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Volumn 5, Issue 2, 2015, Pages 356-377

Impact of oxidative stress on exercising skeletal muscle

Author keywords

Antioxidants; Exercise; Force generation; Mitochondria; PGC 1 ; ROS; Skeletal muscle

Indexed keywords

ADRENALIN; ALPHA TOCOPHEROL; ANTIOXIDANT; ASCORBIC ACID; CAROTENOID; CATALASE; COPPER ZINC SUPEROXIDE DISMUTASE; DOPAMINE; GAMMA INTERFERON; GLUTATHIONE; GLUTATHIONE PEROXIDASE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1; LIPOXYGENASE; MANGANESE SUPEROXIDE DISMUTASE; MITOGEN ACTIVATED PROTEIN KINASE P38; MYOSTATIN; NORADRENALIN; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1BETA; PHOSPHOLIPASE A2; REACTIVE OXYGEN METABOLITE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; THIOREDOXIN REDUCTASE 2; TRANSCRIPTION FACTOR FOXO; TUMOR NECROSIS FACTOR; XANTHINE OXIDASE;

EID: 85012073986     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom5020356     Document Type: Review
Times cited : (305)

References (144)
  • 3
    • 29144493361 scopus 로고    scopus 로고
    • Exercise-induced oxidative stress: Myths, realities and physiological relevance
    • Vollaard, N.B.; Shearman, J.P.; Cooper, C.E. Exercise-induced oxidative stress: Myths, realities and physiological relevance. Sports Med. 2005, 35, 1045-1062.
    • (2005) Sports Med , vol.35 , pp. 1045-1062
    • Vollaard, N.B.1    Shearman, J.P.2    Cooper, C.E.3
  • 4
    • 60849119548 scopus 로고    scopus 로고
    • Acute exercise and oxidative stress: A 30 year history
    • Fisher-Wellman, K.; Bloomer, R.J. Acute exercise and oxidative stress: A 30 year history. Dyn. Med. 2009, doi:10.1186/1476-5918-8-1.
    • (2009) Dyn. Med
    • Fisher-Wellman, K.1    Bloomer, R.J.2
  • 6
    • 77955556016 scopus 로고    scopus 로고
    • Effect of physical training on mitochondrial respiration and reactive oxygen species release in skeletal muscle in patients with obesity and type 2 diabetes
    • Hey-Mogensen, M.; Højlund, K.; Vind, B.F.; Wang, L.; Dela, F.; Beck-Nielsen, H.; Fernström, M.; Sahlin, K. Effect of physical training on mitochondrial respiration and reactive oxygen species release in skeletal muscle in patients with obesity and type 2 diabetes. Diabetologia 2010, 53, 1976-1985.
    • (2010) Diabetologia , vol.53 , pp. 1976-1985
    • Hey-Mogensen, M.1    Højlund, K.2    Vind, B.F.3    Wang, L.4    Dela, F.5    Beck-Nielsen, H.6    Fernström, M.7    Sahlin, K.8
  • 8
    • 55949118714 scopus 로고    scopus 로고
    • Exercise-induced oxidative stress: Cellular mechanisms and impact on muscle force production
    • Powers, S.K.; Jackson, M.J. Exercise-induced oxidative stress: Cellular mechanisms and impact on muscle force production. Physiol. Rev. 2008, 88, 1243-1276.
    • (2008) Physiol. Rev , vol.88 , pp. 1243-1276
    • Powers, S.K.1    Jackson, M.J.2
  • 9
    • 13744252782 scopus 로고    scopus 로고
    • Neutrophil activation, antioxidant supplements and exercise-induced oxidative stress
    • Peake, J.; Suzuki, K. Neutrophil activation, antioxidant supplements and exercise-induced oxidative stress. Exerc. Immunol. Rev. 2004, 10, 129-141.
    • (2004) Exerc. Immunol. Rev , vol.10 , pp. 129-141
    • Peake, J.1    Suzuki, K.2
  • 10
    • 34047213532 scopus 로고    scopus 로고
    • Oxidative stress, chronic disease, and muscle wasting
    • Moylan, J.S.; Reid, M.B. Oxidative stress, chronic disease, and muscle wasting. Muscle Nerve 2007, 35, 411-429.
    • (2007) Muscle Nerve , vol.35 , pp. 411-429
    • Moylan, J.S.1    Reid, M.B.2
  • 11
    • 84863667206 scopus 로고    scopus 로고
    • Oxidants, antioxidants, and the beneficial roles of exercise-induced production of reactive species
    • Gomes, E.C.; Silva, A.N.; de Oliveira, M.R. Oxidants, antioxidants, and the beneficial roles of exercise-induced production of reactive species. Oxid. Med. Cell Longev. 2012, 2012, 756132.
    • (2012) Oxid. Med. Cell Longev , vol.2012 , pp. 756132
    • Gomes, E.C.1    Silva, A.N.2    de Oliveira, M.R.3
  • 12
    • 0027377966 scopus 로고
    • Endothelium-derived oxidative stress may contribute to exercise-induced muscle damage
    • Duarte, J.A.; Appell, H.J.; Carvalho, F.; Bastos, M.L.; Soares, J.M. Endothelium-derived oxidative stress may contribute to exercise-induced muscle damage. Int. J. Sports Med. 1993, 14, 440-443.
    • (1993) Int. J. Sports Med , vol.14 , pp. 440-443
    • Duarte, J.A.1    Appell, H.J.2    Carvalho, F.3    Bastos, M.L.4    Soares, J.M.5
  • 13
    • 58249093939 scopus 로고    scopus 로고
    • How mitochondria produce reactive oxygen species
    • Murphy, M.P. How mitochondria produce reactive oxygen species. Biochem. J. 2009, 417, 1-13.
    • (2009) Biochem. J , vol.417 , pp. 1-13
    • Murphy, M.P.1
  • 14
    • 77952541558 scopus 로고    scopus 로고
    • The sites and topology of mitochondrial superoxide production
    • Brand, M.D. The sites and topology of mitochondrial superoxide production. Exp. Gerontol. 2010, 45, 466-472.
    • (2010) Exp. Gerontol , vol.45 , pp. 466-472
    • Brand, M.D.1
  • 15
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • St-Pierre, J.; Buckingham, J.A.; Roebuck, S.J.; Brand, M.D. Topology of superoxide production from different sites in the mitochondrial electron transport chain. J. Biol. Chem. 2002, 277, 44784-44790.
    • (2002) J. Biol. Chem , vol.277 , pp. 44784-44790
    • St-Pierre, J.1    Buckingham, J.A.2    Roebuck, S.J.3    Brand, M.D.4
  • 16
    • 84878009179 scopus 로고    scopus 로고
    • Sites of superoxide and hydrogen peroxide production during fatty acid oxidation in rat skeletal muscle mitochondria
    • Perevoshchikova, I.V.; Quinlan, C.L.; Orr, A.L.; Gerencser, A.A.; Brand, M.D. Sites of superoxide and hydrogen peroxide production during fatty acid oxidation in rat skeletal muscle mitochondria. Free Radic. Biol. Med. 2013, 61, 298-309.
    • (2013) Free Radic. Biol. Med , vol.61 , pp. 298-309
    • Perevoshchikova, I.V.1    Quinlan, C.L.2    Orr, A.L.3    Gerencser, A.A.4    Brand, M.D.5
  • 17
    • 84900483723 scopus 로고    scopus 로고
    • Production of superoxide/H2O2 by dihydroorotate dehydrogenase in rat skeletal muscle mitochondria
    • Hey-Mogensen, M.; Goncalves, R.L.; Orr, A.L.; Brand, M.D. Production of superoxide/H2O2 by dihydroorotate dehydrogenase in rat skeletal muscle mitochondria. Free Radic. Biol. Med. 2014, 72, 149-155.
