메뉴 건너뛰기




Volumn 41, Issue 7, 2006, Pages 663-667

Alterations in mitochondrial and cytosolic methionine sulfoxide reductase activity during cardiac ischemia and reperfusion

Author keywords

Ischemia reperfusion; Methionine sulfoxide reductase; Mitochondria; MsrA; Oxidized protein repair

Indexed keywords

CYSTEINE; METHIONINE; METHIONINE SULFOXIDE; METHIONINE SULFOXIDE REDUCTASE; MITOCHONDRIAL ENZYME; REACTIVE OXYGEN METABOLITE;

EID: 33745060719     PISSN: 05315565     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.exger.2006.03.011     Document Type: Short Survey
Times cited : (42)

References (33)
  • 1
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • Balaban R.S., Nemoto S., and Finkel T. Mitochondria, oxidants, and aging. Cell 120 (2005) 483-495
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 2
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett B.S., and Stadtman E.R. Protein oxidation in aging, disease, and oxidative stress. J. Biol. Chem. 272 (1997) 20313-20316
    • (1997) J. Biol. Chem. , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 3
    • 0242416188 scopus 로고    scopus 로고
    • ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin
    • Biteau B., Labarre J., and Toledano M.B. ATP-dependent reduction of cysteine-sulphinic acid by S. cerevisiae sulphiredoxin. Nature 425 (2003) 980-984
    • (2003) Nature , vol.425 , pp. 980-984
    • Biteau, B.1    Labarre, J.2    Toledano, M.B.3
  • 4
    • 0032923593 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of myocardial stunning
    • Bolli R., and Marban E. Molecular and cellular mechanisms of myocardial stunning. Physiol. Rev. 79 (1999) 609-634
    • (1999) Physiol. Rev. , vol.79 , pp. 609-634
    • Bolli, R.1    Marban, E.2
  • 5
    • 0036713692 scopus 로고    scopus 로고
    • Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
    • Bota D.A., and Davies K.J. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat. Cell. Biol. 4 (2002) 674-680
    • (2002) Nat. Cell. Biol. , vol.4 , pp. 674-680
    • Bota, D.A.1    Davies, K.J.2
  • 6
    • 0037021453 scopus 로고    scopus 로고
    • Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress
    • Bota D.A., Van Remmen H., and Davies K.J. Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress. FEBS Lett. 532 (2002) 103-106
    • (2002) FEBS Lett. , vol.532 , pp. 103-106
    • Bota, D.A.1    Van Remmen, H.2    Davies, K.J.3
  • 7
    • 0019980984 scopus 로고
    • Reduction of N-acetyl methionine sulfoxide: a simple assay for peptide methionine sulfoxide reductase
    • Brot N., Werth J., Koster D., and Weissbach H. Reduction of N-acetyl methionine sulfoxide: a simple assay for peptide methionine sulfoxide reductase. Anal. Biochem. 122 (1982) 291-294
    • (1982) Anal. Biochem. , vol.122 , pp. 291-294
    • Brot, N.1    Werth, J.2    Koster, D.3    Weissbach, H.4
  • 9
    • 17844393112 scopus 로고    scopus 로고
    • Reversible redox-dependent modulation of mitochondrial aconitase and proteolytic activity during in vivo cardiac ischemia/reperfusion
    • Bulteau A.L., Lundberg K.C., Ikeda-Saito M., Isaya G., and Szweda L.I. Reversible redox-dependent modulation of mitochondrial aconitase and proteolytic activity during in vivo cardiac ischemia/reperfusion. Proc. Natl Acad. Sci. USA 102 (2005) 5987-5991
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 5987-5991
    • Bulteau, A.L.1    Lundberg, K.C.2    Ikeda-Saito, M.3    Isaya, G.4    Szweda, L.I.5
  • 10
    • 0038239701 scopus 로고    scopus 로고
    • Selective degradation of oxidatively modified protein substrates by the proteasome
    • Grune T., Merker K., Sandig G., and Davies K.J. Selective degradation of oxidatively modified protein substrates by the proteasome. Biochem. Biophys. Res. Commun. 305 (2003) 709-718
    • (2003) Biochem. Biophys. Res. Commun. , vol.305 , pp. 709-718
    • Grune, T.1    Merker, K.2    Sandig, G.3    Davies, K.J.4
  • 11
    • 1642464647 scopus 로고    scopus 로고
    • A second human methionine sulfoxide reductase (hMSRB2) reducing methionine-R-sulfoxide displays a tissue expression pattern distinct from hMSRB1
    • Hansel A., Jung S., Hoshi T., and Heinemann S.H. A second human methionine sulfoxide reductase (hMSRB2) reducing methionine-R-sulfoxide displays a tissue expression pattern distinct from hMSRB1. Redox Rep. 8 (2003) 384-388
    • (2003) Redox Rep. , vol.8 , pp. 384-388
    • Hansel, A.1    Jung, S.2    Hoshi, T.3    Heinemann, S.H.4
  • 12
