메뉴 건너뛰기




Volumn 51, Issue 11, 2011, Pages 2108-2117

Glutaredoxin 2 knockout increases sensitivity to oxidative stress in mouse lens epithelial cells

Author keywords

Complex I; Free radicals; Glutaredoxin 2; Glutathionylation; Mitochondria; Oxidative stress

Indexed keywords

ADENOSINE TRIPHOSPHATE; GLUTAREDOXIN; GLUTAREDOXIN 2; GLUTATHIONE; HYDROGEN PEROXIDE; MITOCHONDRIAL PROTEIN; PEROXIDASE; RECOMBINANT ENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); THIOREDOXIN; UNCLASSIFIED DRUG;

EID: 80255140367     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2011.09.011     Document Type: Article
Times cited : (64)

References (28)
  • 3
    • 0033795036 scopus 로고    scopus 로고
    • The role of oxidative stress in the pathogenesis of age-related macular degeneration
    • S. Beatty, H. Koh, M. Phil, D. Henson, and M. Boulton The role of oxidative stress in the pathogenesis of age-related macular degeneration Surv. Ophthalmol. 45 2000 115 134
    • (2000) Surv. Ophthalmol. , vol.45 , pp. 115-134
    • Beatty, S.1    Koh, H.2    Phil, M.3    Henson, D.4    Boulton, M.5
  • 4
    • 0042198801 scopus 로고    scopus 로고
    • Redox regulation in the lens
    • DOI 10.1016/S1350-9462(03)00050-8
    • M.F. Lou Redox regulation in the lens Prog. Retin. Eye Res. 22 2003 657 682 (Pubitemid 36936805)
    • (2003) Progress in Retinal and Eye Research , vol.22 , Issue.5 , pp. 657-682
    • Lou, M.F.1
  • 7
    • 0642334387 scopus 로고    scopus 로고
    • The possible physiological function of thioltransferase in cells
    • K. Xing, and M.F. Lou The possible physiological function of thioltransferase in cells FASEB J. 17 2003 2088 2090
    • (2003) FASEB J. , vol.17 , pp. 2088-2090
    • Xing, K.1    Lou, M.F.2
  • 9
    • 0030851732 scopus 로고    scopus 로고
    • Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro
    • DOI 10.1074/jbc.272.41.25935
    • D.A. Davis, F.M. Newcomb, D.W. Starke, D.E. Ott, J.J. Mieyal, and R. Yarchoan Thioltransferase (glutaredoxin) is detected within HIV-1 and can regulate the activity of glutathionylated HIV-1 protease in vitro J. Biol. Chem. 272 1997 25935 25940 (Pubitemid 27438920)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.41 , pp. 25935-25940
    • Davis, D.A.1    Newcomb, F.M.2    Starke, D.W.3    Ott, D.E.4    Mieyal, J.J.5    Yarchoan, R.6
  • 10
    • 77954368172 scopus 로고    scopus 로고
    • The glutaredoxin/glutathione system modulates NF-kappaB activity by glutathionylation of p65 in cinnamaldehyde-treated endothelial cells
    • B.C. Liao, C.W. Hsieh, Y.C. Lin, and B.S. Wung The glutaredoxin/ glutathione system modulates NF-kappaB activity by glutathionylation of p65 in cinnamaldehyde-treated endothelial cells Toxicol. Sci. 116 2010 151 163
    • (2010) Toxicol. Sci. , vol.116 , pp. 151-163
    • Liao, B.C.1    Hsieh, C.W.2    Lin, Y.C.3    Wung, B.S.4
  • 11
    • 33846809031 scopus 로고    scopus 로고
    • Glutathiolation regulates tumor necrosis factor-α-induced caspase-3 cleavage and apoptosis: Key role for glutaredoxin in the death pathway
    • DOI 10.1161/01.RES.0000256089.30318.20, PII 0000301220070202000008
    • S. Pan, and B.C. Berk Glutathiolation regulates tumor necrosis factor-alpha-induced caspase-3 cleavage and apoptosis: key role for glutaredoxin in the death pathway Circ. Res. 100 2007 213 219 (Pubitemid 46208721)
    • (2007) Circulation Research , vol.100 , Issue.2 , pp. 213-219
    • Pan, S.1    Berk, B.C.2
  • 13
