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Volumn 178, Issue 1, 2012, Pages 8-17

Ischemic preconditioning preserves mitochondrial membrane potential and limits reactive oxygen species production

Author keywords

Cardiac; Heart; Ischemia reperfusion; Ischemic preconditioning; Membrane potential; Mitochondria; Reactive oxygen species

Indexed keywords

CYTOCHROME; REACTIVE OXYGEN METABOLITE; SUPEROXIDE; TETRAPHENYLPHOSPHONIUM;

EID: 84868198865     PISSN: 00224804     EISSN: 10958673     Source Type: Journal    
DOI: 10.1016/j.jss.2012.05.090     Document Type: Article
Times cited : (20)

References (54)
  • 1
    • 0037105335 scopus 로고    scopus 로고
    • Mitochondria: Regulators of signal transduction by reactive oxygen and nitrogen species
    • P.S. Brookes, A.L. Levonen, S. Shiva, P. Sarti, and V.M. Darley-Usmar Mitochondria: regulators of signal transduction by reactive oxygen and nitrogen species Free Rad Biol Med 33 2002 755
    • (2002) Free Rad Biol Med , vol.33 , pp. 755
    • Brookes, P.S.1    Levonen, A.L.2    Shiva, S.3    Sarti, P.4    Darley-Usmar, V.M.5
  • 2
    • 0032889677 scopus 로고    scopus 로고
    • Redox regulation of cellular signaling
    • H. Kamata, and H. Hirata Redox regulation of cellular signaling Cell Signal 11 1999 1
    • (1999) Cell Signal , vol.11 , pp. 1
    • Kamata, H.1    Hirata, H.2
  • 3
    • 0027181186 scopus 로고
    • Evidence that mitochondrial respiration is a source of potentially toxic oxygen free radicals in intact rabbit hearts subjected to ischemia and reflow
    • G. Ambrosio, J.L. Zweier, and C. Duilio Evidence that mitochondrial respiration is a source of potentially toxic oxygen free radicals in intact rabbit hearts subjected to ischemia and reflow J Biol Chem 268 1993 18532
    • (1993) J Biol Chem , vol.268 , pp. 18532
    • Ambrosio, G.1    Zweier, J.L.2    Duilio, C.3
  • 4
    • 33646421637 scopus 로고    scopus 로고
    • 2+ overloading, trigger pH- and mitochondrial permeability transition-dependent death of adult rat myocytes after ischemia-reperfusion
    • 2+ overloading, trigger pH- and mitochondrial permeability transition-dependent death of adult rat myocytes after ischemia-reperfusion Am J Physiol Heart Circ Physiol 290 2006 H2024
    • (2006) Am J Physiol Heart Circ Physiol , vol.290 , pp. 2024
    • Kim, J.S.1    Jin, Y.2    Lemasters, J.J.3
  • 5
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • S.S. Korshunov, V.P. Skulachev, and A.A. Starkov High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria FEBS Lett 416 1997 15
    • (1997) FEBS Lett , vol.416 , pp. 15
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 6
    • 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
    • (2009) Biochem J , vol.417 , pp. 1
    • Murphy, M.P.1
  • 7
    • 33847352937 scopus 로고    scopus 로고
    • Characterization of in vivo tissue redox statuts, oxygenation, and formation of reactive oxygen species in postischemic myocardium
    • X. Zhu, L. Zuo, A.J. Cardounel, J.L. Zweier, and G. He Characterization of in vivo tissue redox statuts, oxygenation, and formation of reactive oxygen species in postischemic myocardium Antiox Redox Signal 9 2007 447
    • (2007) Antiox Redox Signal , vol.9 , pp. 447
    • Zhu, X.1    Zuo, L.2    Cardounel, A.J.3    Zweier, J.L.4    He, G.5
  • 8