    • 12844271548 scopus 로고    scopus 로고
    • Heterogeneity and function of mammalian MSRs: enzymes for repair, protection and regulation
    • Hansel A., Heinemann S.H., and Hoshi T. Heterogeneity and function of mammalian MSRs: enzymes for repair, protection and regulation. Biochim. Biophys. Acta 1703 (2005) 239-247
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 239-247
    • Hansel, A.1    Heinemann, S.H.2    Hoshi, T.3
  • 13
    • 0037063326 scopus 로고    scopus 로고
    • Activity, tissue distribution and site-directed mutagenesis of a human peptide methionine sulfoxide reductase of type B: hCBS1
    • Jung S., Hansel A., Kasperczyk H., Hoshi T., and Heinemann S.H. Activity, tissue distribution and site-directed mutagenesis of a human peptide methionine sulfoxide reductase of type B: hCBS1. FEBS Lett. 527 (2002) 91-94
    • (2002) FEBS Lett. , vol.527 , pp. 91-94
    • Jung, S.1    Hansel, A.2    Kasperczyk, H.3    Hoshi, T.4    Heinemann, S.H.5
  • 14
    • 20144375447 scopus 로고    scopus 로고
    • Role of structural and functional elements of mouse methionine-S-sulfoxide reductase in its subcellular distribution
    • Kim H.Y., and Gladyshev V.N. Role of structural and functional elements of mouse methionine-S-sulfoxide reductase in its subcellular distribution. Biochemistry 44 (2005) 8059-8067
    • (2005) Biochemistry , vol.44 , pp. 8059-8067
    • Kim, H.Y.1    Gladyshev, V.N.2
  • 15
    • 0035846605 scopus 로고    scopus 로고
    • Consequences of brief ischemia: stunning, preconditioning, and their clinical implications: part 1
    • Kloner R.A., and Jennings R.B. Consequences of brief ischemia: stunning, preconditioning, and their clinical implications: part 1. Circulation 104 (2001) 2981-2989
    • (2001) Circulation , vol.104 , pp. 2981-2989
    • Kloner, R.A.1    Jennings, R.B.2
  • 16
    • 0035909985 scopus 로고    scopus 로고
    • Consequences of brief ischemia: stunning, preconditioning, and their clinical implications: part 2
    • Kloner R.A., and Jennings R.B. Consequences of brief ischemia: stunning, preconditioning, and their clinical implications: part 2. Circulation 104 (2001) 3158-3167
    • (2001) Circulation , vol.104 , pp. 3158-3167
    • Kloner, R.A.1    Jennings, R.B.2
  • 17
    • 0032770232 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of a human peptide methionine sulfoxide reductase (hMsrA)
    • Kuschel L., Hansel A., Schonherr R., Weissbach H., Brot N., Hoshi T., and Heinemann S.H. Molecular cloning and functional expression of a human peptide methionine sulfoxide reductase (hMsrA). FEBS Lett. 456 (1999) 17-21
    • (1999) FEBS Lett. , vol.456 , pp. 17-21
    • Kuschel, L.1    Hansel, A.2    Schonherr, R.3    Weissbach, H.4    Brot, N.5    Hoshi, T.6    Heinemann, S.H.7
  • 19
    • 7044246314 scopus 로고    scopus 로고
    • Initiation of mitochondrial mediated apoptosis during cardiac reperfusion. Arch
    • Lundberg K.C., and Szweda L.I. Initiation of mitochondrial mediated apoptosis during cardiac reperfusion. Arch. Biochem. Biophys. 432 (2004) 50-57
    • (2004) Biochem. Biophys. , vol.432 , pp. 50-57
    • Lundberg, K.C.1    Szweda, L.I.2
  • 21
    • 17844372715 scopus 로고    scopus 로고
    • Roles of methionine sulfoxide reductases in antioxidant defense, protein regulation and survival
    • Moskovitz J. Roles of methionine sulfoxide reductases in antioxidant defense, protein regulation and survival. Curr. Pharm. Des. 11 (2005) 1451-1457
    • (2005) Curr. Pharm. Des. , vol.11 , pp. 1451-1457
    • Moskovitz, J.1
  • 22
    • 0032564345 scopus 로고    scopus 로고
    • Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress
    • Moskovitz J., Flescher E., Berlett B.S., Azare J., Poston J.M., and Stadtman E.R. Overexpression of peptide-methionine sulfoxide reductase in Saccharomyces cerevisiae and human T cells provides them with high resistance to oxidative stress. Proc. Natl Acad. Sci. USA 95 (1998) 14071-14075
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 14071-14075
    • Moskovitz, J.1    Flescher, E.2    Berlett, B.S.3    Azare, J.4    Poston, J.M.5    Stadtman, E.R.6
  • 23
    • 12844277331 scopus 로고    scopus 로고
    • Protein maintenance in aging and replicative senescence: a role for the peptide methionine sulfoxide reductases
    • Petropoulos I., and Friguet B. Protein maintenance in aging and replicative senescence: a role for the peptide methionine sulfoxide reductases. Biochim. Biophys. Acta 1703 (2005) 261-266
