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Volumn 44, Issue 2, 2008, Pages 252-260

Retraction notice to "Overexpression of glutaredoxin-2 reduces myocardial cell death by preventing both apoptosis and necrosis" [J. Mol. Cell. Cardiol. 44 (2008) 252-260];Overexpression of glutaredoxin-2 reduces myocardial cell death by preventing both apoptosis and necrosis

Author keywords

Glutaredoxin 2; Heart; Reactive oxygen species; Redox signaling; Transgenic mice

Indexed keywords

GLUTAREDOXIN; GLUTAREDOXIN 2; UNCLASSIFIED DRUG;

EID: 39149138715     PISSN: 00222828     EISSN: 10958584     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2012.08.016     Document Type: Erratum
Times cited : (52)

References (38)
  • 1
    • 33847642071 scopus 로고    scopus 로고
    • Bcl-2 protects against hyperoxia-induced apoptosis through inhibition of the mitochondria-dependent pathway
    • Pagano A., Carnesecchi S., Ody C., Donati Y., and Barazzone A.C. Bcl-2 protects against hyperoxia-induced apoptosis through inhibition of the mitochondria-dependent pathway. Free Radic Biol Med 42 (2007) 1062-1074
    • (2007) Free Radic Biol Med , vol.42 , pp. 1062-1074
    • Pagano, A.1    Carnesecchi, S.2    Ody, C.3    Donati, Y.4    Barazzone, A.C.5
  • 2
    • 33645556312 scopus 로고    scopus 로고
    • Bax translocates to mitochondria of heart cells during simulated ischaemia: involvement of AMP-activated and p38 mitogen-activated protein kinases
    • Capano M., and Crompton M. Bax translocates to mitochondria of heart cells during simulated ischaemia: involvement of AMP-activated and p38 mitogen-activated protein kinases. Biochem J 395 (2006) 57-64
    • (2006) Biochem J , vol.395 , pp. 57-64
    • Capano, M.1    Crompton, M.2
  • 3
    • 34247200969 scopus 로고    scopus 로고
    • RhoA/Rho kinase up-regulate Bax to activate a mitochondrial death pathway and induce cardiomyocyte apoptosis
    • Miyamoto S., and Brown J.H. RhoA/Rho kinase up-regulate Bax to activate a mitochondrial death pathway and induce cardiomyocyte apoptosis. J Biol Chem 282 (2007) 8069-8078
    • (2007) J Biol Chem , vol.282 , pp. 8069-8078
    • Miyamoto, S.1    Brown, J.H.2
  • 5
    • 33745198418 scopus 로고    scopus 로고
    • Redox regulation of cardiac calcium channels and transporters
    • Zima A.V., and Blatter L.A. Redox regulation of cardiac calcium channels and transporters. Cardiovasc Res 71 (2006) 310-321
    • (2006) Cardiovasc Res , vol.71 , pp. 310-321
    • Zima, A.V.1    Blatter, L.A.2
  • 6
    • 33847683419 scopus 로고    scopus 로고
    • Evidence of ROS generation by mitochondria in cells with impaired electron transport chain and mitochondrial DNA damage
    • Indo H.P., Davidson M., Yen H.C., Suenaga S., Tomita K., Nishii T., et al. Evidence of ROS generation by mitochondria in cells with impaired electron transport chain and mitochondrial DNA damage. Mitochondrion 7 (2007) 106-118
    • (2007) Mitochondrion , vol.7 , pp. 106-118
    • Indo, H.P.1    Davidson, M.2    Yen, H.C.3    Suenaga, S.4    Tomita, K.5    Nishii, T.6
  • 7
    • 33847746679 scopus 로고    scopus 로고
    • Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system
    • Berndt C., Lillig C.H., and Holmgren A. Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system. Am J Physiol Heart Circ Physiol 292 (2007) H1227-H1236
    • (2007) Am J Physiol Heart Circ Physiol , vol.292
    • Berndt, C.1    Lillig, C.H.2    Holmgren, A.3
  • 8
    • 0042068217 scopus 로고    scopus 로고
    • Differential role of glutaredoxin and thioredoxin in metabolic oxidative stress-induced activation of apoptosis signal-regulating kinase 1
    • Song J.J., and Lee Y.J. Differential role of glutaredoxin and thioredoxin in metabolic oxidative stress-induced activation of apoptosis signal-regulating kinase 1. Biochem J 373 (2003) 845-885
    • (2003) Biochem J , vol.373 , pp. 845-885
    • Song, J.J.1    Lee, Y.J.2
  • 9
    • 4444337091 scopus 로고    scopus 로고
    • Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide
    • Lillig C.H., Lonn M.E., Enoksson M., Fernandes A.P., and Holmgren A. Short interfering RNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLa cells toward doxorubicin and phenylarsine oxide. Proc Natl Acad Sci U S A 101 (2004) 13227-13232
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 13227-13232
    • Lillig, C.H.1    Lonn, M.E.2    Enoksson, M.3    Fernandes, A.P.4    Holmgren, A.5
  • 10
    • 9144249116 scopus 로고    scopus 로고
    • Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant defence
    • Beer S.M., Taylor E.R., Brown S.E., Dahm C.C., Costa N.J., Runswick M.J., et al. Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant defence. J Biol Chem 279 (2004) 47939-47951
    • (2004) J Biol Chem , vol.279 , pp. 47939-47951
    • Beer, S.M.1    Taylor, E.R.2    Brown, S.E.3    Dahm, C.C.4    Costa, N.J.5    Runswick, M.J.6
  • 11
    • 0008996894 scopus 로고    scopus 로고
    • Overexpression of Bcl-2 attenuates apoptosis and protects against myocardial I/R injury in transgenic mice
    • Chen Z., Chua C.C., Ho Y.-S., Hamdy R.C., and Chua B.H.L. Overexpression of Bcl-2 attenuates apoptosis and protects against myocardial I/R injury in transgenic mice. Am J Physiol Heart Circ Physiol 280 (2001) H2313-H2320
    • (2001) Am J Physiol Heart Circ Physiol , vol.280
    • Chen, Z.1    Chua, C.C.2    Ho, Y.-S.3    Hamdy, R.C.4    Chua, B.H.L.5
  • 12
    • 0026342911 scopus 로고
    • Tissue-specific regulation of the alpha-myosin heavy chain gene promoter in transgenic mice
    • Subramaniam A., Jones W.K., Gulick J., Wert S., Neumann J., and Robbins J. Tissue-specific regulation of the alpha-myosin heavy chain gene promoter in transgenic mice. J Biol Chem 266 (1991) 24613-24620
    • (1991) J Biol Chem , vol.266 , pp. 24613-24620
    • Subramaniam, A.1    Jones, W.K.2    Gulick, J.3    Wert, S.4    Neumann, J.5    Robbins, J.6
  • 14
    • 33744989211 scopus 로고    scopus 로고
    • Attenuation of doxorubicin-induced contractile and mitochondrial dysfunction in mouse heart by cellular glutathione peroxidase
    • Xiong Y., Liu X., Lee C.P., Chua B.H.L., and Ho Y.S. Attenuation of doxorubicin-induced contractile and mitochondrial dysfunction in mouse heart by cellular glutathione peroxidase. Free Radic Biol Med 41 (2006) 46-55
    • (2006) Free Radic Biol Med , vol.41 , pp. 46-55
    • Xiong, Y.1    Liu, X.2    Lee, C.P.3    Chua, B.H.L.4    Ho, Y.S.5
  • 15
    • 0025895933 scopus 로고
    • Thioltransferase in human red blood cells: purification and properties
    • Mieyal J.J., Starke D.W., Gravina S.A., Dothey C., and Chung J.S. Thioltransferase in human red blood cells: purification and properties. Biochemistry 30 (1991) 6088-6097
    • (1991) Biochemistry , vol.30 , pp. 6088-6097
    • Mieyal, J.J.1    Starke, D.W.2    Gravina, S.A.3    Dothey, C.4    Chung, J.S.5
  • 16
    • 0035124724 scopus 로고    scopus 로고
    • Transgene overexpression of alpha B crystallin confers simultaneous protection against cardiomyocyte apoptosis and necrosis during myocardial ischemia and reperfusion
    • Ray P.S., Martin J.L., Swanson E.A., Otani H., Dillman W.H., and Das D.K. Transgene overexpression of alpha B crystallin confers simultaneous protection against cardiomyocyte apoptosis and necrosis during myocardial ischemia and reperfusion. FASEB J 15 (2001) 393-402
    • (2001) FASEB J , vol.15 , pp. 393-402
    • Ray, P.S.1    Martin, J.L.2    Swanson, E.A.3    Otani, H.4    Dillman, W.H.5    Das, D.K.6
  • 17
    • 0038279860 scopus 로고    scopus 로고
    • Thioredoxin redox signaling in the ischemic heart: an insight with transgenic mice overexpressing Trx-1
    • Turoczi T., Chang V.W.H., Engelman R.M., Maulik N., Ho Y.S., and Das D.K. Thioredoxin redox signaling in the ischemic heart: an insight with transgenic mice overexpressing Trx-1. J Mol Cell Cardiol 35 (2003) 695-704
    • (2003) J Mol Cell Cardiol , vol.35 , pp. 695-704