    • (2014) Free Radic. Biol. Med , vol.72 , pp. 149-155
    • Hey-Mogensen, M.1    Goncalves, R.L.2    Orr, A.L.3    Brand, M.D.4
  • 18
    • 0033369476 scopus 로고    scopus 로고
    • Mitochondrial oxygen radical generation and leak: Sites of production in states 4 and 3, organ specificity, and relation to aging and longevity
    • Barja, G. Mitochondrial oxygen radical generation and leak: Sites of production in states 4 and 3, organ specificity, and relation to aging and longevity. J. Bioenerg. Biomembr. 1999, 31, 347-366.
    • (1999) J. Bioenerg. Biomembr , vol.31 , pp. 347-366
    • Barja, G.1
  • 19
    • 10344221083 scopus 로고    scopus 로고
    • Complex III releases superoxide to both sides of the inner mitochondrial membrane
    • Muller, F.L.; Liu, Y.; van Remmen, H. Complex III releases superoxide to both sides of the inner mitochondrial membrane. J. Biol. Chem. 2004, 279, 49064-49073.
    • (2004) J. Biol. Chem , vol.279 , pp. 49064-49073
    • Muller, F.L.1    Liu, Y.2    van Remmen, H.3
  • 20
    • 84920520304 scopus 로고    scopus 로고
    • Sites of superoxide and hydrogen peroxide production by muscle mitochondria assessed ex vivo under conditions mimicking rest and exercise
    • Goncalves, R.L.; Quinlan, C.L.; Perevoshchikova, I.V.; Hey-Mogensen, M.; Brand, M.D. Sites of superoxide and hydrogen peroxide production by muscle mitochondria assessed ex vivo under conditions mimicking rest and exercise. J. Biol. Chem. 2015, 290, 209-227.
    • (2015) J. Biol. Chem , vol.290 , pp. 209-227
    • Goncalves, R.L.1    Quinlan, C.L.2    Perevoshchikova, I.V.3    Hey-Mogensen, M.4    Brand, M.D.5
  • 21
    • 33846794822 scopus 로고    scopus 로고
    • The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology
    • Bedard, K.; Krause, K.H. The NOX family of ROS-generating NADPH oxidases: Physiology and pathophysiology. Physiol. Rev. 2007, 87, 245-313.
    • (2007) Physiol. Rev , vol.87 , pp. 245-313
    • Bedard, K.1    Krause, K.H.2
  • 22
    • 84907455071 scopus 로고    scopus 로고
    • Nox family NADPH oxidases: Molecular mechanisms of activation
    • Brandes, R.P.; Weissmann, N.; Schröder, K. Nox family NADPH oxidases: Molecular mechanisms of activation. Free Radic. Biol. Med. 2014, 76, 208-226.
    • (2014) Free Radic. Biol. Med , vol.76 , pp. 208-226
    • Brandes, R.P.1    Weissmann, N.2    Schröder, K.3
  • 23
    • 0038508928 scopus 로고    scopus 로고
    • Skeletal muscle sarcoplasmic reticulum contains a NADH-dependent oxidase that generates superoxide
    • Xia, R.; Webb, J.A.; Gnall, L.L.; Cutler, K.; Abramson, J.J. Skeletal muscle sarcoplasmic reticulum contains a NADH-dependent oxidase that generates superoxide. Am. J. Physiol. Cell Physiol. 2003, 285, C215-C221.
    • (2003) Am. J. Physiol. Cell Physiol , vol.285 , pp. C215-C221
    • Xia, R.1    Webb, J.A.2    Gnall, L.L.3    Cutler, K.4    Abramson, J.J.5
  • 24
    • 68149117477 scopus 로고    scopus 로고
    • Reciprocal amplification of ROS and Ca2+ signals in stressed mdx dystrophic skeletal muscle fibers
    • Shkryl, V.M.; Martins, A.S.; Ullrich, N.D.; Nowycky, M.C.; Niggli, E.; Shirokova, N. Reciprocal amplification of ROS and Ca2+ signals in stressed mdx dystrophic skeletal muscle fibers. Pflugers Arch. 2009, 458, 915-928.
    • (2009) Pflugers Arch , vol.458 , pp. 915-928
    • Shkryl, V.M.1    Martins, A.S.2    Ullrich, N.D.3    Nowycky, M.C.4    Niggli, E.5    Shirokova, N.6
  • 25
    • 84872433353 scopus 로고    scopus 로고
    • Studies of mitochondrial and nonmitochondrial sources implicate nicotinamide adenine dinucleotide phosphate oxidase(s) in the increased skeletal muscle superoxide generation that occurs during contractile activity
    • Sakellariou, G.K.; Vasilaki, A.; Palomero, J.; Kayani, A.; Zibrik, L.; McArdle, A.; Jackson, M.J. Studies of mitochondrial and nonmitochondrial sources implicate nicotinamide adenine dinucleotide phosphate oxidase(s) in the increased skeletal muscle superoxide generation that occurs during contractile activity. Antioxid. Redox Signal. 2013, 18, 603-621.
    • (2013) Antioxid. Redox Signal , vol.18 , pp. 603-621
    • Sakellariou, G.K.1    Vasilaki, A.2    Palomero, J.3    Kayani, A.4    Zibrik, L.5    McArdle, A.6    Jackson, M.J.7
  • 26
    • 1542373629 scopus 로고    scopus 로고
    • NADH oxidase activity of rat cardiac sarcoplasmic reticulum regulates calcium-induced calcium release
    • Cherednichenko, G.; Zima, A.V.; Feng, W.; Schaefer, S.; Blatter, L.A.; Pessah, I.N. NADH oxidase activity of rat cardiac sarcoplasmic reticulum regulates calcium-induced calcium release. Circ. Res. 2004, 94, 478-486.
    • (2004) Circ. Res , vol.94 , pp. 478-486
    • Cherednichenko, G.1    Zima, A.V.2    Feng, W.3    Schaefer, S.4    Blatter, L.A.5    Pessah, I.N.6
  • 27
    • 33749259960 scopus 로고    scopus 로고
    • Myotube depolarization generates reactive oxygen species through NAD(P)H oxidase; ROS-elicited Ca2+ stimulates ERK, CREB, early genes
    • Espinosa, A.; Leiva, A.; Peña, M.; Müller, M.; Debandi, A.; Hidalgo, C.; Carrasco, M.A.; Jaimovich, E. Myotube depolarization generates reactive oxygen species through NAD(P)H oxidase; ROS-elicited Ca2+ stimulates ERK, CREB, early genes. J. Cell Physiol. 2006, 209, 379-388.
    • (2006) J. Cell Physiol , vol.209 , pp. 379-388
    • Espinosa, A.1    Leiva, A.2    Peña, M.3    Müller, M.4    Debandi, A.5    Hidalgo, C.6    Carrasco, M.A.7    Jaimovich, E.8
  • 28
    • 33748755208 scopus 로고    scopus 로고
    • A transverse tubule NADPH oxidase activity stimulates calcium release from isolated triads via ryanodine receptor type 1 S-glutathionylation
    • Hidalgo, C.; Sánchez, G.; Barrientos, G.; Aracena-Parks, P. A transverse tubule NADPH oxidase activity stimulates calcium release from isolated triads via ryanodine receptor type 1 S-glutathionylation. J. Biol. Chem. 2006, 281, 26473-26482.
    • (2006) J. Biol. Chem , vol.281 , pp. 26473-26482
    • Hidalgo, C.1    Sánchez, G.2    Barrientos, G.3    Aracena-Parks, P.4
  • 29
    • 59049099466 scopus 로고    scopus 로고
    • NADPH oxidase and hydrogen peroxide mediate insulin-induced calcium increase in skeletal muscle cells
    • Espinosa, A.; García, A.; Härtel, S.; Hidalgo, C.; Jaimovich, E. NADPH oxidase and hydrogen peroxide mediate insulin-induced calcium increase in skeletal muscle cells. J. Biol. Chem. 2009, 284, 2568-2575.
    • (2009) J. Biol. Chem , vol.284 , pp. 2568-2575
    • Espinosa, A.1    García, A.2    Härtel, S.3    Hidalgo, C.4    Jaimovich, E.5
  • 30
    • 0037105296 scopus 로고    scopus 로고
    • Structure and function of xanthine oxidoreductase: Where are we now?