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 261-266
    • Petropoulos, I.1    Friguet, B.2
  • 24
    • 0035339675 scopus 로고    scopus 로고
    • Rat peptide methionine sulphoxide reductase: cloning of the cDNA, and down-regulation of gene expression and enzyme activity during aging
    • Petropoulos I., Mary J., Perichon M., and Friguet B. Rat peptide methionine sulphoxide reductase: cloning of the cDNA, and down-regulation of gene expression and enzyme activity during aging. Biochem. J. 355 (2001) 819-825
    • (2001) Biochem. J. , vol.355 , pp. 819-825
    • Petropoulos, I.1    Mary, J.2    Perichon, M.3    Friguet, B.4
  • 25
    • 0842346324 scopus 로고    scopus 로고
    • The peptide methionine sulfoxide reductases, MsrA and MsrB (hCBS-1), are downregulated during replicative senescence of human WI-38 fibroblasts
    • Picot C.R., Perichon M., Cintrat J.C., Friguet B., and Petropoulos I. The peptide methionine sulfoxide reductases, MsrA and MsrB (hCBS-1), are downregulated during replicative senescence of human WI-38 fibroblasts. FEBS Lett. 558 (2004) 74-78
    • (2004) FEBS Lett. , vol.558 , pp. 74-78
    • Picot, C.R.1    Perichon, M.2    Cintrat, J.C.3    Friguet, B.4    Petropoulos, I.5
  • 27
    • 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., Luche S., Rey C., Aebersold R., Benahmed M., Louisot P., and Lunardi J. Proteomics analysis of cellular response to oxidative stress. Evidence for in vivo overoxidation of peroxiredoxins at their active site. J. Biol. Chem. 277 (2002) 19396-19401
    • (2002) J. Biol. Chem. , vol.277 , pp. 19396-19401
    • Rabilloud, T.1    Heller, M.2    Gasnier, F.3    Luche, S.4    Rey, C.5    Aebersold, R.6    Benahmed, M.7    Louisot, P.8    Lunardi, J.9
  • 28
    • 0036401499 scopus 로고    scopus 로고
    • Selective inactivation of redox-sensitive mitochondrial enzymes during cardiac reperfusion
    • Sadek H.A., Humphries K.M., Szweda P.A., and Szweda L.I. Selective inactivation of redox-sensitive mitochondrial enzymes during cardiac reperfusion. Arch. Biochem. Biophys. 406 (2002) 222-228
    • (2002) Arch. Biochem. Biophys. , vol.406 , pp. 222-228
    • Sadek, H.A.1    Humphries, K.M.2    Szweda, P.A.3    Szweda, L.I.4
  • 29
    • 0344063351 scopus 로고    scopus 로고
    • Cardiac ischemia/reperfusion, aging, and redox-dependent alterations in mitochondrial function
    • Sadek H.A., Nulton-Persson A.C., Szweda P.A., and Szweda L.I. Cardiac ischemia/reperfusion, aging, and redox-dependent alterations in mitochondrial function. Arch. Biochem. Biophys. 420 (2003) 201-208
    • (2003) Arch. Biochem. Biophys. , vol.420 , pp. 201-208
    • Sadek, H.A.1    Nulton-Persson, A.C.2    Szweda, P.A.3    Szweda, L.I.4
  • 30
    • 0041845204 scopus 로고    scopus 로고
    • Subcellular localization of methionine sulphoxide reductase A (MsrA): evidence for mitochondrial and cytosolic isoforms in rat liver cells
    • Vougier S., Mary J., and Friguet B. Subcellular localization of methionine sulphoxide reductase A (MsrA): evidence for mitochondrial and cytosolic isoforms in rat liver cells. Biochem. J. 373 (2003) 531-537
    • (2003) Biochem. J. , vol.373 , pp. 531-537
    • Vougier, S.1    Mary, J.2    Friguet, B.3
  • 31
    • 3142661063 scopus 로고    scopus 로고
    • Essential role of methionine residues in calmodulin binding to Bordetella pertussis adenylate cyclase, as probed by selective oxidation and repair by the peptide methionine sulfoxide reductases
    • Vougier S., Mary J., Dautin N., Vinh J., Friguet B., and Ladant D. Essential role of methionine residues in calmodulin binding to Bordetella pertussis adenylate cyclase, as probed by selective oxidation and repair by the peptide methionine sulfoxide reductases. J. Biol. Chem. 279 (2004) 30210-30218
    • (2004) J. Biol. Chem. , vol.279 , pp. 30210-30218
    • Vougier, S.1    Mary, J.2    Dautin, N.3    Vinh, J.4    Friguet, B.5    Ladant, D.6
  • 32
    • 13544272571 scopus 로고    scopus 로고
    • Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-Cys peroxiredoxins
    • Woo H.A., Jeong W., Chang T.S., Park K.J., Park S.J., Yang J.S., and Rhee S.G. Reduction of cysteine sulfinic acid by sulfiredoxin is specific to 2-Cys peroxiredoxins. J. Biol. Chem. 280 (2005) 3125-3128
    • (2005) J. Biol. Chem. , vol.280 , pp. 3125-3128
    • Woo, H.A.1    Jeong, W.2    Chang, T.S.3    Park, K.J.4    Park, S.J.5    Yang, J.S.6    Rhee, S.G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.