    • 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
    • M.R. Fernando, J.M. Lechner, S. Lofgren, V.N. Gladyshev, and M.F. Lou Mitochondrial thioltransferase (glutaredoxin 2) has GSH-dependent and thioredoxin reductase-dependent peroxidase activities in vitro and in lens epithelial cells FASEB J. 20 2006 2645 2647
    • (2006) FASEB J. , vol.20 , pp. 2645-2647
    • Fernando, M.R.1    Lechner, J.M.2    Lofgren, S.3    Gladyshev, V.N.4    Lou, M.F.5
  • 14
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • M.P. Murphy How mitochondria produce reactive oxygen species Biochem. J. 417 2009 1 13
    • (2009) Biochem. J. , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 15
    • 77954525352 scopus 로고    scopus 로고
    • Selenium compounds are substrates for glutaredoxins: A novel pathway for selenium metabolism and a potential mechanism for selenium-mediated cytotoxicity
    • M. Wallenberg, E. Olm, C. Hebert, M. Bjornstedt, and A.P. Fernandes Selenium compounds are substrates for glutaredoxins: a novel pathway for selenium metabolism and a potential mechanism for selenium-mediated cytotoxicity Biochem. J. 429 2010 85 93
    • (2010) Biochem. J. , vol.429 , pp. 85-93
    • Wallenberg, M.1    Olm, E.2    Hebert, C.3    Bjornstedt, M.4    Fernandes, A.P.5
  • 16
    • 34347236921 scopus 로고    scopus 로고
    • Organelle isolation: Functional mitochondria from mouse liver, muscle and cultured filroblasts
    • DOI 10.1038/nprot.2006.478, PII NPROT.2006.478
    • C. Frezza, S. Cipolat, and L. Scorrano Organelle isolation: functional mitochondria from mouse liver, muscle and cultured fibroblasts Nat. Protoc. 2 2007 287 295 (Pubitemid 47040043)
    • (2007) Nature Protocols , vol.2 , Issue.2 , pp. 287-295
    • Frezza, C.1    Cipolat, S.2    Scorrano, L.3
  • 17
    • 49749177569 scopus 로고
    • A colorimetric method for determining low concentrations of mercaptans
    • G.L. Ellman A colorimetric method for determining low concentrations of mercaptans Arch. Biochem. Biophys. 74 1958 443 450
    • (1958) Arch. Biochem. Biophys. , vol.74 , pp. 443-450
    • Ellman, G.L.1
  • 18
    • 0023885730 scopus 로고
    • Glutathione depletion in the lens of galactosemic and diabetic rats
    • M.F. Lou, J.E. Dickerson Jr., R. Garadi, and B.M. York Jr. Glutathione depletion in the lens of galactosemic and diabetic rats Exp. Eye Res. 46 1988 517 530
    • (1988) Exp. Eye Res. , vol.46 , pp. 517-530
    • Lou, M.F.1    Dickerson Jr., J.E.2    Garadi, R.3    York Jr., B.M.4
  • 20
    • 0034641689 scopus 로고    scopus 로고
    • Identification of oxidant-sensitive proteins: TNF-alpha induces protein glutathiolation
    • D.M. Sullivan, N.B. Wehr, M.M. Fergusson, R.L. Levine, and T. Finkel Identification of oxidant-sensitive proteins: TNF-alpha induces protein glutathiolation Biochemistry 39 2000 11121 11128
    • (2000) Biochemistry , vol.39 , pp. 11121-11128
    • Sullivan, D.M.1    Wehr, N.B.2    Fergusson, M.M.3    Levine, R.L.4    Finkel, T.5
  • 21
    • 73349091842 scopus 로고    scopus 로고
    • The role of mitochondria in apoptosis
    • C. Wang, and R.J. Youle The role of mitochondria in apoptosis Annu. Rev. Genet. 43 2009 95 118
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 95-118
    • Wang, C.1    Youle, R.J.2
  • 22
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • DOI 10.1146/annurev.biochem.68.1.383
