메뉴 건너뛰기




Volumn 104, Issue 8, 2004, Pages 2565-2573

SOD2-deficiency anemia: Protein oxidation and altered protein expression reveal targets of damage, stress response, and antioxidant responsiveness

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ANTIOXIDANT; CELL PROTEIN; HYDROGEN PEROXIDE; PROTEOME; REACTIVE OXYGEN METABOLITE; SUPEROXIDE; SUPEROXIDE DISMUTASE;

EID: 4944225788     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood-2003-11-3858     Document Type: Article
Times cited : (158)

References (49)
  • 1
    • 0035896748 scopus 로고    scopus 로고
    • Absence of mitochondrial Superoxide dismutase results in a murine hemolytic anemia responsive to therapy with a catalytic antioxidant
    • Friedman JS, Rebel VI, Derby R, et al. Absence of mitochondrial Superoxide dismutase results in a murine hemolytic anemia responsive to therapy with a catalytic antioxidant. J Exp Med. 2001;193: 925-934.
    • (2001) J Exp Med , vol.193 , pp. 925-934
    • Friedman, J.S.1    Rebel, V.I.2    Derby, R.3
  • 2
    • 0036799489 scopus 로고    scopus 로고
    • The genetics of inherited sideroblastic anemias
    • Fleming MD. The genetics of inherited sideroblastic anemias. Semin Hematol. 2002;39:270-281.
    • (2002) Semin Hematol , vol.39 , pp. 270-281
    • Fleming, M.D.1
  • 3
    • 0028148438 scopus 로고
    • X-linked sideroblastic anemia: Identification of the mutation in the erythroid-specific delta-aminolevulinate synthase gene (ALAS2) in the original family described by Cooley
    • Cotter PD, Rucknagel DL, Bishop DF. X-linked sideroblastic anemia: identification of the mutation in the erythroid-specific delta-aminolevulinate synthase gene (ALAS2) in the original family described by Cooley. Blood. 1994;84:3915-3924.
    • (1994) Blood , vol.84 , pp. 3915-3924
    • Cotter, P.D.1    Rucknagel, D.L.2    Bishop, D.F.3
  • 4
    • 0032920837 scopus 로고    scopus 로고
    • Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-linked sideroblastic anemia and ataxia (XLSA/ A)
    • Allikmets R, Raskind WH, Hutchinson A, Schueck ND, Dean M, Koeller DM. Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-linked sideroblastic anemia and ataxia (XLSA/ A). Hum Mol Genet. 1999;8:743-749.
    • (1999) Hum Mol Genet , vol.8 , pp. 743-749
    • Allikmets, R.1    Raskind, W.H.2    Hutchinson, A.3    Schueck, N.D.4    Dean, M.5    Koeller, D.M.6
  • 5
    • 0035868772 scopus 로고    scopus 로고
    • A mutation in a mitochondrial transmembrane protein is responsible for the pleiotropic hematological and skeletal phenotype of flexed-tail (f/f) mice
    • Fleming MD, Campagna DR, Haslett JN, Trenor CC 3rd, Andrews NC. A mutation in a mitochondrial transmembrane protein is responsible for the pleiotropic hematological and skeletal phenotype of flexed-tail (f/f) mice. Genes Dev. 2001;15:652-657.
    • (2001) Genes Dev , vol.15 , pp. 652-657
    • Fleming, M.D.1    Campagna, D.R.2    Haslett, J.N.3    Trenor III, C.C.4    Andrews, N.C.5
  • 6
    • 0018712317 scopus 로고
    • A new syndrome of refractory sideroblastic anemia with vacuolization of marrow precursors and exocrine pancreatic dysfunction
    • Pearson HA, Lobel JS, Kocoshis SA, et al. A new syndrome of refractory sideroblastic anemia with vacuolization of marrow precursors and exocrine pancreatic dysfunction. J Pediatr. 1979;95:976-984.