    • Harrison, R. Structure and function of xanthine oxidoreductase: Where are we now? Free Radic. Biol. Med. 2002, 33, 774-797.
    • (2002) Free Radic. Biol. Med , vol.33 , pp. 774-797
    • Harrison, R.1
  • 31
    • 0347628958 scopus 로고    scopus 로고
    • Xanthine oxidase and activated neutrophils cause oxidative damage to skeletal muscle after contractile claudication
    • Judge, A.R.; Dodd, S.L. Xanthine oxidase and activated neutrophils cause oxidative damage to skeletal muscle after contractile claudication. Am. J. Physiol. Heart Circ. Physiol. 2004, 286, H252-H256.
    • (2004) Am. J. Physiol. Heart Circ. Physiol , vol.286 , pp. H252-H256
    • Judge, A.R.1    Dodd, S.L.2
  • 32
    • 84873459937 scopus 로고    scopus 로고
    • Oxygen consumption and usage during physical exercise: The balance between oxidative stress and ROS-dependent adaptive signaling
    • Radák, Z.; Zhao, Z.; Koltai, E.; Ohno, H.; Atalay, M. Oxygen consumption and usage during physical exercise: The balance between oxidative stress and ROS-dependent adaptive signaling. Antioxid. Redox Signal. 2013, 18, 1208-1246.
    • (2013) Antioxid. Redox Signal , vol.18 , pp. 1208-1246
    • Radák, Z.1    Zhao, Z.2    Koltai, E.3    Ohno, H.4    Atalay, M.5
  • 33
    • 84884547174 scopus 로고    scopus 로고
    • Exercise training attenuates aging-associated mitochondrial dysfunction in rat skeletal muscle: Role of PGC-1α
    • Kang, C.; Chung, E.; Diffee, G.; Ji, L.L. Exercise training attenuates aging-associated mitochondrial dysfunction in rat skeletal muscle: Role of PGC-1α. Exp. Gerontol. 2013, 48, 1343-1350.
    • (2013) Exp. Gerontol , vol.48 , pp. 1343-1350
    • Kang, C.1    Chung, E.2    Diffee, G.3    Ji, L.L.4
  • 37
    • 0037067321 scopus 로고    scopus 로고
    • Cytosolic phospholipase A2 (cPLA2) regulation of human monocyte NADPH oxidase activity. cPLA2 affects translocation but not phosphorylation of p67(phox) and p47(phox)
    • Zhao, X.; Bey, E.A.; Wientjes, F.B.; Cathcart, M.K. Cytosolic phospholipase A2 (cPLA2) regulation of human monocyte NADPH oxidase activity. cPLA2 affects translocation but not phosphorylation of p67(phox) and p47(phox). J. Biol. Chem. 2002, 277, 25385-25392.
    • (2002) J. Biol. Chem , vol.277 , pp. 25385-25392
    • Zhao, X.1    Bey, E.A.2    Wientjes, F.B.3    Cathcart, M.K.4
  • 38
    • 78649741794 scopus 로고    scopus 로고
    • Mitochondrial phospholipase A2 activated by reactive oxygen species in heart mitochondria induces mild uncoupling
    • Ježek, J.; Jaburek, M.; Zelenka, J.; Ježek, P. Mitochondrial phospholipase A2 activated by reactive oxygen species in heart mitochondria induces mild uncoupling. Physiol. Res. 2010, 59, 737-747.
    • (2010) Physiol. Res , vol.59 , pp. 737-747
    • Ježek, J.1    Jaburek, M.2    Zelenka, J.3    Ježek, P.4
  • 39
    • 33645969808 scopus 로고    scopus 로고
    • Calcium-independent phospholipase A2 modulates cytosolic oxidant activity and contractile function in murine skeletal muscle cells
    • Gong, M.C.; Arbogast, S.; Guo, Z.; Mathenia, J.; Su, W.; Reid, M.B. Calcium-independent phospholipase A2 modulates cytosolic oxidant activity and contractile function in murine skeletal muscle cells. J. Appl. Physiol. 2006, 100, 399-405.
    • (2006) J. Appl. Physiol , vol.100 , pp. 399-405
    • Gong, M.C.1    Arbogast, S.2    Guo, Z.3    Mathenia, J.4    Su, W.5    Reid, M.B.6
  • 40
    • 33645969578 scopus 로고    scopus 로고
    • Redox modulation of contractile function in respiratory and limb skeletal muscle
    • Smith, M.A.; Reid, M.B. Redox modulation of contractile function in respiratory and limb skeletal muscle. Respir. Physiol. Neurobiol. 2006, 151, 229-241.
    • (2006) Respir. Physiol. Neurobiol , vol.151 , pp. 229-241
    • Smith, M.A.1    Reid, M.B.2
  • 41
    • 0034813092 scopus 로고    scopus 로고
    • Adaptation to exercise-induced oxidative stress: From muscle to brain
    • Radák, Z.; Taylor, A.W.; Ohno, H.; Goto, S. Adaptation to exercise-induced oxidative stress: From muscle to brain. Exerc. Immunol. Rev. 2001, 7, 90-107.
    • (2001) Exerc. Immunol. Rev , vol.7 , pp. 90-107
    • Radák, Z.1    Taylor, A.W.2    Ohno, H.3    Goto, S.4
  • 42
    • 37849040918 scopus 로고    scopus 로고
    • Free radicals and muscle fatigue: Of ROS, canaries, and the IOC
    • Reid, M.B. Free radicals and muscle fatigue: Of ROS, canaries, and the IOC. Free Radic. Biol. Med. 2008, 44, 169-179.
    • (2008) Free Radic. Biol. Med , vol.44 , pp. 169-179
    • Reid, M.B.1
  • 43
    • 38349048508 scopus 로고    scopus 로고
    • Skeletal muscle fatigue: Cellular mechanisms
    • Allen, D.G.; Lamb, G.D.; Westerblad, H. Skeletal muscle fatigue: Cellular mechanisms. Physiol. Rev. 2008, 88, 287-332.
    • (2008) Physiol. Rev , vol.88 , pp. 287-332
    • Allen, D.G.1    Lamb, G.D.2    Westerblad, H.3
  • 44
    • 79955415655 scopus 로고    scopus 로고
    • Acute effects of reactive oxygen and nitrogen species on the contractile function of skeletal muscle
    • Lamb, G.D.; Westerblad, H. Acute effects of reactive oxygen and nitrogen species on the contractile function of skeletal muscle. J. Physiol. 2011, 589, 2119-2127.
    • (2011) J. Physiol , vol.589 , pp. 2119-2127
    • Lamb, G.D.1    Westerblad, H.2
  • 45
    • 0037232657 scopus 로고    scopus 로고
    • Effects of oxidation and reduction on contractile function in skeletal muscle fibres of the rat
    • Lamb, G.D.; Posterino, G.S. Effects of oxidation and reduction on contractile function in skeletal muscle fibres of the rat. J. Physiol. 2003, 546, 149-163.
    • (2003) J. Physiol , vol.546 , pp. 149-163
    • Lamb, G.D.1    Posterino, G.S.2
  • 46
    • 0037444666 scopus 로고    scopus 로고
    • Effects of oxidation and cytosolic redox conditions on excitation-contraction coupling in rat skeletal muscle
    • Posterino, G.S.; Cellini, M.A.; Lamb, G.D. Effects of oxidation and cytosolic redox conditions on excitation-contraction coupling in rat skeletal muscle. J. Physiol. 2003, 547, 807-823.
    • (2003) J. Physiol , vol.547 , pp. 807-823
    • Posterino, G.S.1    Cellini, M.A.2    Lamb, G.D.3
  • 47
    • 84921030936 scopus 로고    scopus 로고
    • Antioxidant treatments do not improve force recovery after fatiguing stimulation of mouse skeletal muscle fibres
    • Cheng, A.J.; Bruton, J.D.; Lanner, J.T.; Westerblad, H. Antioxidant treatments do not improve force recovery after fatiguing stimulation of mouse skeletal muscle fibres. J. Physiol. 2015, 593, 457-472.
