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Volumn 224, Issue 1-3, 2008, Pages 1-8

Oxidative effects of gemfibrozil on anion influx and metabolism in normal and beta-thalassemic erythrocytes: Physiological implications

Author keywords

Anion transport; Band 3 protein; Beta thalassemia; Caspase 3; Erythrocyte; Gemfibrozil; Glucose 6 phosphate metabolism

Indexed keywords

CASPASE 3; ERYTHROCYTE BAND 3 PROTEIN; GEMFIBROZIL; ORTHOVANADIC ACID; TERT BUTYL HYDROPEROXIDE;

EID: 52349112250     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00232-008-9122-8     Document Type: Article
Times cited : (19)

References (42)
  • 2
    • 5644292299 scopus 로고    scopus 로고
    • Analysis of erythrocyte and platelet membrane proteins in various forms of β-thalassemia
    • GA Alekperova AG Orudzhev SA Javadov 2004 Analysis of erythrocyte and platelet membrane proteins in various forms of β-thalassemia Biochemistry 69 748 753
    • (2004) Biochemistry , vol.69 , pp. 748-753
    • Alekperova, G.A.1    Orudzhev, A.G.2    Javadov, S.A.3
  • 3
    • 0029095032 scopus 로고
    • Functional link between phosphorylation state of membrane proteins and morphological changes of human erythrocytes
    • L Bordin G Clari I Moro F Dalla Vacchia V Moret 1995 Functional link between phosphorylation state of membrane proteins and morphological changes of human erythrocytes Biochem Biophys Res Commun 213 249 257
    • (1995) Biochem Biophys Res Commun , vol.213 , pp. 249-257
    • Bordin, L.1    Clari, G.2    Moro, I.3    Dalla Vacchia, F.4    Moret, V.5
  • 4
    • 0032054340 scopus 로고    scopus 로고
    • The molecular pathobiology of cell membrane iron: The sickle red cell as a model
    • P Browne O Shalev R Hebbel 1998 The molecular pathobiology of cell membrane iron: the sickle red cell as a model Free Radic Biol Med 24 1040 1048
    • (1998) Free Radic Biol Med , vol.24 , pp. 1040-1048
    • Browne, P.1    Shalev, O.2    Hebbel, R.3
  • 5
    • 0034663190 scopus 로고    scopus 로고
    • Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: Identification of primary and secondary phosphorylation sites
    • AM Brunati L Bordin G Clari P James M Quadroni E Baritono LA Pinna A Donella-Deana 2000 Sequential phosphorylation of protein band 3 by Syk and Lyn tyrosine kinases in intact human erythrocytes: identification of primary and secondary phosphorylation sites Blood 96 1550 1557
    • (2000) Blood , vol.96 , pp. 1550-1557
    • Brunati, A.M.1    Bordin, L.2    Clari, G.3    James, P.4    Quadroni, M.5    Baritono, E.6    Pinna, L.A.7    Donella-Deana, A.8
  • 6
    • 0033057033 scopus 로고    scopus 로고
    • Metabolic indicators of oxidative stress correlate with haemichrome attachment to membrane, band 3 aggregation and erythrophagocytosis in β thalassemia intermedia erythrocytes
    • MD Cappellini D Tavazzi L Duca G Graziadei E Mannu F Turrini P Arese G Fiorelli 1999 Metabolic indicators of oxidative stress correlate with haemichrome attachment to membrane, band 3 aggregation and erythrophagocytosis in β thalassemia intermedia erythrocytes Br J Haematol 104 504 512
    • (1999) Br J Haematol , vol.104 , pp. 504-512
    • Cappellini, M.D.1    Tavazzi, D.2    Duca, L.3    Graziadei, G.4    Mannu, E.5    Turrini, F.6    Arese, P.7    Fiorelli, G.8
  • 9
    • 33847791754 scopus 로고    scopus 로고
    • Amyloid-beta peptide affects the oxygen dependence of erythrocyte metabolism: A role for caspase 3
    • ME Clementi B Giardina D Colucci A Galtieri F Misiti 2007 Amyloid-beta peptide affects the oxygen dependence of erythrocyte metabolism: a role for caspase 3 Int J Biochem Cell Biol 39 727 735
    • (2007) Int J Biochem Cell Biol , vol.39 , pp. 727-735
    • Clementi, M.E.1    Giardina, B.2    Colucci, D.3    Galtieri, A.4    Misiti, F.5
  • 11
    • 0034929864 scopus 로고    scopus 로고
    • Mechanisms of N-acetylcysteine in the prevention of DNA damage and cancer, with special reference to smoking-related end-points
    • S De Flora A Izzotti F D'Agostini RM Balansky 2001 Mechanisms of N-acetylcysteine in the prevention of DNA damage and cancer, with special reference to smoking-related end-points Carcinogenesis 22 999 1013