    • (1979) J Pediatr , vol.95 , pp. 976-984
    • Pearson, H.A.1    Lobel, J.S.2    Kocoshis, S.A.3
  • 7
    • 0031467871 scopus 로고    scopus 로고
    • Heteroplasmic point mutations of mitochondrial DNA affecting subunit I of cytochrome c oxidase in two patients with acquired idiopathic sideroblastic anemia
    • Gattermann N, Retzlaff S, Wang YL, et al. Heteroplasmic point mutations of mitochondrial DNA affecting subunit I of cytochrome c oxidase in two patients with acquired idiopathic sideroblastic anemia. Blood. 1997;90:4961-4972.
    • (1997) Blood , vol.90 , pp. 4961-4972
    • Gattermann, N.1    Retzlaff, S.2    Wang, Y.L.3
  • 8
    • 0030001270 scopus 로고    scopus 로고
    • A heteroplasmic point mutation of mitochondrial tRNALeu(CUN) in non-lymphoid haemopoietic cell lineages from a patient with acquired idiopathic sideroblastic anaemia
    • Gattermann N, Retzlaff S, Wang YL, et al. A heteroplasmic point mutation of mitochondrial tRNALeu(CUN) in non-lymphoid haemopoietic cell lineages from a patient with acquired idiopathic sideroblastic anaemia. Br J Haematol. 1996;93:845-855.
    • (1996) Br J Haematol , vol.93 , pp. 845-855
    • Gattermann, N.1    Retzlaff, S.2    Wang, Y.L.3
  • 9
    • 0032888986 scopus 로고    scopus 로고
    • The MERRF mutation of mitochondrial DNA in the bone marrow of a patient with acquired idiopathic sideroblastic anemia
    • Wang YL, Choi HK, Aul C, Gattermann N, Heinisch J. The MERRF mutation of mitochondrial DNA in the bone marrow of a patient with acquired idiopathic sideroblastic anemia. Am J Hematol. 1999;60:83-84.
    • (1999) Am J Hematol , vol.60 , pp. 83-84
    • Wang, Y.L.1    Choi, H.K.2    Aul, C.3    Gattermann, N.4    Heinisch, J.5
  • 10
    • 0014042534 scopus 로고
    • Reversible sideroblastic anemia caused by chloramphenicol
    • Beck EA, Ziegler G, Schmid R, Ludin H. Reversible sideroblastic anemia caused by chloramphenicol. Acta Haematol. 1967;38:1-10.
    • (1967) Acta Haematol , vol.38 , pp. 1-10
    • Beck, E.A.1    Ziegler, G.2    Schmid, R.3    Ludin, H.4
  • 11
    • 0019072006 scopus 로고
    • Drug-induced mitochondrial damage and sideroblastic change
    • Yunis AA, Salem Z. Drug-induced mitochondrial damage and sideroblastic change. Clin Haematol. 1980;9:607-619.
    • (1980) Clin Haematol , vol.9 , pp. 607-619
    • Yunis, A.A.1    Salem, Z.2
  • 12
    • 0025612762 scopus 로고
    • Anti-tuberculous drugs and sideroblastic anaemia
    • Sharp RA, Lowe JG, Johnston RN. Anti-tuberculous drugs and sideroblastic anaemia. Br J Clin Pract. 1990;44:706-707.
    • (1990) Br J Clin Pract , vol.44 , pp. 706-707
    • Sharp, R.A.1    Lowe, J.G.2    Johnston, R.N.3
  • 14
    • 0029838063 scopus 로고    scopus 로고
    • Neurodegeneration, myocardial injury, and perinatal death in mitochondrial Superoxide dismutase-deficient mice
    • Lebovitz RM, Zhang H, Vogel H, et al. Neurodegeneration, myocardial injury, and perinatal death in mitochondrial Superoxide dismutase-deficient mice. Proc Natl Acad Sci U S A. 1996;93:9782-9787.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 9782-9787
    • Lebovitz, R.M.1    Zhang, H.2    Vogel, H.3
  • 15
    • 0028827252 scopus 로고
    • Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese Superoxide dismutase
    • Li Y, Huang TT, Carlson EJ, et al. Dilated cardiomyopathy and neonatal lethality in mutant mice lacking manganese Superoxide dismutase. Nat Genet. 1995;11:376-381.
