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Volumn 19, Issue 6, 2013, Pages 753-759

Cardioprotection by S-nitrosation of a cysteine switch on mitochondrial complex i

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; MITOCHONDRIAL DNA; MITOCHONDRIAL PROTEIN; NITRIC OXIDE DONOR; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE);

EID: 84880253528     PISSN: 10788956     EISSN: 1546170X     Source Type: Journal    
DOI: 10.1038/nm.3212     Document Type: Article
Times cited : (515)

References (47)
  • 1
    • 20944446791 scopus 로고    scopus 로고
    • Cytoprotective effects of nitrite during in vivo ischemia-reperfusion of the heart and liver
    • Duranski, M.R. et al. Cytoprotective effects of nitrite during in vivo ischemia-reperfusion of the heart and liver. J. Clin. Invest. 115, 1232-1240 (2005).
    • (2005) J. Clin. Invest , vol.115 , pp. 1232-1240
    • Duranski, M.R.1
  • 2
    • 34548412578 scopus 로고    scopus 로고
    • Nitrite augments tolerance to ischemia/reperfusion injury via the modulation of mitochondrial electron transfer
    • Shiva, S. et al. Nitrite augments tolerance to ischemia/reperfusion injury via the modulation of mitochondrial electron transfer. J. Exp. Med. 204, 2089-2102 (2007).
    • (2007) J. Exp. Med , vol.204 , pp. 2089-2102
    • Shiva, S.1
  • 3
    • 38849162730 scopus 로고    scopus 로고
    • The nitrate-nitrite-nitric oxide pathway in physiology and therapeutics
    • Lundberg, J.O., Weitzberg, E. & Gladwin, M.T. The nitrate-nitrite-nitric oxide pathway in physiology and therapeutics. Nat. Rev. Drug Discov. 7, 156-167 (2008).
    • (2008) Nat. Rev. Drug Discov , vol.7 , pp. 156-167
    • Lundberg, J.O.1    Weitzberg, E.2    Gladwin, M.T.3
  • 4
    • 77958064652 scopus 로고    scopus 로고
    • Both A2a and A2b adenosine receptors at reperfusion are necessary to reduce infarct size in mouse hearts
    • Methner, C., Schmidt, K., Cohen, M.V., Downey, J.M. & Krieg, T. Both A2a and A2b adenosine receptors at reperfusion are necessary to reduce infarct size in mouse hearts. Am. J. Physiol. Heart Circ. Physiol. 299, H1262-H1264 (2010).
    • (2010) Am. J. Physiol. Heart Circ. Physiol , vol.299
    • Methner, C.1    Schmidt, K.2    Cohen, M.V.3    Downey, J.M.4    Krieg, T.5
  • 6
    • 24044492874 scopus 로고    scopus 로고
    • Protein kinase G transmits the cardioprotective signal from cytosol to mitochondria
    • Costa, A.D. et al. Protein kinase G transmits the cardioprotective signal from cytosol to mitochondria. Circ. Res. 97, 329-336 (2005).
    • (2005) Circ. Res , vol.97 , pp. 329-336
    • Costa, A.D.1
  • 7
    • 3342971030 scopus 로고    scopus 로고
    • Myocardial protection at a crossroads
    • Bolli, R. et al. Myocardial protection at a crossroads. Circ. Res. 95, 125-134 (2004).
    • (2004) Circ. Res , vol.95 , pp. 125-134
    • Bolli, R.1
  • 8
    • 34548746306 scopus 로고    scopus 로고
    • Myocardial reperfusion injury
    • Yellon, D.M. & Hausenloy, D.J. Myocardial reperfusion injury. N. Engl. J. Med. 357, 1121-1135 (2007).
    • (2007) N. Engl. J. Med , vol.357 , pp. 1121-1135
    • Yellon, D.M.1    Hausenloy, D.J.2
  • 9
    • 77955444881 scopus 로고    scopus 로고
    • Pathogenesis of myocardial ischemia-reperfusion injury and rationale for therapy
    • Turer, A.T. & Hill, J.A. Pathogenesis of myocardial ischemia-reperfusion injury and rationale for therapy. Am. J. Cardiol. 106, 360-368 (2010).