    • (2001) Carcinogenesis , vol.22 , pp. 999-1013
    • De Flora, S.1    Izzotti, A.2    D'Agostini, F.3    Balansky, R.M.4
  • 12
    • 34447557859 scopus 로고    scopus 로고
    • The plasma membrane of erythrocytes plays a fundamental role in the maintenance of the reduced state of the heme iron
    • MC De Rosa C Carelli Alinovi A Galtieri R Scatena B Giardina 2007 The plasma membrane of erythrocytes plays a fundamental role in the maintenance of the reduced state of the heme iron Gene 398 162 171
    • (2007) Gene , vol.398 , pp. 162-171
    • De Rosa, M.C.1    Carelli Alinovi, C.2    Galtieri, A.3    Scatena, R.4    Giardina, B.5
  • 13
    • 42149193219 scopus 로고    scopus 로고
    • Allosteric properties of hemoglobin and the plasma membrane of the erythrocyte: New insights in gas transport and metabolic modulation
    • MC De Rosa C Carelli Alinovi A Galtieri A Russo B Giardina 2008 Allosteric properties of hemoglobin and the plasma membrane of the erythrocyte: new insights in gas transport and metabolic modulation IUBMB Life 60 87 93
    • (2008) IUBMB Life , vol.60 , pp. 87-93
    • De Rosa, M.C.1    Carelli Alinovi, C.2    Galtieri, A.3    Russo, A.4    Giardina, B.5
  • 14
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • W Droge 2002 Free radicals in the physiological control of cell function Physiol Rev 82 47 95
    • (2002) Physiol Rev , vol.82 , pp. 47-95
    • Droge, W.1
  • 15
    • 0023232216 scopus 로고
    • Helsinki Heart Study: Primary-prevention trial with gemfibrozil in middle-aged men with dyslipidemia. Safety of treatment, changes in risk factors, and incidence of coronary heart disease
    • MH Frick O Elo K Haapa OP Heinonen P Heinsalmi P Helo JK Huttunen P Kaitaniemi P Koskinen V Manninen 1987 Helsinki Heart Study: primary-prevention trial with gemfibrozil in middle-aged men with dyslipidemia. Safety of treatment, changes in risk factors, and incidence of coronary heart disease N Engl J Med 317 1237 1245
    • (1987) N Engl J Med , vol.317 , pp. 1237-1245
    • Frick, M.H.1    Elo, O.2    Haapa, K.3    Heinonen, O.P.4    Heinsalmi, P.5    Helo, P.6    Huttunen, J.K.7    Kaitaniemi, P.8    Koskinen, P.9    Manninen, V.10
  • 18
    • 0021229546 scopus 로고
    • Modification of the haemoglobin oxygen dissociation curve in whole blood by a compound with dual action
    • RM Hyde DJ Livingstone RA Patterson JF Batchelor WR King 1984 Modification of the haemoglobin oxygen dissociation curve in whole blood by a compound with dual action Lancet 2 15 16
    • (1984) Lancet , vol.2 , pp. 15-16
    • Hyde, R.M.1    Livingstone, D.J.2    Patterson, R.A.3    Batchelor, J.F.4    King, W.R.5
  • 19
    • 0017811290 scopus 로고
    • Cross-linking of red blood cell membrane proteins induced by oxidative stress in beta thalassemia
    • I Kahane A Shifter EA Rachmilewitz 1978 Cross-linking of red blood cell membrane proteins induced by oxidative stress in beta thalassemia FEBS Lett 85 267 270
    • (1978) FEBS Lett , vol.85 , pp. 267-270
    • Kahane, I.1    Shifter, A.2    Rachmilewitz, E.A.3
  • 21
    • 12744260687 scopus 로고    scopus 로고
    • R-state hemoglobin bound to heterotropic effectors: Model of the DPG, IHP, and RSR 13 binding sites
    • M Laberge I Kovesi T Yonetani J Fidy 2005 R-state hemoglobin bound to heterotropic effectors: model of the DPG, IHP, and RSR 13 binding sites FEBS Lett 579 627 635
    • (2005) FEBS Lett , vol.579 , pp. 627-635
    • Laberge, M.1    Kovesi, I.2    Yonetani, T.3    Fidy, J.4
  • 23
    • 0037181167 scopus 로고    scopus 로고
    • Caspase 3 regulates phosphatidylserine externalization and phagocitosis of oxidatively stressed erythrocytes
    • D Mandal PK Moitra S Saha J Basu 2002 Caspase 3 regulates phosphatidylserine externalization and phagocitosis of oxidatively stressed erythrocytes FEBS 513 184 188
    • (2002) FEBS , vol.513 , pp. 184-188
    • Mandal, D.1    Moitra, P.K.2    Saha, S.3    Basu, J.4
  • 24
    • 0347993072 scopus 로고    scopus 로고
    • Caspase 3-mediated proteolysis of the N-terminal cytoplasmic domain of the human erythroid anion exchanger 1 (band 3)