    • 39549102405 scopus 로고    scopus 로고
    • Ischemic defects in the electron transport chain increase the production of reactive oxygen species from isolated rat heart mitochondria
    • Q. Chen, S. Moghaddas, C.L. Hoppel, and E.J. Lesnefsky Ischemic defects in the electron transport chain increase the production of reactive oxygen species from isolated rat heart mitochondria Am J Physiol Cell Physiol 294 2008 C460
    • (2008) Am J Physiol Cell Physiol , vol.294 , pp. 460
    • Chen, Q.1    Moghaddas, S.2    Hoppel, C.L.3    Lesnefsky, E.J.4
  • 9
    • 0141815741 scopus 로고    scopus 로고
    • Production of reactive oxygen species by mitochondria: Central role of complex III
    • Q. Chen, E.J. Vazquez, S. Moghaddas, C.L. Hoppel, and E.J. Lesnefsky Production of reactive oxygen species by mitochondria: central role of complex III J Biol Chem 278 2003 36027
    • (2003) J Biol Chem , vol.278 , pp. 36027
    • Chen, Q.1    Vazquez, E.J.2    Moghaddas, S.3    Hoppel, C.L.4    Lesnefsky, E.J.5
  • 10
    • 0022970945 scopus 로고
    • Preconditioning with ischemia: A delay of lethal cell injury in ischemic myocardium
    • C.E. Murry, R.B. Jennings, and K.A. Reimer Preconditioning with ischemia: a delay of lethal cell injury in ischemic myocardium Circulation 74 1986 1124
    • (1986) Circulation , vol.74 , pp. 1124
    • Murry, C.E.1    Jennings, R.B.2    Reimer, K.A.3
  • 11
    • 42049108814 scopus 로고    scopus 로고
    • Mechanisms underlying acute protection from cardiac ischemia-reperfusion injury
    • E. Murphy, and C. Steenbergen Mechanisms underlying acute protection from cardiac ischemia-reperfusion injury Physiology Review 88 2008 581
    • (2008) Physiology Review , vol.88 , pp. 581
    • Murphy, E.1    Steenbergen, C.2
  • 17
    • 0017740356 scopus 로고
    • Biochemical properties of subsarcolemmal and interfibrillar mitochondria isolated from rat cardiac muscle
    • J.W. Palmer, B. Tandler, and C.L. Hoppel Biochemical properties of subsarcolemmal and interfibrillar mitochondria isolated from rat cardiac muscle J Biol Chem 252 1977 8731
    • (1977) J Biol Chem , vol.252 , pp. 8731
    • Palmer, J.W.1    Tandler, B.2    Hoppel, C.L.3
  • 18
    • 0020669405 scopus 로고
    • Determination of total protein
    • G.L. Peterson Determination of total protein Methods Enzymol 91 1983 95
    • (1983) Methods Enzymol , vol.91 , pp. 95
    • Peterson, G.L.1
  • 19
    • 27844605495 scopus 로고    scopus 로고
    • Superoxide generation from mitochondrial NADH dehydrogenase induces self-inactivation with specific protein radical formation
    • Y.R. Chen, C.L. Chen, L. Zhang, K.B. Green-Church, and J.L. Zweier Superoxide generation from mitochondrial NADH dehydrogenase induces self-inactivation with specific protein radical formation J Biol Chem 280 2005 37339
    • (2005) J Biol Chem , vol.280 , pp. 37339
    • Chen, Y.R.1    Chen, C.L.2    Zhang, L.3    Green-Church, K.B.4    Zweier, J.L.5
  • 20
    • 0028455102 scopus 로고
    • Simulation of multiple isotropic spin-trap EPR spectra
    • D.R. Duling Simulation of multiple isotropic spin-trap EPR spectra J Magn Reson B 104 1994 105
    • (1994) J Magn Reson B , vol.104 , pp. 105
    • Duling, D.R.1
  • 21
    • 0018665167 scopus 로고