    • (2010) Am. J. Cardiol , vol.106 , pp. 360-368
    • Turer, A.T.1    Hill, J.A.2
  • 10
    • 36348964192 scopus 로고    scopus 로고
    • Preconditioning results in S-nitrosylation of proteins involved in regulation of mitochondrial energetics and calcium transport
    • Sun, J., Morgan, M., Shen, R.F., Steenbergen, C. & Murphy, E. Preconditioning results in S-nitrosylation of proteins involved in regulation of mitochondrial energetics and calcium transport. Circ. Res. 101, 1155-1163 (2007).
    • (2007) Circ. Res , vol.101 , pp. 1155-1163
    • Sun, J.1    Morgan, M.2    Shen, R.F.3    Steenbergen, C.4    Murphy, E.5
  • 11
    • 67649757115 scopus 로고    scopus 로고
    • A mitochondria-targeted S-nitrosothiol modulates respiration nitrosates thiols and protects against ischemia-reperfusion injury
    • Prime, T.A. et al. A mitochondria-targeted S-nitrosothiol modulates respiration, nitrosates thiols, and protects against ischemia-reperfusion injury. Proc. Natl. Acad. Sci. USA 106, 10764-10769 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 10764-10769
    • Prime, T.A.1
  • 12
    • 77955492720 scopus 로고    scopus 로고
    • Identification of S-nitrosated mitochondrial proteins by S-nitrosothiol difference in gel electrophoresis (SNO-DIGE): Implications for the regulation of mitochondrial function by reversible S-nitrosation
    • Chouchani, E.T. et al. Identification of S-nitrosated mitochondrial proteins by S-nitrosothiol difference in gel electrophoresis (SNO-DIGE): implications for the regulation of mitochondrial function by reversible S-nitrosation. Biochem. J. 430, 49-59 (2010).
    • (2010) Biochem. J. , vol.430 , pp. 49-59
    • Chouchani, E.T.1
  • 13
    • 79953179727 scopus 로고    scopus 로고
    • Site-mapping of in vitro S-nitrosation in cardiac mitochondria: Implications for cardioprotection
    • M110.004721
    • Murray, C.I., Kane, L.A., Uhrigshardt, H., Wang, S.B. & Van Eyk, J.E. Site-mapping of in vitro S-nitrosation in cardiac mitochondria: implications for cardioprotection. Mol. Cell Prot. 10, M110.004721 (2011).
    • (2011) Mol. Cell Prot , vol.10
    • Murray, C.I.1    Kane, L.A.2    Uhrigshardt, H.3    Wang, S.B.4    Van Eyk, J.E.5
  • 14
    • 77955266918 scopus 로고    scopus 로고
    • Rapid uptake of lipophilic triphenylphosphonium cations by mitochondria in vivo following intravenous injection: Implications for mitochondria-specific therapies and probes
    • Porteous, C.M. et al. Rapid uptake of lipophilic triphenylphosphonium cations by mitochondria in vivo following intravenous injection: implications for mitochondria-specific therapies and probes. Biochim. Biophys. Acta 1800, 1009-1017 (2010).
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 1009-1017
    • Porteous, C.M.1
  • 15
    • 40949098241 scopus 로고    scopus 로고
    • Copper dependence of the biotin switch assay: Modified assay for measuring cellular and blood nitrosated proteins
    • Wang, X., Kettenhofen, N.J., Shiva, S., Hogg, N. & Gladwin, M.T. Copper dependence of the biotin switch assay: modified assay for measuring cellular and blood nitrosated proteins. Free Radic. Biol. Med. 44, 1362-1372 (2008).
    • (2008) Free Radic. Biol. Med , vol.44 , pp. 1362-1372
    • Wang, X.1    Kettenhofen, N.J.2    Shiva, S.3    Hogg, N.4    Gladwin, M.T.5
  • 16
    • 52049105346 scopus 로고    scopus 로고
    • In-gel detection of S-nitrosated proteins using fluorescence methods
    • Kettenhofen, N.J., Wang, X., Gladwin, M.T. & Hogg, N. In-gel detection of S-nitrosated proteins using fluorescence methods. Methods Enzymol. 441, 53-71 (2008).