    • (1995) Nat Genet , vol.11 , pp. 376-381
    • Li, Y.1    Huang, T.T.2    Carlson, E.J.3
  • 16
    • 13044285432 scopus 로고    scopus 로고
    • Mitochondrial disease in Superoxide dismutase 2 mutant mice
    • Melov S, Coskun P, Patel M, et al. Mitochondrial disease in Superoxide dismutase 2 mutant mice. Proc Natl Acad Sci U S A. 1999;96:846-851.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 846-851
    • Melov, S.1    Coskun, P.2    Patel, M.3
  • 17
    • 0034284973 scopus 로고    scopus 로고
    • Extension of life-span with Superoxide dismutase/catalase mimetics
    • Melov S, Ravenscroft J, Malik S, et al. Extension of life-span with Superoxide dismutase/catalase mimetics. Science. 2000;289:1567-1569.
    • (2000) Science , vol.289 , pp. 1567-1569
    • Melov, S.1    Ravenscroft, J.2    Malik, S.3
  • 18
    • 0035503501 scopus 로고    scopus 로고
    • Lifespan extension and rescue of spongiform encephalopathy in Superoxide dismutase 2 nullizygous mice treated with Superoxide dismutase-catalase mimetics
    • Melov S, Doctrow SR, Schneider JA, et al. Lifespan extension and rescue of spongiform encephalopathy in Superoxide dismutase 2 nullizygous mice treated with Superoxide dismutase-catalase mimetics. J Neurosci. 2001;21:8348-8353.
    • (2001) J Neurosci , vol.21 , pp. 8348-8353
    • Melov, S.1    Doctrow, S.R.2    Schneider, J.A.3
  • 19
    • 0025946254 scopus 로고
    • Direct in vivo biotinylation of erythrocytes as an assay for red cell survival studies
    • Hoffmann-Fezer G, Maschke H, Zeitler HJ, et al. Direct in vivo biotinylation of erythrocytes as an assay for red cell survival studies. Ann Hematol. 1991;63:214-217.
    • (1991) Ann Hematol , vol.63 , pp. 214-217
    • Hoffmann-Fezer, G.1    Maschke, H.2    Zeitler, H.J.3
  • 20
    • 0037040827 scopus 로고    scopus 로고
    • Applied proteomics: Mitochondrial proteins and effect on function
    • Lopez MF, Melov S. Applied proteomics: mitochondrial proteins and effect on function. Circ Res. 2002;90:380-389.
    • (2002) Circ Res , vol.90 , pp. 380-389
    • Lopez, M.F.1    Melov, S.2
  • 21
    • 0036210831 scopus 로고    scopus 로고
    • Multiwell in-gel protein digestion and microscale sample preparation for protein identification by mass spectrometry
    • Pluskal MG, Bogdanova A, Lopez M, Gutierrez S, Pitt AM. Multiwell in-gel protein digestion and microscale sample preparation for protein identification by mass spectrometry. Proteomics. 2002;2: 145-150.
    • (2002) Proteomics , vol.2 , pp. 145-150
    • Pluskal, M.G.1    Bogdanova, A.2    Lopez, M.3    Gutierrez, S.4    Pitt, A.M.5
  • 22
    • 0030905109 scopus 로고    scopus 로고
    • Reproducibility of polypeptide spot positions in two-dimensional gels run using carrier ampholytes in the isoelectric focusing dimension
    • Lopez MF, Patton WF. Reproducibility of polypeptide spot positions in two-dimensional gels run using carrier ampholytes in the isoelectric focusing dimension. Electrophoresis. 1997;18:338-343.
    • (1997) Electrophoresis , vol.18 , pp. 338-343
    • Lopez, M.F.1    Patton, W.F.2
  • 23
    • 0033912405 scopus 로고    scopus 로고
    • Mitochondrial oxidative stress. Physiologic consequences and potential for a role in aging
    • Melov S. Mitochondrial oxidative stress. Physiologic consequences and potential for a role in aging. Ann N Y Acad Sci. 2000;908:219-225.