    • Membrane potential of mitochondria measured with an electrode sensitive to tetraphenyl phosphonium and relationship between proton electrochemical potential and phosphorylation potential in steady state
    • N. Kamo, M. Muratsugu, R. Hongoh, and Y. Kobatake Membrane potential of mitochondria measured with an electrode sensitive to tetraphenyl phosphonium and relationship between proton electrochemical potential and phosphorylation potential in steady state J Membr Biol 49 1979 105
    • (1979) J Membr Biol , vol.49 , pp. 105
    • Kamo, N.1    Muratsugu, M.2    Hongoh, R.3    Kobatake, Y.4
  • 22
    • 0344406123 scopus 로고    scopus 로고
    • Tissue-specific depression of mitochondrial proton leak and substrate oxidation in hibernating arctic ground squirrels
    • J.L. Barger, M.D. Brand, B.M. Barnes, and B.B. Boyer Tissue-specific depression of mitochondrial proton leak and substrate oxidation in hibernating arctic ground squirrels Am J Physiol Regul Integr Comp Physiol 284 2003 R1306
    • (2003) Am J Physiol Regul Integr Comp Physiol , vol.284 , pp. 1306
    • Barger, J.L.1    Brand, M.D.2    Barnes, B.M.3    Boyer, B.B.4
  • 23
    • 0034661503 scopus 로고    scopus 로고
    • Kinetics and control of oxidative phosphorylation in rat liver mitochondria after chronic ethanol feeding
    • A. Marcinkeviciute, V. Mildaziene, S. Crumm, O. Demin, J.B. Hoek, and B. Kholodenko Kinetics and control of oxidative phosphorylation in rat liver mitochondria after chronic ethanol feeding Biochem J 349 2000 519
    • (2000) Biochem J , vol.349 , pp. 519
    • Marcinkeviciute, A.1    Mildaziene, V.2    Crumm, S.3    Demin, O.4    Hoek, J.B.5    Kholodenko, B.6
  • 24
    • 0021280373 scopus 로고
    • Rat liver mitochondria prepared in mannitol media demonstrate increased mitochondrial volumes compared with mitochondria prepared in sucrose media. Relationship to the effect of glucagon on mitochondrial function
    • D.E. Whipps, and A.P. Halestrap Rat liver mitochondria prepared in mannitol media demonstrate increased mitochondrial volumes compared with mitochondria prepared in sucrose media. Relationship to the effect of glucagon on mitochondrial function Biochem J 221 1984 147
    • (1984) Biochem J , vol.221 , pp. 147
    • Whipps, D.E.1    Halestrap, A.P.2
  • 25
    • 0034485383 scopus 로고    scopus 로고
    • Digital imaging analysis for the study of endotoxin-induced mitochondrial ultrastructure injury
    • M.S. Joshi, E.D. Crouser, M.W. Julian, B.L. Schanbacher, and J.A. Bauer Digital imaging analysis for the study of endotoxin-induced mitochondrial ultrastructure injury Anayl Cell Pathol 21 2000 41
    • (2000) Anayl Cell Pathol , vol.21 , pp. 41
    • Joshi, M.S.1    Crouser, E.D.2    Julian, M.W.3    Schanbacher, B.L.4    Bauer, J.A.5
  • 26
    • 0037410208 scopus 로고    scopus 로고
    • Quantification of cytochrome c release from rat liver mitochondria
    • E.D. Crouser, M.E. Gadd, and M.W. Julian Quantification of cytochrome c release from rat liver mitochondria Analy Biochem 317 2003 67
    • (2003) Analy Biochem , vol.317 , pp. 67
    • Crouser, E.D.1    Gadd, M.E.2    Julian, M.W.3
  • 27
    • 4644316100 scopus 로고    scopus 로고
    • Kinetic analysis-based quantitation of free radical generation in EPR spin trapping
    • A. Samouilov, V. Roubaud, P. Kuppusamy, and J.L. Zweier Kinetic analysis-based quantitation of free radical generation in EPR spin trapping Analy Biochem 334 2004 145