    • (2008) Methods Enzymol , vol.441 , pp. 53-71
    • Kettenhofen, N.J.1    Wang, X.2    Gladwin, M.T.3    Hogg, N.4
  • 18
    • 84873938984 scopus 로고    scopus 로고
    • Protection through postconditioning or a mitochondria-targeted S-nitrosothiol is unaffected by cardiomyocyte-selective ablation of protein kinase G
    • Methner, C., Lukowski, R., Hofman, F., Murphy, M.P. & Krieg, T. Protection through postconditioning or a mitochondria-targeted S-nitrosothiol is unaffected by cardiomyocyte-selective ablation of protein kinase G. Basic Res. Cardiol. 108, 337 (2013).
    • (2013) Basic Res. Cardiol , vol.108 , pp. 337
    • Methner, C.1    Lukowski, R.2    Hofman, F.3    Murphy, M.P.4    Krieg, T.5
  • 19
    • 42049108814 scopus 로고    scopus 로고
    • Mechanisms underlying acute protection from cardiac ischemia-reperfusion injury
    • Murphy, E. & Steenbergen, C. Mechanisms underlying acute protection from cardiac ischemia-reperfusion injury. Physiol. Rev. 88, 581-609 (2008).
    • (2008) Physiol. Rev , vol.88 , pp. 581-609
    • Murphy, E.1    Steenbergen, C.2
  • 20
    • 79952144564 scopus 로고    scopus 로고
    • Measurement of H2O2 within living Drosophila during aging using a ratiometric mass spectrometry probe targeted to the mitochondrial matrix
    • Cochemé, H.M. et al. Measurement of H2O2 within living Drosophila during aging using a ratiometric mass spectrometry probe targeted to the mitochondrial matrix. Cell Metab. 13, 340-350 (2011).
    • (2011) Cell Metab , vol.13 , pp. 340-350
    • Cochemé, H.M.1
  • 21
    • 0032560572 scopus 로고    scopus 로고
    • Persistent inhibition of cell respiration by nitric oxide: Crucial role of S-nitrosylation of mitochondrial complex i and protective action of glutathione
    • Clementi, E., Brown, G.C., Feelisch, M. & Moncada, S. Persistent inhibition of cell respiration by nitric oxide: crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione. Proc. Natl. Acad. Sci. USA 95, 7631-7636 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7631-7636
    • Clementi, E.1    Brown, G.C.2    Feelisch, M.3    Moncada, S.4
  • 23
    • 33744527052 scopus 로고    scopus 로고
    • Persistent S-nitrosation of complex i and other mitochondrial membrane proteins by S-nitrosothiols but not nitric oxide or peroxynitrite
    • Dahm, C.C., Moore, K. & Murphy, M.P. Persistent S-nitrosation of complex I and other mitochondrial membrane proteins by S-nitrosothiols but not nitric oxide or peroxynitrite. J. Biol. Chem. 281, 10056-10065 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 10056-10065
    • Dahm, C.C.1    Moore, K.2    Murphy, M.P.3
  • 24
    • 38049136885 scopus 로고    scopus 로고
    • S-nitrosation of mitochondrial complex i depends on its structural conformation
    • Galkin, A. & Moncada, S. S-nitrosation of mitochondrial complex I depends on its structural conformation. J. Biol. Chem. 282, 37448-37453 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 37448-37453
    • Galkin, A.1    Moncada, S.2
  • 25
    • 33751574953 scopus 로고    scopus 로고
    • Bovine complex i is a complex of 45 different subunits
    • Carroll, J. et al. Bovine complex I is a complex of 45 different subunits. J. Biol. Chem. 281, 32724-32727 (2006).
    • (2006) J. Biol. Chem , vol.281 , pp. 32724-32727
    • Carroll, J.1
  • 26
    • 51049093616 scopus 로고    scopus 로고
    • Identification of the mitochondrial ND3 subunit as a structural component involved in the active/deactive enzyme transition of respiratory complex i
    • Galkin, A. et al. Identification of the mitochondrial ND3 subunit as a structural component involved in the active/deactive enzyme transition of respiratory complex I. J. Biol. Chem. 283, 20907-20913 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 20907-20913
    • Galkin, A.1
  • 27
    • 84875388964 scopus 로고    scopus 로고
    • Conformation-specific crosslinking of mitochondrial complex I
    • Ciano, M., Fuszard, M., Heide, H., Botting, C.H. & Galkin, A. Conformation-specific crosslinking of mitochondrial complex I. FEBS Lett. 587, 867-872 (2013).
