메뉴 건너뛰기




Volumn 592, Issue 17, 2014, Pages 3767-3782

Mitochondrial reactive oxygen species production and respiratory complex activity in rats with pressure overload-induced heart failure

Author keywords

[No Author keywords available]

Indexed keywords

2,4 DINITROPHENOL; 4 HYDROXYNONENAL; ADENOSINE TRIPHOSPHATE; ALPHA PHENYL N TERT BUTYL NITRONE; ANTIOXIDANT; CITRATE SYNTHASE; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG; AMINE OXIDE; PHENYL-N-TERT-BUTYLNITRONE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); UBIQUINOL CYTOCHROME C REDUCTASE; UNCOUPLING PROTEIN;

EID: 84906937056     PISSN: 00223751     EISSN: 14697793     Source Type: Journal    
DOI: 10.1113/jphysiol.2014.274704     Document Type: Article
Times cited : (56)

References (66)
  • 1
    • 33745201378 scopus 로고    scopus 로고
    • The good, the bad and the ugly in oxygen-sensing: ROS, cytochromes and prolyl-hydroxylases
    • Acker T, Fandrey J & Acker H (2006). The good, the bad and the ugly in oxygen-sensing: ROS, cytochromes and prolyl-hydroxylases. Cardiovasc Res 71, 195-207.
    • (2006) Cardiovasc Res , vol.71 , pp. 195-207
    • Acker, T.1    Fandrey, J.2    Acker, H.3
  • 2
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • Balaban RS, Nemoto S & Finkel T (2005). Mitochondria, oxidants, and aging. Cell 120, 483-495.
    • (2005) Cell , vol.120 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 3
    • 0036328867 scopus 로고    scopus 로고
    • 2 generation in isolated mitochondria
    • 2 generation in isolated mitochondria. J Bioenerg Biomembr 34, 227-233.
    • (2002) J Bioenerg Biomembr , vol.34 , pp. 227-233
    • Barja, G.1
  • 4
    • 0028630737 scopus 로고
    • Biochemical, mechanical and energetic characterization of right ventricular hypertrophy in the ferret heart
    • Baudet S, Kuznetsov A, Merciai N, Gorza L & Ventura-Clapier R (1994). Biochemical, mechanical and energetic characterization of right ventricular hypertrophy in the ferret heart. J Mol Cell Cardiol 26, 1573-1586.
    • (1994) J Mol Cell Cardiol , vol.26 , pp. 1573-1586
    • Baudet, S.1    Kuznetsov, A.2    Merciai, N.3    Gorza, L.4    Ventura-Clapier, R.5
  • 5
    • 0030841350 scopus 로고    scopus 로고
    • Protein oxidation in aging, disease, and oxidative stress
    • Berlett BS & Stadtman ER (1997). Protein oxidation in aging, disease, and oxidative stress. J Biol Chem 272, 20313-20316.
    • (1997) J Biol Chem , vol.272 , pp. 20313-20316
    • Berlett, B.S.1    Stadtman, E.R.2
  • 6
    • 0023785749 scopus 로고
    • Demonstration of free radical generation in 'stunned' myocardium of intact dogs with the use of the spin trap α-phenyl N-tert-butyl nitrone
    • Bolli R, Patel BS, Jeroudi MO, Lai EK & McCay PB (1988). Demonstration of free radical generation in 'stunned' myocardium of intact dogs with the use of the spin trap α-phenyl N-tert-butyl nitrone. J Clin Invest 82, 476-485.