    • D Mandal V Baudin-Creuza A Bhattacharyya S Pathak J Delaunay M Kundu J Basu 2003 Caspase 3-mediated proteolysis of the N-terminal cytoplasmic domain of the human erythroid anion exchanger 1 (band 3) J Biol Chem 278 52551 52558
    • (2003) J Biol Chem , vol.278 , pp. 52551-52558
    • Mandal, D.1    Baudin-Creuza, V.2    Bhattacharyya, A.3    Pathak, S.4    Delaunay, J.5    Kundu, M.6    Basu, J.7
  • 29
    • 3242735024 scopus 로고    scopus 로고
    • Hydrogen-peroxide-induced heme degradation in red blood cells: The protective roles of catalase and glutathione peroxidase
    • E Nagababu FJ Chrest JM Rifkind 2003 Hydrogen-peroxide-induced heme degradation in red blood cells: the protective roles of catalase and glutathione peroxidase Biochim Biophys Acta 1620 211 217
    • (2003) Biochim Biophys Acta , vol.1620 , pp. 211-217
    • Nagababu, E.1    Chrest, F.J.2    Rifkind, J.M.3
  • 30
    • 0020959160 scopus 로고
    • Bezafibrate lowers oxygen affinity of hemoglobin
    • MF Perutz C Poyart 1983 Bezafibrate lowers oxygen affinity of hemoglobin Lancet 2 881 882
    • (1983) Lancet , vol.2 , pp. 881-882
    • Perutz, M.F.1    Poyart, C.2
  • 31
    • 0022634647 scopus 로고
    • Hemoglobin as a receptor of drugs and peptides: X-ray studies of the stereochemistry of binding
    • MF Perutz G Fermi DJ Abraham C Poyart E Bursaux 1986 Hemoglobin as a receptor of drugs and peptides: X-ray studies of the stereochemistry of binding J Am Chem Soc 108 1064 1078
    • (1986) J Am Chem Soc , vol.108 , pp. 1064-1078
    • Perutz, M.F.1    Fermi, G.2    Abraham, D.J.3    Poyart, C.4    Bursaux, E.5
  • 35
    • 0037064138 scopus 로고    scopus 로고
    • Crystal structure of horse carbon monoxyhemoglobin-bezafibrate complex at 1.55-A resolution
    • N Shibayama S Miura JRH Tame T Yonetani SY Park 2002 Crystal structure of horse carbon monoxyhemoglobin-bezafibrate complex at 1.55-A resolution J Biol Chem 277 38791 38796
    • (2002) J Biol Chem , vol.277 , pp. 38791-38796
    • Shibayama, N.1    Miura, S.2    Tame, J.R.H.3    Yonetani, T.4    Park, S.Y.5
  • 36
    • 36148998364 scopus 로고    scopus 로고
    • Participation of caspase 3 like protease in oxidation induced impairment of erythrocyte membrane properties
    • Y Suzuki N Ohkubo M Aoto N Meada I Cicha T Miki N Mitsuda 2007 Participation of caspase 3 like protease in oxidation induced impairment of erythrocyte membrane properties Biorheology 44 179 190
    • (2007) Biorheology , vol.44 , pp. 179-190
    • Suzuki, Y.1    Ohkubo, N.2    Aoto, M.3    Meada, N.4    Cicha, I.5    Miki, T.6    Mitsuda, N.7
  • 39
    • 0037054844 scopus 로고    scopus 로고
    • Heterotropic effectors control the hemoglobin function by interacting with its T and R states, a new view on the principle of allostery
    • A Tsuneshige S Park T Yonetani 2002 Heterotropic effectors control the hemoglobin function by interacting with its T and R states, a new view on the principle of allostery Biophys Chem 98 49 63
    • (2002) Biophys Chem , vol.98 , pp. 49-63
    • Tsuneshige, A.1    Park, S.2    Yonetani, T.3
  • 41
    • 0026005327 scopus 로고
    • Absorption spectra of human fetal and adult oxyhemoglobin, de-oxyhemoglobin, carboxyhemoglobin and methemoglobin
    • WG Zijlstra A Buursma WP Meeuwsen-Van Der Roest 1991 Absorption spectra of human fetal and adult oxyhemoglobin, de-oxyhemoglobin, carboxyhemoglobin and methemoglobin Clin Chem 37 1633 1638
    • (1991) Clin Chem , vol.37 , pp. 1633-1638
    • Zijlstra, W.G.1    Buursma, A.2    Meeuwsen-Van Der Roest, W.P.3
  • 42
    • 0031005935 scopus 로고    scopus 로고
    • Erythrocyte thiol status regulates band 3 phosphotyrosine level via oxidation/reduction of band 3-associated phosphotyrosine phosphatase
    • Y Zipser A Piade NS Kosower 1997 Erythrocyte thiol status regulates band 3 phosphotyrosine level via oxidation/reduction of band 3-associated phosphotyrosine phosphatase FEBS Lett 406 126 130
    • (1997) FEBS Lett , vol.406 , pp. 126-130
    • Zipser, Y.1    Piade, A.2    Kosower, N.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.