    • (2000) Ann N Y Acad Sci , vol.908 , pp. 219-225
    • Melov, S.1
  • 24
  • 25
    • 0027183423 scopus 로고
    • Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions
    • Stadtman ER. Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metal-catalyzed reactions. Annu Rev Biochem. 1993;62:797-821.
    • (1993) Annu Rev Biochem , vol.62 , pp. 797-821
    • Stadtman, E.R.1
  • 26
    • 0037033433 scopus 로고    scopus 로고
    • Discrete generation of Superoxide and hydrogen peroxide by T cell receptor stimulation: Selective regulation of mitogen-activated protein kinase activation and fas ligand expression
    • Devadas S, Zaritskaya L, Rhee SG, Oberley L, Williams MS. Discrete generation of Superoxide and hydrogen peroxide by T cell receptor stimulation: selective regulation of mitogen-activated protein kinase activation and fas ligand expression. J Exp Med. 2002;195:59-70.
    • (2002) J Exp Med , vol.195 , pp. 59-70
    • Devadas, S.1    Zaritskaya, L.2    Rhee, S.G.3    Oberley, L.4    Williams, M.S.5
  • 27
    • 0016750343 scopus 로고
    • Red cell iron uptake in hereditary microcytic anemia
    • Edwards JA, Hoke JE. Red cell iron uptake in hereditary microcytic anemia. Blood. 1975;46:381-388.
    • (1975) Blood , vol.46 , pp. 381-388
    • Edwards, J.A.1    Hoke, J.E.2
  • 28
    • 0037428060 scopus 로고    scopus 로고
    • Oxidative stress-induced iron signaling is responsible for peroxide-dependent oxidation of dichlorodihydrofluorescein in endothelial cells: Role of transferrin receptor-dependent iron uptake in apoptosis
    • Tampo Y, Kotamraju S, Chitambar CR, et al. Oxidative stress-induced iron signaling is responsible for peroxide-dependent oxidation of dichlorodihydrofluorescein in endothelial cells: role of transferrin receptor-dependent iron uptake in apoptosis. Circ Res. 2003;92:56-63.
    • (2003) Circ Res , vol.92 , pp. 56-63
    • Tampo, Y.1    Kotamraju, S.2    Chitambar, C.R.3
  • 29
    • 17544367057 scopus 로고    scopus 로고
    • Hemolytic anemia induced by ribavirin therapy in patients with chronic hepatitis C virus infection: Role of membrane oxidative damage
    • De Franceschi L, Fattovich G, Turrini F, et al. Hemolytic anemia induced by ribavirin therapy in patients with chronic hepatitis C virus infection: role of membrane oxidative damage. Hepatology. 2000;31:997-1004.
    • (2000) Hepatology , vol.31 , pp. 997-1004
    • De Franceschi, L.1    Fattovich, G.2    Turrini, F.3
  • 30
    • 0024510178 scopus 로고
    • Stimulation of K-C1 cotransport in rat red cells by a hemolytic anemia-producing metabolite of dapsone
    • Haas M, Harrison JH Jr. Stimulation of K-C1 cotransport in rat red cells by a hemolytic anemia-producing metabolite of dapsone. Am J Physiol. 1989;256:C265-C272.
    • (1989) Am J Physiol , vol.256
    • Haas, M.1    Harrison Jr., J.H.2
  • 32
    • 0027232102 scopus 로고
    • Effect of excess alpha-hemoglobin chains on cellular and membrane oxidation in model beta-thalassemic erythrocytes
    • Scott MD, van den Berg JJ, Repka T, et al. Effect of excess alpha-hemoglobin chains on cellular and membrane oxidation in model beta-thalassemic erythrocytes. J Clin Invest. 1993;91:1706-1712.
    • (1993) J Clin Invest , vol.91 , pp. 1706-1712
    • Scott, M.D.1    Van Den Berg, J.J.2    Repka, T.3
  • 33
    • 0021171846 scopus 로고
    • Increased red blood cell protoporphyrin in thalassemia: A result of relative iron deficiency
    • Pootrakul P, Wattanasaree J, Anuwatanakulchai M, Wasi P. Increased red blood cell protoporphyrin in thalassemia: a result of relative iron deficiency. Am J Clin Pathol. 1984;82:289-293.