    • (1988) J Clin Invest , vol.82 , pp. 476-485
    • Bolli, R.1    Patel, B.S.2    Jeroudi, M.O.3    Lai, E.K.4    McCay, P.B.5
  • 7
    • 17844393112 scopus 로고    scopus 로고
    • Reversible redox-dependent modulation of mitochondrial aconitase and proteolytic activity during in vivo cardiac ischemia/reperfusion
    • Bulteau AL, Lundberg KC, Ikeda-Saito M, Isaya G & Szweda LI (2005). Reversible redox-dependent modulation of mitochondrial aconitase and proteolytic activity during in vivo cardiac ischemia/reperfusion. Proc Natl Acad Sci U S A 102, 5987-5991.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 5987-5991
    • Bulteau, A.L.1    Lundberg, K.C.2    Ikeda-Saito, M.3    Isaya, G.4    Szweda, L.I.5
  • 9
    • 70349478990 scopus 로고    scopus 로고
    • MicroRNA-210 controls mitochondrial metabolism during hypoxia by repressing the iron-sulfur cluster assembly proteins ISCU1/2
    • Chan SY, Zhang YY, Hemann C, Mahoney CE, Zweier JL & Loscalzo J (2009). MicroRNA-210 controls mitochondrial metabolism during hypoxia by repressing the iron-sulfur cluster assembly proteins ISCU1/2. Cell Metab 10, 273-284.
    • (2009) Cell Metab , vol.10 , pp. 273-284
    • Chan, S.Y.1    Zhang, Y.Y.2    Hemann, C.3    Mahoney, C.E.4    Zweier, J.L.5    Loscalzo, J.6
  • 10
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • Chance B, Sies H & Boveris A (1979). Hydroperoxide metabolism in mammalian organs. Physiol Rev 59, 527-605.
    • (1979) Physiol Rev , vol.59 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 11
    • 77049249588 scopus 로고
    • Respiratory enzymes in oxidative phosphorylation: III. The steady state
    • Chance B & Williams GR (1955). Respiratory enzymes in oxidative phosphorylation: III. The steady state. J Biol Chem 217, 409-427.
    • (1955) J Biol Chem , vol.217 , pp. 409-427
    • Chance, B.1    Williams, G.R.2
  • 12
    • 39549102405 scopus 로고    scopus 로고
    • Ischemic defects in the electron transport chain increase the production of reactive oxygen species from isolated rat heart mitochondria
    • Chen Q, Moghaddas S, Hoppel CL & Lesnefsky EJ (2008). 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, C460-C466.
    • (2008) Am J Physiol Cell Physiol , vol.294
    • Chen, Q.1    Moghaddas, S.2    Hoppel, C.L.3    Lesnefsky, E.J.4
  • 13
    • 0141815741 scopus 로고    scopus 로고
    • Production of reactive oxygen species by mitochondria: central role of complex III
    • Chen Q, Vazquez EJ, Moghaddas S, Hoppel CL & Lesnefsky EJ (2003). Production of reactive oxygen species by mitochondria: central role of complex III. J Biol Chem 278, 36027-36031.
    • (2003) J Biol Chem , vol.278 , pp. 36027-36031
    • Chen, Q.1    Vazquez, E.J.2    Moghaddas, S.3    Hoppel, C.L.4    Lesnefsky, E.J.5
  • 15
    • 84555188518 scopus 로고    scopus 로고
    • Mitochondrial proteome remodelling in pressure overload-induced heart failure: the role of mitochondrial oxidative stress
    • Dai D-F, Hsieh EJ, Liu Y, Chen T, Beyer RP, Chin MT, MacCoss MJ & Rabinovitch PS (2012). Mitochondrial proteome remodelling in pressure overload-induced heart failure: the role of mitochondrial oxidative stress. Cardiovasc Res 93, 79-88.
    • (2012) Cardiovasc Res , vol.93 , pp. 79-88
    • Dai, D.-F.1    Hsieh, E.J.2    Liu, Y.3    Chen, T.4    Beyer, R.P.5    Chin, M.T.6    MacCoss, M.J.7    Rabinovitch, P.S.8
  • 18
    • 0030221307 scopus 로고    scopus 로고
    • Role of oxidative stress in transition of hypertrophy to heart failure
    • Dhalla AK, Hill MF & Singal PK (1996). Role of oxidative stress in transition of hypertrophy to heart failure. J Am Coll Cardiol 28, 506-514.