    • (2015) J. Physiol , vol.593 , pp. 457-472
    • Cheng, A.J.1    Bruton, J.D.2    Lanner, J.T.3    Westerblad, H.4
  • 48
    • 0032103008 scopus 로고    scopus 로고
    • Effect of hydrogen peroxide and dithiothreitol on contractile function of single skeletal muscle fibres from the mouse
    • Andrade, F.H.; Reid, M.B.; Allen, D.G.; Westerblad, H. Effect of hydrogen peroxide and dithiothreitol on contractile function of single skeletal muscle fibres from the mouse. J. Physiol. 1998, 509, 565-575.
    • (1998) J. Physiol , vol.509 , pp. 565-575
    • Andrade, F.H.1    Reid, M.B.2    Allen, D.G.3    Westerblad, H.4
  • 49
    • 55849141926 scopus 로고    scopus 로고
    • Changes in actin structural transitions associated with oxidative inhibition of muscle contraction
    • Prochniewicz, E.; Spakowicz, D.; Thomas, D.D. Changes in actin structural transitions associated with oxidative inhibition of muscle contraction. Biochemistry 2008, 47, 11811-11817.
    • (2008) Biochemistry , vol.47 , pp. 11811-11817
    • Prochniewicz, E.1    Spakowicz, D.2    Thomas, D.D.3
  • 50
    • 84858226713 scopus 로고    scopus 로고
    • S-glutathionylation of troponin I (fast) increases contractile apparatus Ca2+ sensitivity in fast-twitch muscle fibres of rats and humans
    • Mollica, J.P.; Dutka, T.L.; Merry, T.L.; Lamboley, C.R.; McConell, G.K.; McKenna, M.J.; Murphy, R.M.; Lamb, G.D. S-glutathionylation of troponin I (fast) increases contractile apparatus Ca2+ sensitivity in fast-twitch muscle fibres of rats and humans. J. Physiol. 2012, 590, 1443-1463.
    • (2012) J. Physiol , vol.590 , pp. 1443-1463
    • Mollica, J.P.1    Dutka, T.L.2    Merry, T.L.3    Lamboley, C.R.4    McConell, G.K.5    McKenna, M.J.6    Murphy, R.M.7    Lamb, G.D.8
  • 52
    • 84872364008 scopus 로고    scopus 로고
    • Atrogin-1, MuRF-1, and sarcopenia
    • Gumucio, J.P.; Mendias, C.L. Atrogin-1, MuRF-1, and sarcopenia. Endocrine 2013, 43, 12-21.
    • (2013) Endocrine , vol.43 , pp. 12-21
    • Gumucio, J.P.1    Mendias, C.L.2
  • 53
    • 20544438018 scopus 로고    scopus 로고
    • MURF-1 and MURF-2 target a specific subset of myofibrillar proteins redundantly: Towards understanding MURF-dependent muscle ubiquitination
    • Witt, S.H.; Granzier, H.; Witt, C.C.; Labeit, S. MURF-1 and MURF-2 target a specific subset of myofibrillar proteins redundantly: Towards understanding MURF-dependent muscle ubiquitination. J. Mol. Biol. 2005, 350, 713-722.
    • (2005) J. Mol. Biol , vol.350 , pp. 713-722
    • Witt, S.H.1    Granzier, H.2    Witt, C.C.3    Labeit, S.4
  • 54
    • 67449132363 scopus 로고    scopus 로고
    • During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation
    • Cohen, S.; Brault, J.J.; Gygi, S.P.; Glass, D.J.; Valenzuela, D.M.; Gartner, C.; Latres, E.; Goldberg, A.L. During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation. J. Cell Biol. 2009, 185, 1083-1095.
    • (2009) J. Cell Biol , vol.185 , pp. 1083-1095
    • Cohen, S.1    Brault, J.J.2    Gygi, S.P.3    Glass, D.J.4    Valenzuela, D.M.5    Gartner, C.6    Latres, E.7    Goldberg, A.L.8
  • 55
    • 0032747796 scopus 로고    scopus 로고
    • Antioxidants and oxidative stress in exercise
    • Ji, L.L. Antioxidants and oxidative stress in exercise. Proc. Soc. Exp. Biol. Med. 1999, 222, 283-292.
    • (1999) Proc. Soc. Exp. Biol. Med , vol.222 , pp. 283-292
    • Ji, L.L.1
  • 60
    • 0023257674 scopus 로고
    • Formation and reduction of glutathione-protein mixed disulfides during oxidative stress. A study with isolated hepatocytes and menadione (2-methyl-1,4-naphthoquinone)
    • Bellomo, G.; Mirabelli, F.; DiMonte, D.; Richelmi, P.; Thor, H.; Orrenius, C.; Orrenius, S. Formation and reduction of glutathione-protein mixed disulfides during oxidative stress. A study with isolated hepatocytes and menadione (2-methyl-1,4-naphthoquinone). Biochem. Pharmacol. 1987, 36, 1313-1320.
    • (1987) Biochem. Pharmacol , vol.36 , pp. 1313-1320
    • Bellomo, G.1    Mirabelli, F.2    DiMonte, D.3    Richelmi, P.4    Thor, H.5    Orrenius, C.6    Orrenius, S.7
  • 61
    • 0026438913 scopus 로고
    • Glutathione and antioxidant enzymes in skeletal muscle: Effects of fiber type and exercise intensity
    • Ji, L.L.; Fu, R.; Mitchell, E.W. Glutathione and antioxidant enzymes in skeletal muscle: Effects of fiber type and exercise intensity. J. Appl. Physiol. 1992, 73, 1854-1859.
    • (1992) J. Appl. Physiol , vol.73 , pp. 1854-1859
    • Ji, L.L.1    Fu, R.2    Mitchell, E.W.3
  • 62
    • 0021859601 scopus 로고
    • Changes in the glutathione status of plasma, liver and muscle following exhaustive exercise in rats
    • Lew, H.; Pyke, S.; Quintanilha, A. Changes in the glutathione status of plasma, liver and muscle following exhaustive exercise in rats. FEBS Lett. 1985, 185, 262-266.
    • (1985) FEBS Lett , vol.185 , pp. 262-266
    • Lew, H.1    Pyke, S.2    Quintanilha, A.3
  • 63
    • 0027526581 scopus 로고
    • Enzymes of glutathione synthesis in dog skeletal muscles and their response to training
    • Marin, E.; Kretzschmar, M.; Arokoski, J.; Hänninen, O.; Klinger, W. Enzymes of glutathione synthesis in dog skeletal muscles and their response to training. Acta Physiol. Scand. 1993, 147, 369-373.
    • (1993) Acta Physiol. Scand , vol.147 , pp. 369-373
    • Marin, E.1    Kretzschmar, M.2    Arokoski, J.3    Hänninen, O.4    Klinger, W.5
  • 64
    • 0031032934 scopus 로고    scopus 로고
    • Adaptations of glutathione antioxidant system to endurance training are tissue and muscle fiber specific
    • Leeuwenburgh, C.; Hollander, J.; Leichtweis, S.; Griffiths, M.; Gore, M.; Ji, L.L. Adaptations of glutathione antioxidant system to endurance training are tissue and muscle fiber specific. Am. J. Physiol. 1997, 272, R363-R369.
    • (1997) Am. J. Physiol , vol.272 , pp. R363-R369
    • Leeuwenburgh, C.1    Hollander, J.2    Leichtweis, S.3    Griffiths, M.4    Gore, M.5    Ji, L.L.6
  • 65
    • 0029198208 scopus 로고
    • Exercise and oxidative stress: Role of the cellular antioxidant systems
    • Ji, L.L. Exercise and oxidative stress: Role of the cellular antioxidant systems. Exerc. Sport Sci. Rev. 1995, 23, 135-166.
    • (1995) Exerc. Sport Sci. Rev , vol.23 , pp. 135-166
    • Ji, L.L.1
  • 66
    • 0029022127 scopus 로고
    • Oxidants and antioxidants in exercise
    • Sen, C.K. Oxidants and antioxidants in exercise. J. Appl. Physiol. 1995, 79, 675-686.
