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Volumn 55, Issue 3, 2015, Pages 499-506

Thiol-based regulation of glyceraldehyde-3-phosphate dehydrogenase in blood bank-stored red blood cells: A strategy to counteract oxidative stress

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOSE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; THIOL; ADENINE; ADSOL; CYSTEINE; CYSTINE; ERYTHROCYTE BAND 3 PROTEIN; MANNITOL; SODIUM CHLORIDE; SOLUTION AND SOLUBILITY; THIOL DERIVATIVE;

EID: 84924447697     PISSN: 00411132     EISSN: 15372995     Source Type: Journal    
DOI: 10.1111/trf.12855     Document Type: Article
Times cited : (25)

References (25)
  • 1
    • 14044251591 scopus 로고    scopus 로고
    • Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane
    • Campanella ME, Chu H, Low PS,. Assembly and regulation of a glycolytic enzyme complex on the human erythrocyte membrane. Proc Natl Acad Sci U S A 2005; 102: 2402-2407.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 2402-2407
    • Campanella, M.E.1    Chu, H.2    Low, P.S.3
  • 2
    • 73249136098 scopus 로고    scopus 로고
    • Role of band 3 in regulating metabolic flux of red blood cells
    • Lewis IA, Campanella ME, Markley JL, et-al. Role of band 3 in regulating metabolic flux of red blood cells. Proc Natl Acad Sci U S A 2009; 106: 18515-18520.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 18515-18520
    • Lewis, I.A.1    Campanella, M.E.2    Markley, J.L.3
  • 3
    • 78049408664 scopus 로고    scopus 로고
    • Oxygen-linked modulation of erythrocyte metabolism: State of the art
    • Castagnola M, Messana I, Sanna MT, et-al. Oxygen-linked modulation of erythrocyte metabolism: state of the art. Blood Transfus 2010; 8 (Suppl 3): s53-58.
    • (2010) Blood Transfus , vol.8 , pp. s53-s58
    • Castagnola, M.1    Messana, I.2    Sanna, M.T.3
  • 4
    • 38349184814 scopus 로고    scopus 로고
    • 2 regulation of erythrocyte properties
    • 2 regulation of erythrocyte properties. Blood 2008; 111: 932-938.
    • (2008) Blood , vol.111 , pp. 932-938
    • Chu, H.1    Breite, A.2    Ciraolo, P.3
  • 7
    • 42149193219 scopus 로고    scopus 로고
    • Allosteric properties of hemoglobin and the plasma membrane of the erythrocyte: New insights in gas transport and metabolic modulation
    • De Rosa MC, Carelli Alinovi C, Galtieri A, et-al. Allosteric properties of hemoglobin and the plasma membrane of the erythrocyte: new insights in gas transport and metabolic modulation. IUBMB Life 2008; 60: 87-93.
    • (2008) IUBMB Life , vol.60 , pp. 87-93
    • De Rosa, M.C.1    Carelli Alinovi, C.2    Galtieri, A.3
  • 9
    • 84869872689 scopus 로고    scopus 로고
    • Alterations of red blood cell metabolome during cold liquid storage of erythrocyte concentrates in CPD-SAGM
    • Gevi F, D'Alessandro A, Rinalducci S, et-al. Alterations of red blood cell metabolome during cold liquid storage of erythrocyte concentrates in CPD-SAGM. J Proteomics 2012; 76: 168-180.
    • (2012) J Proteomics , vol.76 , pp. 168-180
    • Gevi, F.1    D'Alessandro, A.2    Rinalducci, S.3
  • 10
    • 0000635608 scopus 로고
    • Erythrocyte metabolism. II. Glucose metabolism and pathways
    • Murphy J,. Erythrocyte metabolism. II. Glucose metabolism and pathways. J Lab Clin Med 1960; 55: 286-302.
    • (1960) J Lab Clin Med , vol.55 , pp. 286-302
    • Murphy, J.1
  • 11
    • 84855214147 scopus 로고    scopus 로고
    • Time-course investigation of SAGM-stored leukocyte-filtered red bood cell concentrates: From metabolism to proteomics
    • D'Alessandro A, D'Amici GM, Vaglio S, et-al. Time-course investigation of SAGM-stored leukocyte-filtered red bood cell concentrates: from metabolism to proteomics. Haematologica 2012; 97: 107-115.
    • (2012) Haematologica , vol.97 , pp. 107-115
    • D'Alessandro, A.1    D'Amici, G.M.2    Vaglio, S.3
  • 12
    • 8844231118 scopus 로고    scopus 로고
    • Metabolic pathway analysis of enzyme-deficient human red blood cells
    • Cakir T, Tacer CS, Ulgen KO,. Metabolic pathway analysis of enzyme-deficient human red blood cells. Biosystems 2004; 78: 49-67.
    • (2004) Biosystems , vol.78 , pp. 49-67
    • Cakir, T.1    Tacer, C.S.2    Ulgen, K.O.3
  • 13
    • 28844437319 scopus 로고
    • A new erythrocytic enzyme defect with hemolytic anemia: Glyceraldehyde-3-phosphate dehydrogenase deficiency
    • Harkness DR,. A new erythrocytic enzyme defect with hemolytic anemia: glyceraldehyde-3-phosphate dehydrogenase deficiency. J Lab Clin Med 1966; 68: 879-880.
    • (1966) J Lab Clin Med , vol.68 , pp. 879-880
    • Harkness, D.R.1
  • 14
    • 64549097266 scopus 로고    scopus 로고
    • Thiol-based redox switches in eukaryotic proteins
    • Brandes N, Schmitt S, Jakob U,. Thiol-based redox switches in eukaryotic proteins. Antioxid Redox Signal 2009; 11: 997-1014.
    • (2009) Antioxid Redox Signal , vol.11 , pp. 997-1014