    • (1996) J Am Coll Cardiol , vol.28 , pp. 506-514
    • Dhalla, A.K.1    Hill, M.F.2    Singal, P.K.3
  • 19
    • 77952364346 scopus 로고    scopus 로고
    • Decreased rates of substrate oxidation ex vivo predict the onset of heart failure and contractile dysfunction in rats with pressure overload
    • Doenst T, Pytel G, Schrepper A, Amorim P, Färber G, Shingu Y, Mohr FW & Schwarzer M (2010). Decreased rates of substrate oxidation ex vivo predict the onset of heart failure and contractile dysfunction in rats with pressure overload. Cardiovasc Res 86, 461-470.
    • (2010) Cardiovasc Res , vol.86 , pp. 461-470
    • Doenst, T.1    Pytel, G.2    Schrepper, A.3    Amorim, P.4    Färber, G.5    Shingu, Y.6    Mohr, F.W.7    Schwarzer, M.8
  • 20
    • 77957003282 scopus 로고
    • Mitochondrial respiratory control and the polarographic measurement of ADP:O ratios
    • Estabrook RW (1967). Mitochondrial respiratory control and the polarographic measurement of ADP:O ratios. Methods Enzymol 10, 41-47.
    • (1967) Methods Enzymol , vol.10 , pp. 41-47
    • Estabrook, R.W.1
  • 21
    • 79960286223 scopus 로고    scopus 로고
    • Signal transduction by reactive oxygen species
    • Finkel T (2011). Signal transduction by reactive oxygen species. J Cell Biol 194, 7-15.
    • (2011) J Cell Biol , vol.194 , pp. 7-15
    • Finkel, T.1
  • 22
    • 14644442283 scopus 로고    scopus 로고
    • Oxygen, oxidative stress, hypoxia, and heart failure
    • Giordano FJ (2005). Oxygen, oxidative stress, hypoxia, and heart failure. J Clin Invest 115, 500-508.
    • (2005) J Clin Invest , vol.115 , pp. 500-508
    • Giordano, F.J.1
  • 23
  • 27
    • 33750452307 scopus 로고    scopus 로고
    • Molecular mechanisms in heart failure: focus on cardiac hypertrophy, inflammation, angiogenesis, and apoptosis
    • Hilfiker-Kleiner D, Landmesser U & Drexler H (2006). Molecular mechanisms in heart failure: focus on cardiac hypertrophy, inflammation, angiogenesis, and apoptosis. J Am Coll Cardiol 48, A56-66.
    • (2006) J Am Coll Cardiol , vol.48
    • Hilfiker-Kleiner, D.1    Landmesser, U.2    Drexler, H.3
  • 29
    • 7044220612 scopus 로고    scopus 로고
    • A possible link between skeletal muscle mitochondrial efficiency and age-induced insulin resistance
    • Iossa S, Mollica MP, Lionetti L, Crescenzo R, Tasso R & Liverini G (2004). A possible link between skeletal muscle mitochondrial efficiency and age-induced insulin resistance. Diabetes 53, 2861-2866.
    • (2004) Diabetes , vol.53 , pp. 2861-2866
    • Iossa, S.1    Mollica, M.P.2    Lionetti, L.3    Crescenzo, R.4    Tasso, R.5    Liverini, G.6
  • 31
    • 0028865472 scopus 로고
    • The antioxidant vitamins and cardiovascular disease. A critical review of epidemiologic and clinical trial data
    • Jha P, Flather M, Lonn E, Farkouh M & Yusuf S (1995). The antioxidant vitamins and cardiovascular disease. A critical review of epidemiologic and clinical trial data. Ann Intern Med 123, 860-872.
    • (1995) Ann Intern Med , vol.123 , pp. 860-872
    • Jha, P.1    Flather, M.2    Lonn, E.3    Farkouh, M.4    Yusuf, S.5
  • 33
    • 0025836574 scopus 로고
    • Decreased activities of ubiquinol:ferricytochrome c oxidoreductase (complex III) and ferrocytochrome c:oxygen oxidoreductase (complex IV) in liver mitochondria from rats with hydroxycobalamin[c-lactam]-induced methylmalonic aciduria
    • Krahenbuhl S, Chang M, Brass EP & Hoppel CL (1991). Decreased activities of ubiquinol:ferricytochrome c oxidoreductase (complex III) and ferrocytochrome c:oxygen oxidoreductase (complex IV) in liver mitochondria from rats with hydroxycobalamin[c-lactam]-induced methylmalonic aciduria. J Biol Chem 266, 20998-21003.
