat. Acad. Sci. USA , vol.78 , pp. 2120-2124
    • Levine, R.L.1    Oliver, C.N.2    Fulks, R.N.3    Stadtman, E.R.4
  • 35
    • 0022498102 scopus 로고
    • Site-specific modification of albumin by free radicals. Reaction with copper (II) and ascorbate
    • Marx G., Chevion M.: Site-specific modification of albumin by free radicals. Reaction with copper (II) and ascorbate. Biochem. J., 1985, 236, 397-400.
    • (1985) Biochem. J. , vol.236 , pp. 397-400
    • Marx, G.1    Chevion, M.2
  • 36
    • 0002015313 scopus 로고
    • Ed. Pryar W. B., Academic Press, New York
    • Mead J.C.: In: Free Radicals in Biology. Ed. Pryar W. B., Academic Press, New York, 1976, Vol. I, 53-68.
    • (1976) Free Radicals in Biology , vol.1 , pp. 53-68
    • Mead, J.C.1
  • 39
    • 0344683171 scopus 로고
    • Improved procedure for the extraction of lipids from human erythrocytes
    • Rose H. G., Oklander M.: Improved procedure for the extraction of lipids from human erythrocytes. J. Lipid Res., 1965, 6, 428-431.
    • (1965) J. Lipid Res. , vol.6 , pp. 428-431
    • Rose, H.G.1    Oklander, M.2
  • 40
    • 0023901506 scopus 로고
    • Human erythrocyte protein 4.1 is a phosphatidylserine binding protein
    • Rybicki A., Heath R., Lubin B., Schwartz R.: Human erythrocyte protein 4.1 is a phosphatidylserine binding protein. J. Clin. Invest., 1988, 81, 255-260.
    • (1988) J. Clin. Invest. , vol.81 , pp. 255-260
    • Rybicki, A.1    Heath, R.2    Lubin, B.3    Schwartz, R.4
  • 41
    • 0026423662 scopus 로고
    • Transbilayered movement of phospholipids in red cell and platelet membranes
    • Schroit A. J., Zwaal R. F. A.: Transbilayered movement of phospholipids in red cell and platelet membranes. Biochim. Biophys. Acta, 1991, 1071, 313-329.
    • (1991) Biochim. Biophys. Acta , vol.1071 , pp. 313-329
    • Schroit, A.J.1    Zwaal, R.F.A.2
  • 42
    • 0019834266 scopus 로고
    • Abnormal erythrocyte calcium homeostasis in oxidant-induced hemolytic disease
    • Shalev O., Leida M. N., Hebbel R. P., Jacob M. S., Eaton J. W.: Abnormal erythrocyte calcium homeostasis in oxidant-induced hemolytic disease. Blood, 1981, 58, 1232-1235.
    • (1981) Blood , vol.58 , pp. 1232-1235
    • Shalev, O.1    Leida, M.N.2    Hebbel, R.P.3    Jacob, M.S.4    Eaton, J.W.5
  • 43
    • 0021112881 scopus 로고
    • The analogous mechanisms of enzymatic inactivation induced by ascorbate and superoxide in the presence of copper
    • Shinar E., Navok T., Chevion M.: The analogous mechanisms of enzymatic inactivation induced by ascorbate and superoxide in the presence of copper. J. Biol. Chem., 1983, 258, 14778-14783.
    • (1983) J. Biol. Chem. , vol.258 , pp. 14778-14783
    • Shinar, E.1    Navok, T.2    Chevion, M.3
  • 44
    • 0024078249 scopus 로고
    • Free-radical generation by copper ions and hydrogen peroxide
    • Simpson J. A., Cheeseman K. H., Smith S. E., Dean R. T.: Free-radical generation by copper ions and hydrogen peroxide. Biochem. J., 1988, 254, 519-523.