    • W.C. Earnshaw, L.M. Martins, and S.H. Kaufmann Mammalian caspases: structure, activation, substrates, and functions during apoptosis Annu. Rev. Biochem. 68 1999 383 424 (Pubitemid 29449198)
    • (1999) Annual Review of Biochemistry , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 23
    • 77955556206 scopus 로고    scopus 로고
    • 2-induced cell apoptosis by protecting complex i activity in the mitochondria
    • 2-induced cell apoptosis by protecting complex I activity in the mitochondria Biochim. Biophys. Acta 1797 2010 1705 1715
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1705-1715
    • Wu, H.1    Xing, K.2    Lou, M.F.3
  • 24
    • 70350728795 scopus 로고    scopus 로고
    • Absence of glutaredoxin1 increases lens susceptibility to oxidative stress induced by UVR-B
    • L.M. Meyer, S. Lofgren, Y.S. Ho, M. Lou, A. Wegener, F. Holz, and P. Soderberg Absence of glutaredoxin1 increases lens susceptibility to oxidative stress induced by UVR-B Exp. Eye Res. 89 2009 833 839
    • (2009) Exp. Eye Res. , vol.89 , pp. 833-839
    • Meyer, L.M.1    Lofgren, S.2    Ho, Y.S.3    Lou, M.4    Wegener, A.5    Holz, F.6    Soderberg, P.7
  • 25
    • 34047250626 scopus 로고    scopus 로고
    • Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria
    • DOI 10.1074/jbc.M608179200
    • C. Johansson, K.L. Kavanagh, O. Gileadi, and U. Oppermann Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria J. Biol. Chem. 282 2007 3077 3082 (Pubitemid 47084316)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.5 , pp. 3077-3082
    • Johansson, C.1    Kavanagh, K.L.2    Gileadi, O.3    Oppermann, U.4
  • 26
    • 53449095486 scopus 로고    scopus 로고
    • Effect of thioltransferase (glutaredoxin) deletion on cellular sensitivity to oxidative stress and cell proliferation in lens epithelial cells of thioltransferase knockout mouse
    • S. Lofgren, M.R. Fernando, K.Y. Xing, Y. Wang, C.A. Kuszynski, Y.S. Ho, and M.F. Lou Effect of thioltransferase (glutaredoxin) deletion on cellular sensitivity to oxidative stress and cell proliferation in lens epithelial cells of thioltransferase knockout mouse Invest. Ophthalmol. Vis. Sci. 49 2008 4497 4505
    • (2008) Invest. Ophthalmol. Vis. Sci. , vol.49 , pp. 4497-4505
    • Lofgren, S.1    Fernando, M.R.2    Xing, K.Y.3    Wang, Y.4    Kuszynski, C.A.5    Ho, Y.S.6    Lou, M.F.7
  • 27
    • 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 defense
    • DOI 10.1074/jbc.M408011200
    • S.M. Beer, E.R. Taylor, S.E. Brown, C.C. Dahm, N.J. Costa, M.J. Runswick, and M.P. Murphy Glutaredoxin 2 catalyzes the reversible oxidation and glutathionylation of mitochondrial membrane thiol proteins: implications for mitochondrial redox regulation and antioxidant defense J. Biol. Chem. 279 2004 47939 47951 (Pubitemid 39540945)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.46 , 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    Murphy, M.P.7
  • 28
    • 34248569415 scopus 로고    scopus 로고
    • Site-specific S-glutathiolation of mitochondrial NADH ubiquinone reductase
    • DOI 10.1021/bi602580c
    • C.L. Chen, L. Zhang, A. Yeh, C.A. Chen, K.B. Green-Church, J.L. Zweier, and Y.R. Chen Site-specific S-glutathiolation of mitochondrial NADH ubiquinone reductase Biochemistry 46 2007 5754 5765 (Pubitemid 46764124)
    • (2007) Biochemistry , vol.46 , Issue.19 , pp. 5754-5765
    • Chen, C.-L.1    Zhang, L.2    Yeh, A.3    Chen, C.-A.4    Green-Church, K.B.5    Zweier, J.L.6    Chen, Y.-R.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.