    • Turoczi, T.1    Chang, V.W.H.2    Engelman, R.M.3    Maulik, N.4    Ho, Y.S.5    Das, D.K.6
  • 18
    • 3042511840 scopus 로고    scopus 로고
    • Role of Akt signaling in mitochondrial survival pathway triggered by hypoxic preconditioning
    • Uchiyama T., Engelman R.M., Maulik N., and Das D.K. Role of Akt signaling in mitochondrial survival pathway triggered by hypoxic preconditioning. Circulation 109 (2004) 3042-3049
    • (2004) Circulation , vol.109 , pp. 3042-3049
    • Uchiyama, T.1    Engelman, R.M.2    Maulik, N.3    Das, D.K.4
  • 19
    • 0033066832 scopus 로고    scopus 로고
    • Differential regulation of Bcl-2, AP-1 and NFκB on cardiomyocyte apoptosis during myocardial ischemic stress adaptation
    • Maulik N., Goswami S., Galang N., and Das D.K. Differential regulation of Bcl-2, AP-1 and NFκB on cardiomyocyte apoptosis during myocardial ischemic stress adaptation. FEBS Lett 443 (1999) 331-336
    • (1999) FEBS Lett , vol.443 , pp. 331-336
    • Maulik, N.1    Goswami, S.2    Galang, N.3    Das, D.K.4
  • 20
    • 0029112921 scopus 로고
    • Detection of oxidative stress in heart by estimating the dinitrophenyhydrazine derivative of malonaldehyde
    • Cordis G.A., Maulik N., and Das D.K. Detection of oxidative stress in heart by estimating the dinitrophenyhydrazine derivative of malonaldehyde. J Mol Cell Cardiol 27 (1995) 1645-1650
    • (1995) J Mol Cell Cardiol , vol.27 , pp. 1645-1650
    • Cordis, G.A.1    Maulik, N.2    Das, D.K.3
  • 21
    • 0034306791 scopus 로고    scopus 로고
    • Mitochondrial phospholipid hydroperoxide glutathione peroxidase inhibits the release of cytochrome c from mitochondria by suppressing the peroxidation of cardiolipin in hypoglycaemia-induced apoptosis
    • Nomura K., Imai H., Koumura T., Kobayash T., and Nakagawa Y. Mitochondrial phospholipid hydroperoxide glutathione peroxidase inhibits the release of cytochrome c from mitochondria by suppressing the peroxidation of cardiolipin in hypoglycaemia-induced apoptosis. Biochem J 351 (2000) 183-193
    • (2000) Biochem J , vol.351 , pp. 183-193
    • Nomura, K.1    Imai, H.2    Koumura, T.3    Kobayash, T.4    Nakagawa, Y.5
  • 22
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: a primary site for bcl-2 regulation of apoptosis
    • Kluck R.M., Bossy-wetzel E., Green D.R., and Newmeyer D.D. The release of cytochrome c from mitochondria: a primary site for bcl-2 regulation of apoptosis. Science 275 (1997) 1132-1136
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 23
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner M.O. The biochemistry of apoptosis. Nature 407 (2000) 770-776
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 26
    • 0026603840 scopus 로고
    • Cardiolipins and biomembrane function
    • Hoch F.L. Cardiolipins and biomembrane function. Biochim Biophys Acta 1113 (1992) 71-133
    • (1992) Biochim Biophys Acta , vol.1113 , pp. 71-133
    • Hoch, F.L.1
  • 28
    • 4344661748 scopus 로고    scopus 로고
    • The cardiolipin binding domain of Bid affects mitochondrial respiration and enhances cytochrome c release
    • Liu J., Weiss A., Durrant D., Chi N.-W., and Lee R.M. The cardiolipin binding domain of Bid affects mitochondrial respiration and enhances cytochrome c release. Apoptosis 29 (2004) 533-541
    • (2004) Apoptosis , vol.29 , pp. 533-541
    • Liu, J.1    Weiss, A.2    Durrant, D.3    Chi, N.-W.4    Lee, R.M.5
  • 29
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • Holmgren A. Thioredoxin and glutaredoxin systems. J Biol Chem 264 (1989) 13963-13966
    • (1989) J Biol Chem , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 30
    • 0028804668 scopus 로고
    • Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin
    • Padilla C.A., Martinez-Galisteo E., Barcena J.A., Spyrou G., and Holmgren A. Purification from placenta, amino acid sequence, structure comparisons and cDNA cloning of human glutaredoxin. Eur J Biochem 227 (1995) 27-34
    • (1995) Eur J Biochem , vol.227 , pp. 27-34