    • (1991) J Biol Chem , vol.266 , pp. 20998-21003
    • Krahenbuhl, S.1    Chang, M.2    Brass, E.P.3    Hoppel, C.L.4
  • 35
    • 80255129364 scopus 로고    scopus 로고
    • Mitochondrial respiratory control and early defects of oxidative phosphorylation in the failing human heart
    • Lemieux H, Semsroth S, Antretter H, Hofer D & Gnaiger E (2011). Mitochondrial respiratory control and early defects of oxidative phosphorylation in the failing human heart. Int J Biochem Cell Biol 43, 1729-1738.
    • (2011) Int J Biochem Cell Biol , vol.43 , pp. 1729-1738
    • Lemieux, H.1    Semsroth, S.2    Antretter, H.3    Hofer, D.4    Gnaiger, E.5
  • 38
    • 79952011065 scopus 로고    scopus 로고
    • In vivo detection of oxidized proteins: a practical approach to tissue-derived mitochondria
    • Maltecca F & Casari G (2010). In vivo detection of oxidized proteins: a practical approach to tissue-derived mitochondria. Methods Mol Biol 648, 257-267.
    • (2010) Methods Mol Biol , vol.648 , pp. 257-267
    • Maltecca, F.1    Casari, G.2
  • 40
    • 41249086364 scopus 로고    scopus 로고
    • Mitochondrial centrality in heart failure
    • Marín-García J & Goldenthal MJ (2008). Mitochondrial centrality in heart failure. Heart Fail Rev 13, 137-150.
    • (2008) Heart Fail Rev , vol.13 , pp. 137-150
    • Marín-García, J.1    Goldenthal, M.J.2
  • 42
    • 42749085693 scopus 로고    scopus 로고
    • Increased mitochondrial uncoupling proteins, respiratory uncoupling and decreased efficiency in the chronically infarcted rat heart
    • Murray AJ, Cole MA, Lygate CA, Carr CA, Stuckey DJ, Little SE, Neubauer S & Clarke K (2008). Increased mitochondrial uncoupling proteins, respiratory uncoupling and decreased efficiency in the chronically infarcted rat heart. J Mol Cell Cardiol 44, 694-700.
    • (2008) J Mol Cell Cardiol , vol.44 , pp. 694-700
    • Murray, A.J.1    Cole, M.A.2    Lygate, C.A.3    Carr, C.A.4    Stuckey, D.J.5    Little, S.E.6    Neubauer, S.7    Clarke, K.8
  • 43
    • 42949126387 scopus 로고    scopus 로고
    • Mitochondrial uncoupling protein 3 and its role in cardiac- and skeletal muscle metabolism
    • Nabben M & Hoeks J (2008). Mitochondrial uncoupling protein 3 and its role in cardiac- and skeletal muscle metabolism. Physiol Behav 94, 259-269.
    • (2008) Physiol Behav , vol.94 , pp. 259-269
    • Nabben, M.1    Hoeks, J.2
  • 45
    • 80052095662 scopus 로고    scopus 로고
    • Assessment of left ventricular function in aortic stenosis
    • Ozkan A, Kapadia S, Tuzcu M & Marwick TH (2011). Assessment of left ventricular function in aortic stenosis. Nat Rev Cardiol 8, 494-501.
    • (2011) Nat Rev Cardiol , vol.8 , pp. 494-501
    • Ozkan, A.1    Kapadia, S.2    Tuzcu, M.3    Marwick, T.H.4
  • 46
    • 0346059551 scopus 로고    scopus 로고
    • Decrease in mitochondrial complex I activity in ischemic/reperfused rat heart: involvement of reactive oxygen species and cardiolipin
    • Paradies G, Petrosillo G, Pistolese M, Di Venosa N, Federici A & Ruggiero FM (2004). Decrease in mitochondrial complex I activity in ischemic/reperfused rat heart: involvement of reactive oxygen species and cardiolipin. Circ Res 94, 53-59.