    • Brandes, N.1    Schmitt, S.2    Jakob, U.3
  • 15
    • 37549072681 scopus 로고    scopus 로고
    • Dynamic rerouting of the carbohydrate flux is key to counteracting oxidative stress
    • Ralser M, Wamelink MM, Kowald A, et-al. Dynamic rerouting of the carbohydrate flux is key to counteracting oxidative stress. J Biol 2007; 6: 10.
    • (2007) J Biol , vol.6 , pp. 10
    • Ralser, M.1    Wamelink, M.M.2    Kowald, A.3
  • 16
    • 79960154426 scopus 로고    scopus 로고
    • Peroxiredoxin-2 as a candidate biomarker to test oxidative stress levels of stored red blood cells under blood bank conditions
    • Rinalducci S, D'Amici GM, Blasi B, et-al. Peroxiredoxin-2 as a candidate biomarker to test oxidative stress levels of stored red blood cells under blood bank conditions. Transfusion 2011; 51: 1439-1449.
    • (2011) Transfusion , vol.51 , pp. 1439-1449
    • Rinalducci, S.1    D'Amici, G.M.2    Blasi, B.3
  • 17
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko A, Tomas H, Havlis J, et-al. In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat Protoc 2006; 1: 2856-2860.
    • (2006) Nat Protoc , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3
  • 18
    • 79956000611 scopus 로고    scopus 로고
    • Proteomic analysis of plasma derived from platelet buffy coats during storage at room temperature. An application of ProteoMiner™ technology
    • Egidi MG, Rinalducci S, Marrocco C, et-al. Proteomic analysis of plasma derived from platelet buffy coats during storage at room temperature. An application of ProteoMiner™ technology. Platelets 2011; 22: 252-269.
    • (2011) Platelets , vol.22 , pp. 252-269
    • Egidi, M.G.1    Rinalducci, S.2    Marrocco, C.3
  • 19
    • 0020478636 scopus 로고
    • Effect of red cell membrane binding on the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase
    • Tsai IH, Murthy SN, Steck TL,. Effect of red cell membrane binding on the catalytic activity of glyceraldehyde-3-phosphate dehydrogenase. J Biol Chem 1982; 257: 1438-1442.
    • (1982) J Biol Chem , vol.257 , pp. 1438-1442
    • Tsai, I.H.1    Murthy, S.N.2    Steck, T.L.3
  • 20
    • 70350091586 scopus 로고    scopus 로고
    • Oxidative modifications of glyceraldehyde-3-phosphate dehydrogenase play a key role in its multiple cellular functions
    • Hwang NR, Yim SH, Kim YM, et-al. Oxidative modifications of glyceraldehyde-3-phosphate dehydrogenase play a key role in its multiple cellular functions. Biochem J 2009; 423: 253-264.
    • (2009) Biochem J , vol.423 , pp. 253-264
    • Hwang, N.R.1    Yim, S.H.2    Kim, Y.M.3
  • 21
    • 79953853832 scopus 로고    scopus 로고
    • Oxidative stress-dependent oligomeric status of erythrocyte peroxiredoxin II (PrxII) during storage under standard blood banking conditions
    • Rinalducci S, D'Amici GM, Blasi B, et-al. Oxidative stress-dependent oligomeric status of erythrocyte peroxiredoxin II (PrxII) during storage under standard blood banking conditions. Biochimie 2011; 93: 845-853.
    • (2011) Biochimie , vol.93 , pp. 845-853
    • Rinalducci, S.1    D'Amici, G.M.2    Blasi, B.3
  • 22
    • 0034121328 scopus 로고    scopus 로고
    • Blood bank conditions and RBCs: The progressive loss of metabolic modulation
    • Messana I, Ferroni L, Misiti F, et-al. Blood bank conditions and RBCs: the progressive loss of metabolic modulation. Transfusion 2000; 40: 353-360.
    • (2000) Transfusion , vol.40 , pp. 353-360
    • Messana, I.1    Ferroni, L.2    Misiti, F.3
  • 23
    • 28844480498 scopus 로고    scopus 로고
    • Thiol redox control via thioredoxin and glutaredoxin systems
    • Holmgren A, Johansson C, Berndt C, et-al. Thiol redox control via thioredoxin and glutaredoxin systems. Biochem Soc Trans 2005; 33: 1375-1377.
    • (2005) Biochem Soc Trans , vol.33 , pp. 1375-1377
    • Holmgren, A.1    Johansson, C.2    Berndt, C.3
  • 24
    • 84869882271 scopus 로고    scopus 로고
    • Effects of pre-storage leukoreduction on stored red blood cells signaling: A time-course evaluation from shape to proteome
    • Antonelou MH, Tzounakas VL, Velentzas AD, et-al. Effects of pre-storage leukoreduction on stored red blood cells signaling: a time-course evaluation from shape to proteome. J Proteomics 2012; 76: 220-238.
    • (2012) J Proteomics , vol.76 , pp. 220-238
    • Antonelou, M.H.1    Tzounakas, V.L.2    Velentzas, A.D.3
  • 25
    • 84872351455 scopus 로고    scopus 로고
    • Identification of the components of a glycolytic enzyme metabolon on the human red blood cell membrane
    • Puchulu-Campanella E, Chu H, Anstee DJ, et-al. Identification of the components of a glycolytic enzyme metabolon on the human red blood cell membrane. J Biol Chem 2013; 288: 848-858.
    • (2013) J Biol Chem , vol.288 , pp. 848-858
    • Puchulu-Campanella, E.1    Chu, H.2    Anstee, D.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.