    • (1995) J. Appl. Physiol , vol.79 , pp. 675-686
    • Sen, C.K.1
  • 68
    • 37849002320 scopus 로고    scopus 로고
    • Modulation of skeletal muscle antioxidant defense by exercise: Role of redox signaling
    • Ji, L.L. Modulation of skeletal muscle antioxidant defense by exercise: Role of redox signaling. Free Radic. Biol. Med. 2008, 44, 142-152.
    • (2008) Free Radic. Biol. Med , vol.44 , pp. 142-152
    • Ji, L.L.1
  • 69
  • 71
    • 0032862719 scopus 로고    scopus 로고
    • Superoxide dismutase gene expression in skeletal muscle: Fiber-specific adaptation to endurance training
    • Hollander, J.; Fiebig, R.; Gore, M.; Bejma, J.; Ookawara, T.; Ohno, H.; Ji, L.L. Superoxide dismutase gene expression in skeletal muscle: Fiber-specific adaptation to endurance training. Am. J. Physiol. 1999, 277, R856-R862.
    • (1999) Am. J. Physiol , vol.277 , pp. R856-R862
    • Hollander, J.1    Fiebig, R.2    Gore, M.3    Bejma, J.4    Ookawara, T.5    Ohno, H.6    Ji, L.L.7
  • 72
    • 33846876334 scopus 로고    scopus 로고
    • Effects of aerobic exercise training on antioxidant enzyme activities and mRNA levels in soleus muscle from young and aged rats
    • Lambertucci, R.H.; Levada-Pires, A.C.; Rossoni, L.V.; Curi, R.; Pithon-Curi, T.C. Effects of aerobic exercise training on antioxidant enzyme activities and mRNA levels in soleus muscle from young and aged rats. Mech. Ageing Dev. 2007, 128, 267-275.
    • (2007) Mech. Ageing Dev , vol.128 , pp. 267-275
    • Lambertucci, R.H.1    Levada-Pires, A.C.2    Rossoni, L.V.3    Curi, R.4    Pithon-Curi, T.C.5
  • 74
    • 0026552277 scopus 로고
    • Responses of glutathione system and antioxidant enzymes to exhaustive exercise and hydroperoxide
    • Ji, L.L.; Fu, R. Responses of glutathione system and antioxidant enzymes to exhaustive exercise and hydroperoxide. J. Appl. Physiol. 1992, 72, 549-554.
    • (1992) J. Appl. Physiol , vol.72 , pp. 549-554
    • Ji, L.L.1    Fu, R.2
  • 75
    • 0027730593 scopus 로고
    • Acute exercise and skeletal muscle antioxidant and metabolic enzymes: Effects of fiber type and age
    • Lawler, J.M.; Powers, S.K.; Visser, T.; van Dijk, H.; Kordus, M.J.; Ji, L.L. Acute exercise and skeletal muscle antioxidant and metabolic enzymes: Effects of fiber type and age. Am. J. Physiol. 1993, 265, R1344-R1350.
    • (1993) Am. J. Physiol , vol.265 , pp. R1344-R1350
    • Lawler, J.M.1    Powers, S.K.2    Visser, T.3    van Dijk, H.4    Kordus, M.J.5    Ji, L.L.6
  • 76
    • 0034950434 scopus 로고    scopus 로고
    • Superoxide dismutase gene expression is activated by a single bout of exercise in rat skeletal muscle
    • Hollander, J.; Fiebig, R.; Gore, M.; Ookawara, T.; Ohno, H.; Ji, L.L. Superoxide dismutase gene expression is activated by a single bout of exercise in rat skeletal muscle. Pflugers Arch. 2001, 442, 426-434.
    • (2001) Pflugers Arch , vol.442 , pp. 426-434
    • Hollander, J.1    Fiebig, R.2    Gore, M.3    Ookawara, T.4    Ohno, H.5    Ji, L.L.6
  • 77
  • 78
    • 0029163219 scopus 로고
    • Superoxide dismutase derivative reduces oxidative damage in skeletal muscle of rats during exhaustive exercise
    • Radák, Z.; Asano, K.; Inoue, M.; Kizaki, T.; Oh-Ishi, S.; Suzuki, K.; Taniguchi, N.; Ohno, H. Superoxide dismutase derivative reduces oxidative damage in skeletal muscle of rats during exhaustive exercise. J. Appl. Physiol. 1995, 79, 129-135.
    • (1995) J. Appl. Physiol , vol.79 , pp. 129-135
    • Radák, Z.1    Asano, K.2    Inoue, M.3    Kizaki, T.4    Oh-Ishi, S.5    Suzuki, K.6    Taniguchi, N.7    Ohno, H.8
  • 79
    • 0023893173 scopus 로고
    • Lipid peroxidation and scavenger enzymes during exercise: Adaptive response to training
    • Alessio, H.M.; Goldfarb, A.H. Lipid peroxidation and scavenger enzymes during exercise: Adaptive response to training. J. Appl. Physiol. 1988, 64, 1333-1336.
    • (1988) J. Appl. Physiol , vol.64 , pp. 1333-1336
    • Alessio, H.M.1    Goldfarb, A.H.2
  • 80
    • 0035478983 scopus 로고    scopus 로고
    • Oxidative stress in athletes during extreme endurance exercise
    • Mastaloudis, A.; Leonard, S.W.; Traber, M.G. Oxidative stress in athletes during extreme endurance exercise. Free Radic. Biol. Med. 2001, 31, 911-922.
    • (2001) Free Radic. Biol. Med , vol.31 , pp. 911-922
    • Mastaloudis, A.1    Leonard, S.W.2    Traber, M.G.3
  • 83
    • 0028926381 scopus 로고
    • Measurement of serum lipid peroxidation during exercise using three different methods: Diene conjugation, thiobarbituric acid reactive material and fluorescent chromolipids
    • Vasankari, T.; Kujala, U.; Heinonen, O.; Kapanen, J.; Ahotupa, M. Measurement of serum lipid peroxidation during exercise using three different methods: Diene conjugation, thiobarbituric acid reactive material and fluorescent chromolipids. Clin. Chim. Acta 1995, 234, 63-69.
    • (1995) Clin. Chim. Acta , vol.234 , pp. 63-69
    • Vasankari, T.1    Kujala, U.2    Heinonen, O.3    Kapanen, J.4    Ahotupa, M.5
  • 84
    • 0033820864 scopus 로고    scopus 로고
    • Influence of one bout of vigorous exercise on ascorbic acid in plasma and oxidative damage to DNA in blood cells and muscle in untrained rats
    • Umegaki, K.; Daohua, P.; Sugisawa, A.; Kimura, M.; Higuchi, M. Influence of one bout of vigorous exercise on ascorbic acid in plasma and oxidative damage to DNA in blood cells and muscle in untrained rats. J. Nutr. Biochem. 2000, 11, 401-407.
    • (2000) J. Nutr. Biochem , vol.11 , pp. 401-407
    • Umegaki, K.1    Daohua, P.2    Sugisawa, A.3    Kimura, M.4    Higuchi, M.5
  • 85
  • 86
    • 0028331680 scopus 로고
    • Influence of exercise and fiber type on antioxidant enzyme activity in rat skeletal muscle
    • Powers, S.K.; Criswell, D.; Lawler, J.; Ji, L.L.; Martin, D.; Herb, R.A.; Dudley, G. Influence of exercise and fiber type on antioxidant enzyme activity in rat skeletal muscle. Am. J. Physiol. 1994, 266, R375-R380.
    • (1994) Am. J. Physiol , vol.266 , pp. R375-R380
    • Powers, S.K.1    Criswell, D.2    Lawler, J.3    Ji, L.L.4    Martin, D.5    Herb, R.A.6    Dudley, G.7
  • 87
    • 0036452555 scopus 로고    scopus 로고
    • Exercise training decreases DNA damage and increases DNA repair and resistance against oxidative stress of proteins in aged rat skeletal muscle
    • Radák, Z.; Naito, H.; Kaneko, T.; Tahara, S.; Nakamoto, H.; Takahashi, R.; Cardozo-Pelaez, F.; Goto, S. Exercise training decreases DNA damage and increases DNA repair and resistance against oxidative stress of proteins in aged rat skeletal muscle. Pflugers Arch. 2002, 445, 273-278.