    • (2004) Circ Res , vol.94 , pp. 53-59
    • Paradies, G.1    Petrosillo, G.2    Pistolese, M.3    Di Venosa, N.4    Federici, A.5    Ruggiero, F.M.6
  • 47
    • 69849097192 scopus 로고    scopus 로고
    • Mitochondrial generation of free radicals and hypoxic signalling
    • Poyton RO, Ball KA & Castello PR (2009). Mitochondrial generation of free radicals and hypoxic signalling. Trends Endocrinol Metab 20, 332-340.
    • (2009) Trends Endocrinol Metab , vol.20 , pp. 332-340
    • Poyton, R.O.1    Ball, K.A.2    Castello, P.R.3
  • 48
    • 47249142777 scopus 로고    scopus 로고
    • Iron-sulfur cluster biogenesis and human disease
    • Rouault TA & Tong WH (2008). Iron-sulfur cluster biogenesis and human disease. Trends Genet 24, 398-407.
    • (2008) Trends Genet , vol.24 , pp. 398-407
    • Rouault, T.A.1    Tong, W.H.2
  • 49
    • 0028239163 scopus 로고
    • Oxidative damage to proteins: spectrophotometric method for carbonyl assay
    • Reznick AZ & Packer L (1994). Oxidative damage to proteins: spectrophotometric method for carbonyl assay. Methods Enzymol 233, 357-363.
    • (1994) Methods Enzymol , vol.233 , pp. 357-363
    • Reznick, A.Z.1    Packer, L.2
  • 50
    • 67650656563 scopus 로고    scopus 로고
    • New aspects of impaired mitochondrial function in heart failure
    • Rosca MG & Hoppel CL (2009). New aspects of impaired mitochondrial function in heart failure. J Bioenerg Biomembr 41, 107-112.
    • (2009) J Bioenerg Biomembr , vol.41 , pp. 107-112
    • Rosca, M.G.1    Hoppel, C.L.2
  • 52
    • 1942452894 scopus 로고    scopus 로고
    • Echocardiographic assessment of global ventricular function using the myocardial performance index in rats with hypertrophy
    • Salemi VM, Pires MD, Cestari IN, Cestari IA, Picard MH, Leirner AA & Mady C (2004). Echocardiographic assessment of global ventricular function using the myocardial performance index in rats with hypertrophy. Artif Organs 28, 332-337.
    • (2004) Artif Organs , vol.28 , pp. 332-337
    • Salemi, V.M.1    Pires, M.D.2    Cestari, I.N.3    Cestari, I.A.4    Picard, M.H.5    Leirner, A.A.6    Mady, C.7
  • 53
    • 0042155851 scopus 로고    scopus 로고
    • Temperature dependence of rat liver mitochondrial respiration with uncoupling of oxidative phosphorylation by fatty acids. Influence of inorganic phosphate
    • Samartsev VN, Chezganova SA, Polishchuk LS, Paydyganov AP, Vidyakina OV & Zeldi IP (2003). Temperature dependence of rat liver mitochondrial respiration with uncoupling of oxidative phosphorylation by fatty acids. Influence of inorganic phosphate. Biochemistry (Mosc) 68, 618-626.
    • (2003) Biochemistry (Mosc) , vol.68 , pp. 618-626
    • Samartsev, V.N.1    Chezganova, S.A.2    Polishchuk, L.S.3    Paydyganov, A.P.4    Vidyakina, O.V.5    Zeldi, I.P.6
  • 54
    • 84155194899 scopus 로고    scopus 로고
    • Biphasic response of skeletal muscle mitochondria to chronic cardiac pressure overload - role of respiratory chain complex activity
    • Schrepper A, Schwarzer M, Schope M, Amorim PA & Doenst T (2012). Biphasic response of skeletal muscle mitochondria to chronic cardiac pressure overload - role of respiratory chain complex activity. J Mol Cell Cardiol 52, 125-135.