    • (1984) Am J Clin Pathol , vol.82 , pp. 289-293
    • Pootrakul, P.1    Wattanasaree, J.2    Anuwatanakulchai, M.3    Wasi, P.4
  • 34
    • 0034213904 scopus 로고    scopus 로고
    • Prohibitins act as a membrane-bound chaperone for the stabilization of mitochondrial proteins
    • Nijtmans LG, de Jong L, Artal Sanz M, et al. Prohibitins act as a membrane-bound chaperone for the stabilization of mitochondrial proteins. EMBO J. 2000;19:2444-2451.
    • (2000) EMBO J , vol.19 , pp. 2444-2451
    • Nijtmans, L.G.1    De Jong, L.2    Artal Sanz, M.3
  • 35
    • 0037113995 scopus 로고    scopus 로고
    • Mitochondrial Hsp60, resistance to oxidative stress, and the labile iron pool are closely connected in Saccharomyces cerevisiae
    • Cabiscol E, Belli G, Tamarit J, Echave P, Herrero E, Ros J. Mitochondrial Hsp60, resistance to oxidative stress, and the labile iron pool are closely connected in Saccharomyces cerevisiae. J Biol Chem. 2002;277:44531-44538.
    • (2002) J Biol Chem , vol.277 , pp. 44531-44538
    • Cabiscol, E.1    Belli, G.2    Tamarit, J.3    Echave, P.4    Herrero, E.5    Ros, J.6
  • 36
    • 0028925757 scopus 로고
    • Cation transport in mouse erythrocytes: Role of K(+)-Cl-cotransport in regulatory volume decrease
    • Armsby CC, Brugnara C, Alper SL. Cation transport in mouse erythrocytes: role of K(+)-Cl-cotransport in regulatory volume decrease. Am J Physiol. 1995;268:C894-C902.
    • (1995) Am J Physiol , vol.268
    • Armsby, C.C.1    Brugnara, C.2    Alper, S.L.3
  • 37
    • 0032579371 scopus 로고    scopus 로고
    • Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress
    • Tamarit J, Cabiscol E, Ros J. Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress. J Biol Chem. 1998;273:3027-3032.
    • (1998) J Biol Chem , vol.273 , pp. 3027-3032
    • Tamarit, J.1    Cabiscol, E.2    Ros, J.3
  • 38
    • 0015237988 scopus 로고
    • Catalysis of methaemoglobin reduction by erythrocyte cytochrome B5 and cytochrome B5 reductase
    • Hultquist DE, Passon PG. Catalysis of methaemoglobin reduction by erythrocyte cytochrome B5 and cytochrome B5 reductase. Nat New Biol. 1971;229:252-254.
    • (1971) Nat New Biol , vol.229 , pp. 252-254
    • Hultquist, D.E.1    Passon, P.G.2
  • 39
    • 0028335565 scopus 로고
    • Cloning and nucleotide sequence of a cDNA of the human erythrocyte NADPH-flavin reductase
    • Chikuba K, Yubisui T, Shirabe K, Takeshita M. Cloning and nucleotide sequence of a cDNA of the human erythrocyte NADPH-flavin reductase. Biochem Biophys Res Commun. 1994;198:1170-1176.
    • (1994) Biochem Biophys Res Commun , vol.198 , pp. 1170-1176
    • Chikuba, K.1    Yubisui, T.2    Shirabe, K.3    Takeshita, M.4
  • 40
    • 0141746553 scopus 로고    scopus 로고
    • Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha
    • Kang SW, Chae HZ, Seo MS, Kim K, Baines IC, Rhee SG. Mammalian peroxiredoxin isoforms can reduce hydrogen peroxide generated in response to growth factors and tumor necrosis factor-alpha. J Biol Chem. 1998;273:6297-6302.