    • (1988) Biochem. J. , vol.254 , pp. 519-523
    • Simpson, J.A.1    Cheeseman, K.H.2    Smith, S.E.3    Dean, R.T.4
  • 45
    • 0022408547 scopus 로고
    • Effect of hydrogen peroxide exposure on normal human erythrocyte deformability, morphology, surface characteristics, and spectrin hemoglobin cross-linking
    • Synder L. M., Fortier N. L., Trainor J., Jacob S. J., Leb L., Lubin B., Chiu D., Shohet S., Mohandas N.: Effect of hydrogen peroxide exposure on normal human erythrocyte deformability, morphology, surface characteristics, and spectrin hemoglobin cross-linking. J. Clin. Invest., 1985, 76, 1971-1977.
    • (1985) J. Clin. Invest. , vol.76 , pp. 1971-1977
    • Synder, L.M.1    Fortier, N.L.2    Trainor, J.3    Jacob, S.J.4    Leb, L.5    Lubin, B.6    Chiu, D.7    Shohet, S.8    Mohandas, N.9
  • 46
    • 0021139803 scopus 로고
    • Vanadate inhibits the ATP-dependent degradation of proteins in reticulocytes without affecting ubiquitin conjugation
    • Tanaka K., Waxman L., Goldberg A. L.: Vanadate inhibits the ATP-dependent degradation of proteins in reticulocytes without affecting ubiquitin conjugation. J. Biol. Chem., 1984, 259, 2803-2809.
    • (1984) J. Biol. Chem. , vol.259 , pp. 2803-2809
    • Tanaka, K.1    Waxman, L.2    Goldberg, A.L.3
  • 47
    • 0021144921 scopus 로고
    • Reaction of phenylhydrazine with erythrocytes cross-linking of spectrin by disulfide exchange with oxidized hemoglobin
    • Vilsen B., Nielsen H.: Reaction of phenylhydrazine with erythrocytes cross-linking of spectrin by disulfide exchange with oxidized hemoglobin. Biochem. Pharmacol., 1984, 33, 2739-2748.
    • (1984) Biochem. Pharmacol. , vol.33 , pp. 2739-2748
    • Vilsen, B.1    Nielsen, H.2
  • 48
    • 0000569087 scopus 로고
    • A fluorometric method for the estimation of tyrosine in plasma and tissues
    • Waalkes T. P., Udenfriend S.: A fluorometric method for the estimation of tyrosine in plasma and tissues. J. Lab. Clin. Med., 1957, 50, 733-736.
    • (1957) J. Lab. Clin. Med. , vol.50 , pp. 733-736
    • Waalkes, T.P.1    Udenfriend, S.2
  • 49
    • 0020357482 scopus 로고
    • Involvement of spectrin in the maintainance of phase-state asymmetry in the erythrocyte membrane
    • Williamson P., Bateman J., Kozarsky K., Mattocks K., Hermanowicz N., Choe H., Schlegel R.A.: Involvement of spectrin in the maintainance of phase-state asymmetry in the erythrocyte membrane. Cell, 1982, 30, 725-733.
    • (1982) Cell , vol.30 , pp. 725-733
    • Williamson, P.1    Bateman, J.2    Kozarsky, K.3    Mattocks, K.4    Hermanowicz, N.5    Choe, H.6    Schlegel, R.A.7
  • 50
    • 0022451471 scopus 로고
    • Fragmentation of proteins by free radicals and its effect on their susceptibility to enzymic hydrolysis
    • Wolff S. P., Dean R. T.: Fragmentation of proteins by free radicals and its effect on their susceptibility to enzymic hydrolysis. Biochem. J., 1986, 234, 397-403.
    • (1986) Biochem. J. , vol.234 , pp. 397-403
    • Wolff, S.P.1    Dean, R.T.2
  • 51
    • 0026688548 scopus 로고
    • Platelet procoagulant activity of microvesicle formation, its putative role in hemostasis and thrombosis
    • Zwaal R. F. A., Confurius P., Bevers E. M.: Platelet procoagulant activity of microvesicle formation, its putative role in hemostasis and thrombosis. Biochim. Biophys. Acta, 1992, 1180, 1-8.
    • (1992) Biochim. Biophys. Acta , vol.1180 , pp. 1-8
    • Zwaal, R.F.A.1    Confurius, P.2    Bevers, E.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.