    • (2012) J Mol Cell Cardiol , vol.52 , pp. 125-135
    • Schrepper, A.1    Schwarzer, M.2    Schope, M.3    Amorim, P.A.4    Doenst, T.5
  • 55
    • 84874101104 scopus 로고    scopus 로고
    • Pressure overload differentially affects respiratory capacity in interfibrillar and subsarcolemmal mitochondria
    • Schwarzer M, Schrepper A, Amorim PA, Osterholt M & Doenst T (2013). Pressure overload differentially affects respiratory capacity in interfibrillar and subsarcolemmal mitochondria. Am J Physiol Heart Circ Physiol 304, H529-H537.
    • (2013) Am J Physiol Heart Circ Physiol , vol.304
    • Schwarzer, M.1    Schrepper, A.2    Amorim, P.A.3    Osterholt, M.4    Doenst, T.5
  • 57
  • 58
    • 0029765443 scopus 로고    scopus 로고
    • Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants
    • Skulachev VP (1996). Role of uncoupled and non-coupled oxidations in maintenance of safely low levels of oxygen and its one-electron reductants. Q Rev Biophys 29, 169-202.
    • (1996) Q Rev Biophys , vol.29 , pp. 169-202
    • Skulachev, V.P.1
  • 59
    • 77957010982 scopus 로고
    • Citrate synthase
    • Srere PA (1969). Citrate synthase. Methods Enzymol 13, 3-11.
    • (1969) Methods Enzymol , vol.13 , pp. 3-11
    • Srere, P.A.1
  • 60
    • 21244492310 scopus 로고    scopus 로고
    • Myocardial substrate metabolism in the normal and failing heart
    • Stanley WC, Recchia FA & Lopaschuk GD (2005). Myocardial substrate metabolism in the normal and failing heart. Physiol Rev 85, 1093-1129.
    • (2005) Physiol Rev , vol.85 , pp. 1093-1129
    • Stanley, W.C.1    Recchia, F.A.2    Lopaschuk, G.D.3
  • 61
    • 0016794134 scopus 로고
    • Carnitine palmitoyltransferase in bovine fetal heart mitochondria
    • Tomec RJ & Hoppel CL (1975). Carnitine palmitoyltransferase in bovine fetal heart mitochondria. Arch Biochem Biophys 170, 716-723.
    • (1975) Arch Biochem Biophys , vol.170 , pp. 716-723
    • Tomec, R.J.1    Hoppel, C.L.2
  • 63
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens JF (2003). Mitochondrial formation of reactive oxygen species. J Physiol 552, 335-344.
    • (2003) J Physiol , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 64
    • 84878819977 scopus 로고    scopus 로고
    • Quantification of protein carbonylation
    • Wehr NB & Levine RL (2013). Quantification of protein carbonylation. Methods Mol Biol 965, 265-281.
    • (2013) Methods Mol Biol , vol.965 , pp. 265-281
    • Wehr, N.B.1    Levine, R.L.2
  • 65
    • 38749151858 scopus 로고    scopus 로고
    • Phenyl-α-tert-butyl nitrone reverses mitochondrial decay in acute Chagas' disease
    • Wen JJ, Bhatia V, Popov VL & Garg NJ (2006). Phenyl-α-tert-butyl nitrone reverses mitochondrial decay in acute Chagas' disease. Am J Pathol 169, 1953-1964.
    • (2006) Am J Pathol , vol.169 , pp. 1953-1964
    • Wen, J.J.1    Bhatia, V.2    Popov, V.L.3    Garg, N.J.4
  • 66
    • 2042432480 scopus 로고
    • Cytochrome oxidase from beef heart mitochondria
    • Wharton DC & Tzagoloff A (1967). Cytochrome oxidase from beef heart mitochondria. Methods Enzymol 10, 245-250.
    • (1967) Methods Enzymol , vol.10 , pp. 245-250
    • Wharton, D.C.1    Tzagoloff, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.