    • (2002) Pflugers Arch , vol.445 , pp. 273-278
    • Radák, Z.1    Naito, H.2    Kaneko, T.3    Tahara, S.4    Nakamoto, H.5    Takahashi, R.6    Cardozo-Pelaez, F.7    Goto, S.8
  • 88
    • 37849004479 scopus 로고    scopus 로고
    • Systemic adaptation to oxidative challenge induced by regular exercise
    • Radák, Z.; Chung, H.Y.; Goto, S. Systemic adaptation to oxidative challenge induced by regular exercise. Free Radic. Biol. Med. 2008, 44, 153-159.
    • (2008) Free Radic. Biol. Med , vol.44 , pp. 153-159
    • Radák, Z.1    Chung, H.Y.2    Goto, S.3
  • 89
    • 85006974482 scopus 로고    scopus 로고
    • The “Goldilocks Zone” from a redox perspective-Adaptive vs. deleterious responses to oxidative stress in striated muscle
    • Alleman, R.J.; Katunga, L.A.; Nelson, M.A.M.; Brown, D.A.; Anderson, E.J. The "Goldilocks Zone" from a redox perspective-Adaptive vs. deleterious responses to oxidative stress in striated muscle. Front. Physiol. 2014, doi:10.3389/fphys.2014.00358.
    • (2014) Front. Physiol
    • Alleman, R.J.1    Katunga, L.A.2    Nelson, M.A.M.3    Brown, D.A.4    Anderson, E.J.5
  • 90
    • 84902322007 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species: A double edged sword in ischemia/reperfusion vs. preconditioning
    • Kalogeris, T.; Bao, Y.; Korthuis, R.J. Mitochondrial reactive oxygen species: A double edged sword in ischemia/reperfusion vs. preconditioning. Redox Biol. 2014, 2, 702-714.
    • (2014) Redox Biol , vol.2 , pp. 702-714
    • Kalogeris, T.1    Bao, Y.2    Korthuis, R.J.3
  • 91
    • 73949088946 scopus 로고    scopus 로고
    • Ros-mediated activation of NF-kappaB and Foxo during muscle disuse
    • Dodd, S.L.; Gagnon, B.J.; Senf, S.M.; Hain, B.A.; Judge, A.R. Ros-mediated activation of NF-kappaB and Foxo during muscle disuse. Muscle Nerve 2010, 41, 110-113.
    • (2010) Muscle Nerve , vol.41 , pp. 110-113
    • Dodd, S.L.1    Gagnon, B.J.2    Senf, S.M.3    Hain, B.A.4    Judge, A.R.5
  • 94
    • 78650894319 scopus 로고    scopus 로고
    • Crosstalk of reactive oxygen species and NF-κB signaling
    • Morgan, M.J.; Liu, Z.G. Crosstalk of reactive oxygen species and NF-κB signaling. Cell Res. 2011, 21, 103-115.
    • (2011) Cell Res , vol.21 , pp. 103-115
    • Morgan, M.J.1    Liu, Z.G.2
  • 95
    • 9244223545 scopus 로고    scopus 로고
    • Preconditioning of skeletal muscle against contraction-induced damage: The role of adaptations to oxidants in mice
    • McArdle, F.; Spiers, S.; Aldemir, H.; Vasilaki, A.; Beaver, A.; Iwanejko, L.; McArdle, A.; Jackson, M.J. Preconditioning of skeletal muscle against contraction-induced damage: The role of adaptations to oxidants in mice. J. Physiol. 2004, 561, 233-244.
    • (2004) J. Physiol , vol.561 , pp. 233-244
    • McArdle, F.1    Spiers, S.2    Aldemir, H.3    Vasilaki, A.4    Beaver, A.5    Iwanejko, L.6    McArdle, A.7    Jackson, M.J.8
  • 96
    • 0027504262 scopus 로고
    • Genotoxic properties of 4-hydroxyalkenals and analogous aldehydes
    • Eckl, P.M.; Ortner, A.; Esterbauer, H. Genotoxic properties of 4-hydroxyalkenals and analogous aldehydes. Mutat. Res. 1993, 290, 183-192.
    • (1993) Mutat. Res , vol.290 , pp. 183-192
    • Eckl, P.M.1    Ortner, A.2    Esterbauer, H.3
  • 97
    • 45249124663 scopus 로고    scopus 로고
    • 4-hydroxynonenal: A membrane lipid oxidation product of medicinal interest
    • Poli, G.; Schaur, R.J.; Siems, W.G.; Leonarduzzi, G. 4-hydroxynonenal: A membrane lipid oxidation product of medicinal interest. Med. Res. Rev. 2008, 28, 569-631.
    • (2008) Med. Res. Rev , vol.28 , pp. 569-631
    • Poli, G.1    Schaur, R.J.2    Siems, W.G.3    Leonarduzzi, G.4
  • 98
    • 1642396537 scopus 로고    scopus 로고
    • Role of Nrf2 in the regulation of CD36 and stress protein expression in murine macrophages: Activation by oxidatively modified LDL and 4-hydroxynonenal
    • Ishii, T.; Itoh, K.; Ruiz, E.; Leake, D.S.; Unoki, H.; Yamamoto, M.; Mann, G.E. Role of Nrf2 in the regulation of CD36 and stress protein expression in murine macrophages: Activation by oxidatively modified LDL and 4-hydroxynonenal. Circ. Res. 2004, 94, 609-616.
    • (2004) Circ. Res , vol.94 , pp. 609-616
    • Ishii, T.1    Itoh, K.2    Ruiz, E.3    Leake, D.S.4    Unoki, H.5    Yamamoto, M.6    Mann, G.E.7
  • 99
    • 1642282736 scopus 로고    scopus 로고
    • Cellular mechanisms of redox cell signalling: Role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products
    • Levonen, A.L.; Landar, A.; Ramachandra, A.; Cease, E.K.; Dickinson, D.A.; Zanoni, G.; Morrow, J.D.; Darley-Usmar, V.M. Cellular mechanisms of redox cell signalling: Role of cysteine modification in controlling antioxidant defences in response to electrophilic lipid oxidation products. Biochem. J. 2004, 378, 373-382.
    • (2004) Biochem. J , vol.378 , pp. 373-382
    • Levonen, A.L.1    Landar, A.2    Ramachandra, A.3    Cease, E.K.4    Dickinson, D.A.5    Zanoni, G.6    Morrow, J.D.7    Darley-Usmar, V.M.8
  • 101
    • 23844540597 scopus 로고    scopus 로고
    • Decreasing xanthine oxidase-mediated oxidative stress prevents useful cellular adaptations to exercise in rats
    • Gomez-Cabrera, M.C.; Borrás, C.; Pallardó, F.V.; Sastre, J.; Ji, L.L.; Viña, J. Decreasing xanthine oxidase-mediated oxidative stress prevents useful cellular adaptations to exercise in rats. J. Physiol. 2005, 567, 113-120.
    • (2005) J. Physiol , vol.567 , pp. 113-120
    • Gomez-Cabrera, M.C.1    Borrás, C.2    Pallardó, F.V.3    Sastre, J.4    Ji, L.L.5    Viña, J.6
  • 102
    • 37849021505 scopus 로고    scopus 로고
    • Moderate exercise is an antioxidant: Upregulation of antioxidant genes by training
    • Gomez-Cabrera, M.C.; Domenech, E.; Viña, J. Moderate exercise is an antioxidant: Upregulation of antioxidant genes by training. Free Radic. Biol. Med. 2008, 44, 126-131.
    • (2008) Free Radic. Biol. Med , vol.44 , pp. 126-131
    • Gomez-Cabrera, M.C.1    Domenech, E.2    Viña, J.3
  • 103
    • 5044227528 scopus 로고    scopus 로고
    • Acute exercise activates nuclear factor (NF)-kappaB signaling pathway in rat skeletal muscle
    • Ji, L.L.; Gomez-Cabrera, M.C.; Steinhafel, N.; Viña, J. Acute exercise activates nuclear factor (NF)-kappaB signaling pathway in rat skeletal muscle. FASEB J. 2004, 18, 1499-1506.