    • (2004) Analy Biochem , vol.334 , pp. 145
    • Samouilov, A.1    Roubaud, V.2    Kuppusamy, P.3    Zweier, J.L.4
  • 29
    • 0020048321 scopus 로고
    • Production of hydroxyl radical by decomposition of superoxide spin-trapped adducts
    • E. Finkelstein, G.M. Rosen, and E.J. Rauckman Production of hydroxyl radical by decomposition of superoxide spin-trapped adducts Molec Pharma 21 1982 262
    • (1982) Molec Pharma , vol.21 , pp. 262
    • Finkelstein, E.1    Rosen, G.M.2    Rauckman, E.J.3
  • 30
    • 0023867107 scopus 로고
    • Measurement of superoxide-derived free radicals in the reperfused heart
    • J.L. Zweier Measurement of superoxide-derived free radicals in the reperfused heart J Biol Chem 263 1988 1353
    • (1988) J Biol Chem , vol.263 , pp. 1353
    • Zweier, J.L.1
  • 31
    • 0024821055 scopus 로고
    • Measurement and characterization of postischemic free radical generation in the isolated perfused heart
    • J.L. Zweier, P. Kuppusamy, and R. Williams Measurement and characterization of postischemic free radical generation in the isolated perfused heart J Biol Chem 264 1989 18890
    • (1989) J Biol Chem , vol.264 , pp. 18890
    • Zweier, J.L.1    Kuppusamy, P.2    Williams, R.3
  • 32
    • 34547130863 scopus 로고    scopus 로고
    • The role of mitochondria in protection of the heart by preconditioning
    • A.P. Halestrap, S.J. Clarke, and I. Khaliulin The role of mitochondria in protection of the heart by preconditioning Biochim Biophys Acta 1767 2007 1007
    • (2007) Biochim Biophys Acta , vol.1767 , pp. 1007
    • Halestrap, A.P.1    Clarke, S.J.2    Khaliulin, I.3
  • 33
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • 552.2
    • J.F. Turrens Mitochondrial formation of reactive oxygen species J Physiol 552.2 2003 335
    • (2003) J Physiol , pp. 335
    • Turrens, J.F.1
  • 35
    • 0030890196 scopus 로고    scopus 로고
    • Oxygen radicals released during ischemic preconditioning contribute to cardioprotection in the rabbit myocardium
    • C.P. Baines, M. Goto, and J.M. Downey Oxygen radicals released during ischemic preconditioning contribute to cardioprotection in the rabbit myocardium J Mol Cell Cardio 29 1997 207
    • (1997) J Mol Cell Cardio , vol.29 , pp. 207
    • Baines, C.P.1    Goto, M.2    Downey, J.M.3
  • 36
    • 0034665065 scopus 로고    scopus 로고
    • Opening of mitochondrial KATP channels triggers the preconditioned state by generating free radicals
    • T. Pain, X.M. Yang, and S.D. Critz Opening of mitochondrial KATP channels triggers the preconditioned state by generating free radicals Circ Res 87 2000 460
    • (2000) Circ Res , vol.87 , pp. 460
    • Pain, T.1    Yang, X.M.2    Critz, S.D.3
  • 37
    • 33646055216 scopus 로고    scopus 로고
    • The role of oxidants and free radicals in reperfusion injury
    • J.L. Zweier, and M.A.H. Talukder The role of oxidants and free radicals in reperfusion injury Cardiovasc Res 70 2006 181
    • (2006) Cardiovasc Res , vol.70 , pp. 181
    • Zweier, J.L.1    Talukder, M.A.H.2
  • 38
    • 46349106237 scopus 로고    scopus 로고
    • The Endogenous mitochondrial complex II inhibitor malonate regulates mitochondrial ATP-sensitive potassium channels: Implications for ischemic preconditioning