    • (2013) FEBS Lett , vol.587 , pp. 867-872
    • Ciano, M.1    Fuszard, M.2    Heide, H.3    Botting, C.H.4    Galkin, A.5
  • 28
    • 84884623857 scopus 로고    scopus 로고
    • Conformational change of mitochondrial complex i increases ROS sensitivity during ischemia
    • published online, http://dx.doi.org/10.1089/ARS.2012.4698 29 March 2013)
    • Gorenkova, N., Robinson, E., Grieve, D.J. & Galkin, A. Conformational change of mitochondrial complex I increases ROS sensitivity during ischemia. Antioxid. Redox Signal. published online, http://dx.doi.org/10.1089/ARS.2012. 4698 (29 March 2013).
    • Antioxid. Redox Signal
    • Gorenkova, N.1    Robinson, E.2    Grieve, D.J.3    Galkin, A.4
  • 29
    • 77954754565 scopus 로고    scopus 로고
    • Targeted quantitation of site-specific cysteine oxidation in endogenous proteins using a differential alkylation and multiple reaction monitoring mass spectrometry approach
    • Held, J.M. et al. Targeted quantitation of site-specific cysteine oxidation in endogenous proteins using a differential alkylation and multiple reaction monitoring mass spectrometry approach. Mol. Cell. Proteomics 9, 1400-1410 (2010).
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 1400-1410
    • Held, J.M.1
  • 30
    • 79851516716 scopus 로고    scopus 로고
    • Measuring mitochondrial protein thiol redox state
    • Requejo, R. et al. Measuring mitochondrial protein thiol redox state. Methods Enzymol. 474, 123-147 (2010).
    • (2010) Methods Enzymol , vol.474 , pp. 123-147
    • Requejo, R.1
  • 31
    • 79957512037 scopus 로고    scopus 로고
    • The mitochondrial-encoded subunits of respiratory complex i (NADH: Ubiquinone oxidoreductase): Identifying residues important in mechanism and disease
    • Bridges, H.R., Birrell, J.A. & Hirst, J. The mitochondrial-encoded subunits of respiratory complex I (NADH: ubiquinone oxidoreductase): identifying residues important in mechanism and disease. Biochem. Soc. Trans. 39, 799-806 (2011).
    • (2011) Biochem. Soc. Trans , vol.39 , pp. 799-806
    • Bridges, H.R.1    Birrell, J.A.2    Hirst, J.3
  • 32
    • 33644872938 scopus 로고    scopus 로고
    • Structure of the hydrophilic domain of respiratory complex i from Thermus thermophilus
    • Sazanov, L.A. & Hinchcliffe, P. Structure of the hydrophilic domain of respiratory complex I from Thermus thermophilus. Science 311, 1430-1436 (2006).
    • (2006) Science , vol.311 , pp. 1430-1436
    • Sazanov, L.A.1    Hinchcliffe, P.2
  • 33
    • 80052068980 scopus 로고    scopus 로고
    • Structure of the membrane domain of respiratory complex I
    • Efremov, R.G. & Sazanov, L.A. Structure of the membrane domain of respiratory complex I. Nature 476, 414-420 (2011).
    • (2011) Nature , vol.476 , pp. 414-420
    • Efremov, R.G.1    Sazanov, L.A.2
  • 34
    • 84874352529 scopus 로고    scopus 로고
    • Crystal structure of the entire respiratory complex I
    • Baradaran, R., Berrisford, J.M., Minhas, G.S. & Sazanov, L.A. Crystal structure of the entire respiratory complex I. Nature 494, 443-448 (2013).
    • (2013) Nature , vol.494 , pp. 443-448
    • Baradaran, R.1    Berrisford, J.M.2    Minhas, G.S.3    Sazanov, L.A.4
  • 35
    • 84859432015 scopus 로고    scopus 로고
    • A cell-based phenotypic assay to identify cardioprotective agents
    • Guo, S. et al. A cell-based phenotypic assay to identify cardioprotective agents. Circ. Res. 110, 948-957 (2012).
    • (2012) Circ. Res , vol.110 , pp. 948-957
    • Guo, S.1
  • 36
    • 84860697620 scopus 로고    scopus 로고
    • Understanding mitochondrial complex i assembly in health and disease
    • Mimaki, M. et al. Understanding mitochondrial complex I assembly in health and disease. Biochim. Biophys. Acta 1817, 851-862 (2012).