    • (1998) J Biol Chem , vol.273 , pp. 6297-6302
    • Kang, S.W.1    Chae, H.Z.2    Seo, M.S.3    Kim, K.4    Baines, I.C.5    Rhee, S.G.6
  • 41
    • 0036970951 scopus 로고    scopus 로고
    • Numerous proteins in mammalian cells are prone to iron-dependent oxidation and proteasomal degradation
    • Drake SK, Bourdon E, Wehr N, et al. Numerous proteins in mammalian cells are prone to iron-dependent oxidation and proteasomal degradation. Dev Neurosci. 2002;24:114-124.
    • (2002) Dev Neurosci , vol.24 , pp. 114-124
    • Drake, S.K.1    Bourdon, E.2    Wehr, N.3
  • 42
    • 0037205455 scopus 로고    scopus 로고
    • Proteomics analysis of cellular response to oxidative stress: Evidence for in vivo overoxidation of peroxiredoxins at their active site
    • Rabilloud T, Heller M, Gasnier F, et al. Proteomics analysis of cellular response to oxidative stress: evidence for in vivo overoxidation of peroxiredoxins at their active site. J Biol Chem. 2002;277: 19396-19401.
    • (2002) J Biol Chem , vol.277 , pp. 19396-19401
    • Rabilloud, T.1    Heller, M.2    Gasnier, F.3
  • 43
    • 10744233389 scopus 로고    scopus 로고
    • Peroxiredoxin II is essential for sustaining life span of erythrocytes in mice
    • Lee TH, Kim SU, Yu SL, et al. Peroxiredoxin II is essential for sustaining life span of erythrocytes in mice. Blood. 2003;101:5033-5038.
    • (2003) Blood , vol.101 , pp. 5033-5038
    • Lee, T.H.1    Kim, S.U.2    Yu, S.L.3
  • 46
    • 0034054183 scopus 로고    scopus 로고
    • The role of the membrane-bound tumour antigen, melanotransferrin (p97), in iron uptake by the human malignant melanoma cell
    • Richardson DR. The role of the membrane-bound tumour antigen, melanotransferrin (p97), in iron uptake by the human malignant melanoma cell. Eur J Biochem. 2000;267:1290-1298.
    • (2000) Eur J Biochem , vol.267 , pp. 1290-1298
    • Richardson, D.R.1
  • 47
    • 0029897658 scopus 로고    scopus 로고
    • Increased adhesion of erythrocytes to components of the extracellular matrix: Isolation and characterization of a red blood cell lipid that binds thrombospondin and laminin
    • Hillery CA, Du MC, Montgomery RR, Scott JP. Increased adhesion of erythrocytes to components of the extracellular matrix: isolation and characterization of a red blood cell lipid that binds thrombospondin and laminin. Blood. 1996;87: 4879-4886.
    • (1996) Blood , vol.87 , pp. 4879-4886
    • Hillery, C.A.1    Du, M.C.2    Montgomery, R.R.3    Scott, J.P.4
  • 48
    • 0343339958 scopus 로고    scopus 로고
    • Adherence of phosphatidylserine-exposing erythrocytes to endothelial matrix thrombospondin
    • Manodori AB, Barabino GA, Lubin BH, Kuypers FA. Adherence of phosphatidylserine-exposing erythrocytes to endothelial matrix thrombospondin. Blood. 2000;95:1293-1300.
    • (2000) Blood , vol.95 , pp. 1293-1300
    • Manodori, A.B.1    Barabino, G.A.2    Lubin, B.H.3    Kuypers, F.A.4
  • 49
    • 0037113995 scopus 로고    scopus 로고
    • Mitochondrial Hsp60, resistance to oxidative stress, and the labile iron pool are closely connected in Saccharomyces cerevisiae
    • Cabiscol E, Belli G, Tamarit J, Echave P, Herrero E, Ros J. Mitochondrial Hsp60, resistance to oxidative stress, and the labile iron pool are closely connected in Saccharomyces cerevisiae. J Biol Chem. 2002;277:44531-44538.
    • (2002) J Biol Chem , vol.277 , pp. 44531-44538
    • Cabiscol, E.1    Belli, G.2    Tamarit, J.3    Echave, P.4    Herrero, E.5    Ros, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.