    • Epub 2008 Apr 8
    • A.P. Wojtovich, and P.S. Brookes The Endogenous mitochondrial complex II inhibitor malonate regulates mitochondrial ATP-sensitive potassium channels: implications for ischemic preconditioning Biochim Biophys Acta 1777 2008 882 Epub 2008 Apr 8
    • (2008) Biochim Biophys Acta , vol.1777 , pp. 882
    • Wojtovich, A.P.1    Brookes, P.S.2
  • 39
    • 33846335174 scopus 로고    scopus 로고
    • Modulation of electron transport protects cardiac mitochondria and decreases myocardial injury during ischemia and reperfusion
    • Q. Chen, A.K.S. Camara, D.F. Stowe, C.L. Hoppel, and E.J. Lesnefsky Modulation of electron transport protects cardiac mitochondria and decreases myocardial injury during ischemia and reperfusion Am J Physiol Cell Physiol 292 2007 C137
    • (2007) Am J Physiol Cell Physiol , vol.292 , pp. 137
    • Chen, Q.1    Camara, A.K.S.2    Stowe, D.F.3    Hoppel, C.L.4    Lesnefsky, E.J.5
  • 40
    • 0042433242 scopus 로고    scopus 로고
    • 2 production by membrane potential and NAD(P)H redox state
    • 2 production by membrane potential and NAD(P)H redox state J Neurochem 86 2003 1101
    • (2003) J Neurochem , vol.86 , pp. 1101
    • Starkov, A.A.1    Fiskum, G.2
  • 41
    • 77953809992 scopus 로고    scopus 로고
    • Redox-optimized ROS balance: A unifying hypothesis
    • M.A. Aon, S. Cortassa, and B. O'Rourke Redox-optimized ROS balance: a unifying hypothesis Biochim Biophys Acta 1797 2010 865
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 865
    • Aon, M.A.1    Cortassa, S.2    O'Rourke, B.3
  • 43
    • 0037745119 scopus 로고    scopus 로고
    • Fluctuations in mitochondria membrane potential caused by repetitive gating of the permeability transition pore
    • J. Huser, and L.A. Blatter Fluctuations in mitochondria membrane potential caused by repetitive gating of the permeability transition pore Biochem J 343 1999 311
    • (1999) Biochem J , vol.343 , pp. 311
    • Huser, J.1    Blatter, L.A.2
  • 44
    • 66249144695 scopus 로고    scopus 로고
    • Transient opening of mitochondrial permeability transition pore by reactive oxygen species protects myocardium from ischemia-reperfusion injury
    • M. Saotome, H. Katoh, and Y. Yaguchi Transient opening of mitochondrial permeability transition pore by reactive oxygen species protects myocardium from ischemia-reperfusion injury Am J Physiol Heart Circ Physiol 296 2009 H1125
    • (2009) Am J Physiol Heart Circ Physiol , vol.296 , pp. 1125
    • Saotome, M.1    Katoh, H.2    Yaguchi, Y.3
  • 45
    • 0037087782 scopus 로고    scopus 로고
    • 2+ and sustained opening of the permeability transition pore
    • 2+ and sustained opening of the permeability transition pore J Cell Sci 115 2002 1175
    • (2002) J Cell Sci , vol.115 , pp. 1175
    • Jacobson, J.1    Duchen, M.R.2
  • 46
    • 38849156952 scopus 로고    scopus 로고
    • Heart mitochondria: Gates of life and death
    • A.B. Gustafsson, and R.A. Gottlieb Heart mitochondria: gates of life and death Cardiovasc Res 77 2008 334
    • (2008) Cardiovasc Res , vol.77 , pp. 334
    • Gustafsson, A.B.1    Gottlieb, R.A.2
  • 47
    • 34547578624 scopus 로고    scopus 로고
    • Sequential opening of mitochondrial ion channels as a function of glutathione redox thiol status