    • Padilla, C.A.1    Martinez-Galisteo, E.2    Barcena, J.A.3    Spyrou, G.4    Holmgren, A.5
  • 31
    • 1542320094 scopus 로고    scopus 로고
    • Human mitochondrial glutartedoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase
    • Johansson C., Lillig C.H., and Holmgren A. Human mitochondrial glutartedoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. J Biol Chem 279 (2004) 7537-7543
    • (2004) J Biol Chem , vol.279 , pp. 7537-7543
    • Johansson, C.1    Lillig, C.H.2    Holmgren, A.3
  • 32
    • 0030695902 scopus 로고    scopus 로고
    • Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria
    • Aslund F., Berndt K.D., and Holmgren A. Redox potentials of glutaredoxins and other thiol-disulfide oxidoreductases of the thioredoxin superfamily determined by direct protein-protein redox equilibria. J Biol Chem 272 (1997) 30780-30786
    • (1997) J Biol Chem , vol.272 , pp. 30780-30786
    • Aslund, F.1    Berndt, K.D.2    Holmgren, A.3
  • 33
    • 20444411531 scopus 로고    scopus 로고
    • Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor
    • Lillig C.H., Berndt C., Vergnolle O., Lonn M.E., Hudemann C., Bill E., et al. Characterization of human glutaredoxin 2 as iron-sulfur protein: a possible role as redox sensor. Proc Nat Acad Sci U S A 102 (2005) 8168-8173
    • (2005) Proc Nat Acad Sci U S A , vol.102 , pp. 8168-8173
    • Lillig, C.H.1    Berndt, C.2    Vergnolle, O.3    Lonn, M.E.4    Hudemann, C.5    Bill, E.6
  • 34
    • 33845667283 scopus 로고    scopus 로고
    • Mitochondrial thioltransferase (glutaredoxin 2) has GSH-dependent and thioredoxin reductase-dependent peroxidase activities in vitro and in lens epithelial cells
    • Fernando M.R., Lechner J.M., Lofgren S., Gladyshev V.N., and Lou M.F. Mitochondrial thioltransferase (glutaredoxin 2) has GSH-dependent and thioredoxin reductase-dependent peroxidase activities in vitro and in lens epithelial cells. FASEB J 20 (2006) E2240-E2248
    • (2006) FASEB J , vol.20
    • Fernando, M.R.1    Lechner, J.M.2    Lofgren, S.3    Gladyshev, V.N.4    Lou, M.F.5
  • 35
    • 9144249116 scopus 로고    scopus 로고
    • Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant defence
    • Beer S.M., Taylor E.R., Brown S.E., Dahm C.C., Costa N.J., Runswick M.J., et al. Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant defence. J Biol Chem 279 (2004) 47939-47951
    • (2004) J Biol Chem , vol.279 , pp. 47939-47951
    • Beer, S.M.1    Taylor, E.R.2    Brown, S.E.3    Dahm, C.C.4    Costa, N.J.5    Runswick, M.J.6
  • 36
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: a play in three Akts
    • Datta S.R., Brunet A., and Greenberg M.E. Cellular survival: a play in three Akts. Genes Dev 13 (1999) 2905-2927
    • (1999) Genes Dev , vol.13 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 37
    • 0035877650 scopus 로고    scopus 로고
    • Glutaredoxin protects cerebellar granule neurons from dopamine-induced apoptosis by dual activation of the Ras-phosphoinositide-3-kinase and Jun N-terminal kinase pathways
    • Daily D., Vlamis-Gardikas A., Offen D., Mittelman L., Melamed E., Holmgren A., et al. Glutaredoxin protects cerebellar granule neurons from dopamine-induced apoptosis by dual activation of the Ras-phosphoinositide-3-kinase and Jun N-terminal kinase pathways. J Biol Chem 276 (2001) 21618-21626
    • (2001) J Biol Chem , vol.276 , pp. 21618-21626
    • Daily, D.1    Vlamis-Gardikas, A.2    Offen, D.3    Mittelman, L.4    Melamed, E.5    Holmgren, A.6
  • 38
    • 0033582929 scopus 로고    scopus 로고
    • Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor
    • Brunet A., Bonni A., Zigmond M.J., Lin M.J., Juo P., Hu L.S., et al. Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor. Cell 96 (1999) 857-868
    • (1999) Cell , vol.96 , pp. 857-868
    • Brunet, A.1    Bonni, A.2    Zigmond, M.J.3    Lin, M.J.4    Juo, P.5    Hu, L.S.6


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