    • (2004) FASEB J , vol.18 , pp. 1499-1506
    • Ji, L.L.1    Gomez-Cabrera, M.C.2    Steinhafel, N.3    Viña, J.4
  • 105
    • 0012971383 scopus 로고    scopus 로고
    • Overloaded training increases exercise-induced oxidative stress and damage
    • Palazzetti, S.; Richard, M.J.; Favier, A.; Margaritis, I. Overloaded training increases exercise-induced oxidative stress and damage. Can. J. Appl. Physiol. 2003, 28, 588-604.
    • (2003) Can. J. Appl. Physiol , vol.28 , pp. 588-604
    • Palazzetti, S.1    Richard, M.J.2    Favier, A.3    Margaritis, I.4
  • 106
    • 77949391048 scopus 로고    scopus 로고
    • Altered oxidative stress in overtrained athletes
    • Tanskanen, M.; Atalay, M.; Uusitalo, A. Altered oxidative stress in overtrained athletes. J. Sports Sci. 2010, 28, 309-317.
    • (2010) J. Sports Sci , vol.28 , pp. 309-317
    • Tanskanen, M.1    Atalay, M.2    Uusitalo, A.3
  • 107
    • 0038587678 scopus 로고    scopus 로고
    • PPARγ coactivator-1α expression during thyroid hormone-and contractile activity-induced mitochondrial adaptations
    • Irrcher, I.; Adhihetty, P.J.; Sheehan, T.; Joseph, A.M.; Hood, D.A. PPARγ coactivator-1α expression during thyroid hormone-and contractile activity-induced mitochondrial adaptations. Am. J. Physiol. Cell Physiol. 2003, 284, C1669-C1677.
    • (2003) Am. J. Physiol. Cell Physiol , vol.284 , pp. C1669-C1677
    • Irrcher, I.1    Adhihetty, P.J.2    Sheehan, T.3    Joseph, A.M.4    Hood, D.A.5
  • 108
    • 63649121321 scopus 로고    scopus 로고
    • Regulation by exercise of skeletal muscle content of mitochondria and GLUT4
    • Holloszy, J.O. Regulation by exercise of skeletal muscle content of mitochondria and GLUT4. J. Physiol. Pharmacol. 2008, 59, 5-18.
    • (2008) J. Physiol. Pharmacol , vol.59 , pp. 5-18
    • Holloszy, J.O.1
  • 109
    • 79251479441 scopus 로고    scopus 로고
    • Regulation of exercise-induced fiber type transformation, mitochondrial biogenesis, and angiogenesis in skeletal muscle
    • Yan, Z.; Okutsu, M.; Akhtar, Y.N.; Lira, V.A. Regulation of exercise-induced fiber type transformation, mitochondrial biogenesis, and angiogenesis in skeletal muscle. J. Appl. Physiol. 2011, 110, 264-274.
    • (2011) J. Appl. Physiol , vol.110 , pp. 264-274
    • Yan, Z.1    Okutsu, M.2    Akhtar, Y.N.3    Lira, V.A.4
  • 110
    • 29944445284 scopus 로고    scopus 로고
    • Increased intramuscular lipid storage in the insulin-resistant and endurance-trained state
    • Van Loon, L.J.C.; Goodpaster, B.H. Increased intramuscular lipid storage in the insulin-resistant and endurance-trained state. Pflugers Arch. 2006, 451, 606-616.
    • (2006) Pflugers Arch , vol.451 , pp. 606-616
    • Van Loon, L.J.C.1    Goodpaster, B.H.2
  • 111
    • 37249066135 scopus 로고    scopus 로고
    • Exercise training-induced improvements in insulin action
    • Hawley, J.A.; Lessard, S.J. Exercise training-induced improvements in insulin action. Acta Physiol. 2008, 192, 127-135.
    • (2008) Acta Physiol , vol.192 , pp. 127-135
    • Hawley, J.A.1    Lessard, S.J.2
  • 112
    • 77952892253 scopus 로고    scopus 로고
    • PGC-1α-mediated adaptations in skeletal muscle
    • Olesen, J.; Kiilerich, K.; Pilegaard, H. PGC-1α-mediated adaptations in skeletal muscle. Pflugers Arch. 2010, 460, 153-162.
    • (2010) Pflugers Arch , vol.460 , pp. 153-162
    • Olesen, J.1    Kiilerich, K.2    Pilegaard, H.3
  • 113
    • 84897924122 scopus 로고    scopus 로고
    • Role of PGC-1α in muscle function and aging
    • Kang, C.; Ji, L.L. Role of PGC-1α in muscle function and aging. J. Sport Health Sci. 2013, 2, 81-86.
    • (2013) J. Sport Health Sci , vol.2 , pp. 81-86
    • Kang, C.1    Ji, L.L.2
  • 114
    • 22744446447 scopus 로고    scopus 로고
    • Substrate availability and transcriptional regulation of metabolic genes in human skeletal muscle during recovery from exercise
    • Pilegaard, H.; Osada, T.; Andersen, L.T.; Helge, J.W.; Saltin, B.; Neufer, P.D. Substrate availability and transcriptional regulation of metabolic genes in human skeletal muscle during recovery from exercise. Metabolism 2005, 54, 1048-1055.
    • (2005) Metabolism , vol.54 , pp. 1048-1055
    • Pilegaard, H.1    Osada, T.2    Andersen, L.T.3    Helge, J.W.4    Saltin, B.5    Neufer, P.D.6
  • 116
    • 55449106960 scopus 로고    scopus 로고
    • Rapid exercise-induced changes in PGC-1α mRNA and protein in human skeletal muscle
    • Mathai, A.S.; Bonen, A.; Benton, C.R.; Robinson, D.L.; Graham, T.E. Rapid exercise-induced changes in PGC-1α mRNA and protein in human skeletal muscle. J. Appl. Physiol. 2008, 105, 1098-1105.
    • (2008) J. Appl. Physiol , vol.105 , pp. 1098-1105
    • Mathai, A.S.1    Bonen, A.2    Benton, C.R.3    Robinson, D.L.4    Graham, T.E.5
  • 117
    • 79958851262 scopus 로고    scopus 로고
    • An acute bout of high-intensity interval training increases the nuclear abundance of PGC-1α and activates mitochondrial biogenesis in human skeletal muscle
    • Little, J.P.; Safdar, A.; Bishop, D.; Tarnopolsky, M.A.; Gibala, M.J. An acute bout of high-intensity interval training increases the nuclear abundance of PGC-1α and activates mitochondrial biogenesis in human skeletal muscle. Am. J. Physiol. Regul. Integr. Comp. Physiol. 2011, 300, R1303-R1310.
    • (2011) Am. J. Physiol. Regul. Integr. Comp. Physiol , vol.300 , pp. R1303-R1310
    • Little, J.P.1    Safdar, A.2    Bishop, D.3    Tarnopolsky, M.A.4    Gibala, M.J.5
  • 119
    • 33846992686 scopus 로고    scopus 로고
    • Exercise-induced mitochondrial biogenesis begins before the increase in muscle PGC-1α expression
    • Wright, D.C.; Han, D.H.; Garcia-Roves, P.M.; Geiger, P.C.; Jones, T.E.; Holloszy, J. Exercise-induced mitochondrial biogenesis begins before the increase in muscle PGC-1α expression. J. Biol. Chem. 2007, 282, 194-199.
    • (2007) J. Biol. Chem , vol.282 , pp. 194-199
    • Wright, D.C.1    Han, D.H.2    Garcia-Roves, P.M.3    Geiger, P.C.4    Jones, T.E.5    Holloszy, J.6
  • 121
    • 25844432311 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-γ co-activator 1α-mediated metabolic remodeling of skeletal myocytes mimics exercise training and reverses lipid-induced mitochondrial inefficiency
    • Koves, T.R.; Li, P.; An, J.; Akimoto, T.; Slentz, D.; Ilkayeva, O.; Dohm, G.L.; Yan, Z.; Newgard, C.B.; Muoio, D.M. Peroxisome proliferator-activated receptor-γ co-activator 1α-mediated metabolic remodeling of skeletal myocytes mimics exercise training and reverses lipid-induced mitochondrial inefficiency. J. Biol. Chem. 2005, 280, 33588-33598.