    • M.A. Aon, S. Cortassa, C. Maack, and B. O'Rourke Sequential opening of mitochondrial ion channels as a function of glutathione redox thiol status J Biol Chem 282 2007 21889
    • (2007) J Biol Chem , vol.282 , pp. 21889
    • Aon, M.A.1    Cortassa, S.2    Maack, C.3    O'Rourke, B.4
  • 48
    • 0038172269 scopus 로고    scopus 로고
    • Ischemic preconditioning inhibits opening of mitochondrial permeability transition pores in the reperfused rat heart
    • S.A. Javadov, S. Clarke, M. Das, J. Griffiths, K.H.H. Lim, and A.P. Halestrap Ischemic preconditioning inhibits opening of mitochondrial permeability transition pores in the reperfused rat heart J Physiol 549 Pt 2 2003 513
    • (2003) J Physiol , vol.549 , Issue.PART 2 , pp. 513
    • Javadov, S.A.1    Clarke, S.2    Das, M.3    Griffiths, J.4    Lim, K.H.H.5    Halestrap, A.P.6
  • 49
    • 77955955395 scopus 로고    scopus 로고
    • A pore way to die: The role of mitochondria in reperfusion injury and cardioprotection
    • A.P. Halestrap A pore way to die: the role of mitochondria in reperfusion injury and cardioprotection Biochem Soc Trans 38 2010 841
    • (2010) Biochem Soc Trans , vol.38 , pp. 841
    • Halestrap, A.P.1
  • 50
    • 77953357715 scopus 로고    scopus 로고
    • Oxidative stress causes reversible changes in mitochondrial permeability and structure
    • 10.1016/j.exger.2010.01.016
    • N.B. Cole, M.P. Daniels, R.L. Levine, and G. Kim Oxidative stress causes reversible changes in mitochondrial permeability and structure Exp Gerentol 2010 10.1016/j.exger.2010.01.016
    • (2010) Exp Gerentol
    • Cole, N.B.1    Daniels, M.P.2    Levine, R.L.3    Kim, G.4
  • 51
    • 33751276291 scopus 로고    scopus 로고
    • Myocardial ischemia decreases oxidative phosphorylation through cytochrome oxidase in subsarcolemmal mitochondria
    • E.J. Lesnefsky, B. Tandler, J. Ye, T.J. Slabe, J. Turkaly, and C.L. Hoppel Myocardial ischemia decreases oxidative phosphorylation through cytochrome oxidase in subsarcolemmal mitochondria Am J Physiol 273 1997 H1544
    • (1997) Am J Physiol , vol.273 , pp. 1544
    • Lesnefsky, E.J.1    Tandler, B.2    Ye, J.3    Slabe, T.J.4    Turkaly, J.5    Hoppel, C.L.6
  • 52
    • 23744471140 scopus 로고    scopus 로고
    • Mitochondria and ischemia/reperfusion injury
    • H.M. Honda, P. Korge, and J.N. Weiss Mitochondria and ischemia/reperfusion injury Ann NY Acad Sci 1047 2005 248
    • (2005) Ann NY Acad Sci , vol.1047 , pp. 248
    • Honda, H.M.1    Korge, P.2    Weiss, J.N.3
  • 53
    • 0036007116 scopus 로고    scopus 로고
    • A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis
    • L. Scorrano, M. Ashiya, and K. Buttle A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis Dev Cell 2 2002 55
    • (2002) Dev Cell , vol.2 , pp. 55
    • Scorrano, L.1    Ashiya, M.2    Buttle, K.3
  • 54
    • 33747779443 scopus 로고    scopus 로고
    • Preconditioning prevents loss in mitochondrial function and release of cytochrome c during prolonged cardiac ischemia/reperfusion
    • K.C. Lundberg, and L.I. Szweda Preconditioning prevents loss in mitochondrial function and release of cytochrome c during prolonged cardiac ischemia/reperfusion Arch Biochem Biophys 453 2006 130
    • (2006) Arch Biochem Biophys , vol.453 , pp. 130
    • Lundberg, K.C.1    Szweda, L.I.2


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