    • (2012) Biochim. Biophys. Acta , vol.1817 , pp. 851-862
    • Mimaki, M.1
  • 37
    • 62249194823 scopus 로고    scopus 로고
    • Nitrite mediates cytoprotection after ischemia/reperfusion by modulating mitochondrial function
    • Shiva, S. & Gladwin, M.T. Nitrite mediates cytoprotection after ischemia/reperfusion by modulating mitochondrial function. Basic Res. Cardiol. 104, 113-119 (2009).
    • (2009) Basic Res. Cardiol , vol.104 , pp. 113-119
    • Shiva, S.1    Gladwin, M.T.2
  • 38
    • 4544378255 scopus 로고    scopus 로고
    • Reduction of nitrite to nitric oxide during ischemia protects against myocardial ischemia-reperfusion damage
    • Webb, A. et al. Reduction of nitrite to nitric oxide during ischemia protects against myocardial ischemia-reperfusion damage. Proc. Natl. Acad. Sci. USA 101, 13683-13688 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13683-13688
    • Webb, A.1
  • 39
    • 84871926566 scopus 로고    scopus 로고
    • Essential role of nitric oxide in acute ischemic preconditioning: S-nitros(yl)ation versus sGC/cGMP/PKG signaling? Free Radic
    • Sun, J. et al. Essential role of nitric oxide in acute ischemic preconditioning: S-nitros(yl)ation versus sGC/cGMP/PKG signaling? Free Radic. Biol. Med. 54, 105-112 (2013).
    • (2013) Biol. Med , vol.54 , pp. 105-112
    • Sun, J.1
  • 40
    • 79551470041 scopus 로고    scopus 로고
    • Lysine deacetylation in ischaemic preconditioning: The role of SIRT1
    • Nadtochiy, S.M., Redman, E., Rahman, I. & Brookes, P.S. Lysine deacetylation in ischaemic preconditioning: the role of SIRT1. Cardiovasc. Res. 89, 643-649 (2011).
    • (2011) Cardiovasc. Res , vol.89 , pp. 643-649
    • Nadtochiy, S.M.1    Redman, E.2    Rahman, I.3    Brookes, P.S.4
  • 41
    • 77954322925 scopus 로고    scopus 로고
    • Cardioprotective effects of mineralocorticoid receptor antagonists at reperfusion
    • Schmidt, K. et al. Cardioprotective effects of mineralocorticoid receptor antagonists at reperfusion. Eur. Heart J. 31, 1655-1662 (2010).
    • (2010) Eur. Heart J. , vol.31 , pp. 1655-1662
    • Schmidt, K.1
  • 43
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D.N., Pappin, D.J., Creasy, D.M. & Cottrell, J.S. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567 (1999).
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 45
    • 3543043510 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis for the isolation of integral membrane proteins and mass spectrometric identification
    • Rais, I., Karas, M. & Schagger, H. Two-dimensional electrophoresis for the isolation of integral membrane proteins and mass spectrometric identification. Proteomics 4, 2567-2571 (2004).
    • (2004) Proteomics , vol.4 , pp. 2567-2571
    • Rais, I.1    Karas, M.2    Schagger, H.3
  • 46
    • 77957010982 scopus 로고
    • Citrate synthase
    • Srere, P.A. Citrate synthase. Methods Enzymol. 13, 3-10 (1969).
    • (1969) Methods Enzymol , vol.13 , pp. 3-10
    • Srere, P.A.1
  • 47
    • 72449148626 scopus 로고    scopus 로고
    • Reactions of the flavin mononucleotide in complex I: A combined mechanism describes NADH oxidation coupled to the reduction of APAD+, ferricyanide, or molecular oxygen
    • Birrell, J.A., Yakovlev, G. & Hirst, J. Reactions of the flavin mononucleotide in complex I: a combined mechanism describes NADH oxidation coupled to the reduction of APAD+, ferricyanide, or molecular oxygen. Biochemistry 48, 12005-12013 (2009).
    • (2009) Biochemistry , vol.48 , pp. 12005-12013
    • Birrell, J.A.1    Yakovlev, G.2    Hirst, J.3


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