    • (2005) J. Biol. Chem , vol.280 , pp. 33588-33598
    • Koves, T.R.1    Li, P.2    An, J.3    Akimoto, T.4    Slentz, D.5    Ilkayeva, O.6    Dohm, G.L.7    Yan, Z.8    Newgard, C.B.9    Muoio, D.M.10
  • 123
    • 35648937073 scopus 로고    scopus 로고
    • Skeletal muscle fiber-type switching, exercise intolerance, and myopathy in PGC-1α muscle-specific knock-out animals
    • Handschin, C.; Chin, S.; Li, P.; Liu, F.; Maratos-Flier, E.; Lebrasseur, N.K.; Yan, Z.; Spiegelman, B.M. Skeletal muscle fiber-type switching, exercise intolerance, and myopathy in PGC-1α muscle-specific knock-out animals. J. Biol. Chem. 2007, 282, 30014-30021.
    • (2007) J. Biol. Chem , vol.282 , pp. 30014-30021
    • Handschin, C.1    Chin, S.2    Li, P.3    Liu, F.4    Maratos-Flier, E.5    Lebrasseur, N.K.6    Yan, Z.7    Spiegelman, B.M.8
  • 124
    • 0037326196 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-γ coactivator 1α (PGC-1α): Transcriptional coactivator and metabolic regulator
    • Puigserver, P.; Spiegelman, B.M. Peroxisome proliferator-activated receptor-γ coactivator 1α (PGC-1α): Transcriptional coactivator and metabolic regulator. Endocr. Rev. 2003, 24, 78-90.
    • (2003) Endocr. Rev , vol.24 , pp. 78-90
    • Puigserver, P.1    Spiegelman, B.M.2
  • 125
    • 84865414333 scopus 로고    scopus 로고
    • Transcriptional integration of mitochondrial biogenesis
    • Scarpulla, R.C.; Vega, R.B.; Kelly, D.P. Transcriptional integration of mitochondrial biogenesis. Trends Endocrinol. Metab. 2012, 23, 459-466.
    • (2012) Trends Endocrinol. Metab , vol.23 , pp. 459-466
    • Scarpulla, R.C.1    Vega, R.B.2    Kelly, D.P.3
  • 126
    • 0037394603 scopus 로고    scopus 로고
    • Potentiation of liver X receptor transcriptional activity by peroxisome-proliferator-activated receptor γ co-activator 1α
    • Oberkofler, H.; Schraml, E.; Krempler, F.; Patsch, W. Potentiation of liver X receptor transcriptional activity by peroxisome-proliferator-activated receptor γ co-activator 1α. Biochem. J. 2003, 371, 89-96.
    • (2003) Biochem. J , vol.371 , pp. 89-96
    • Oberkofler, H.1    Schraml, E.2    Krempler, F.3    Patsch, W.4
  • 127
    • 77958453583 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor γ coactivator 1α (PGC-1α) promotes skeletal muscle lipid refueling in vivo by activating de novo lipogenesis and the pentose phosphate pathway
    • Summermatter, S.; Baum, O.; Santos, G.; Hoppeler, H.; Handschin, C. Peroxisome proliferator-activated receptor γ coactivator 1α (PGC-1α) promotes skeletal muscle lipid refueling in vivo by activating de novo lipogenesis and the pentose phosphate pathway. J. Biol. Chem. 2010, 285, 32793-32800.
    • (2010) J. Biol. Chem , vol.285 , pp. 32793-32800
    • Summermatter, S.1    Baum, O.2    Santos, G.3    Hoppeler, H.4    Handschin, C.5
  • 133
    • 0038810035 scopus 로고    scopus 로고
    • An autoregulatory loop controls peroxisome proliferator-activated receptor γ coactivator 1α expression in muscle
    • Handschin, C.; Rhee, J.; Lin, J.; Tarr, P.T.; Spiegelman, B.M. An autoregulatory loop controls peroxisome proliferator-activated receptor γ coactivator 1α expression in muscle. Proc. Natl. Acad. Sci. USA 2003, 100, 7111-7116.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7111-7116
    • Handschin, C.1    Rhee, J.2    Lin, J.3    Tarr, P.T.4    Spiegelman, B.M.5
  • 134
    • 70350020773 scopus 로고    scopus 로고
    • Exercise activation of muscle peroxisome proliferator-activated receptor-gamma coactivator-1α signaling is redox sensitive
    • Kang, C.; O'Moore, K.M.; Dickman, J.R.; Ji, L.L. Exercise activation of muscle peroxisome proliferator-activated receptor-gamma coactivator-1α signaling is redox sensitive. Free Radic. Biol. Med. 2009, 47, 1394-1400.
    • (2009) Free Radic. Biol. Med , vol.47 , pp. 1394-1400
    • Kang, C.1    O'Moore, K.M.2    Dickman, J.R.3    Ji, L.L.4
  • 137
    • 77955347446 scopus 로고    scopus 로고
    • Sirtuin 3, a new target of PGC-1α, plays an important role in the suppression of ROS and mitochondrial biogenesis
    • Kong, X.; Wang, R.; Xue, Y.; Liu, X.; Zhang, H.; Chen, Y.; Fang, F.; Chang, Y. Sirtuin 3, a new target of PGC-1α, plays an important role in the suppression of ROS and mitochondrial biogenesis. PLoS ONE 2010, 5, e11707.
    • (2010) PLoS ONE , vol.5
    • Kong, X.1    Wang, R.2    Xue, Y.3    Liu, X.4    Zhang, H.5    Chen, Y.6    Fang, F.7    Chang, Y.8
  • 140
    • 78649521247 scopus 로고    scopus 로고
    • Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation
    • Qiu, X.; Brown, K.; Hirschey, M.D.; Verdin, E.; Chen, D. Calorie restriction reduces oxidative stress by SIRT3-mediated SOD2 activation. Cell Metab. 2010, 12, 662-667.
    • (2010) Cell Metab , vol.12 , pp. 662-667
    • Qiu, X.1    Brown, K.2    Hirschey, M.D.3    Verdin, E.4    Chen, D.5
  • 142
    • 79957979314 scopus 로고    scopus 로고
    • Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS
    • Chen, Y.; Zhang, J.; Lin, Y.; Lei, Q.; Guan, K.L.; Zhao, S.; Xiong, Y. Tumour suppressor SIRT3 deacetylates and activates manganese superoxide dismutase to scavenge ROS. EMBO Rep. 2011, 12, 534-541.
    • (2011) EMBO Rep , vol.12 , pp. 534-541
    • Chen, Y.1    Zhang, J.2    Lin, Y.3    Lei, Q.4    Guan, K.L.5    Zhao, S.6    Xiong, Y.7
  • 143
    • 73949099327 scopus 로고    scopus 로고
    • Increased muscle PGC-1α expression protects from sarcopenia and metabolic disease during aging
    • Wenz, T.; Rossi, S.G.; Rotundo, R.L.; Spiegelman, B.M.; Moraes, C.T. Increased muscle PGC-1α expression protects from sarcopenia and metabolic disease during aging. Proc. Natl. Acad. Sci. USA 2009, 106, 20405-20410.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 20405-20410
    • Wenz, T.1    Rossi, S.G.2    Rotundo, R.L.3    Spiegelman, B.M.4    Moraes, C.T.5
  • 144
    • 0038036024 scopus 로고    scopus 로고
    • Bioenergetic analysis of peroxisome proliferator-activated receptor γ coactivators 1α and 1β (PGC-1α and PGC-1β) in muscle cells
    • St-Pierre, J.; Lin, J.; Krauss, S.; Tarr, P.T.; Yang, R.; Newgard, C.B.; Spiegelman, B.M. Bioenergetic analysis of peroxisome proliferator-activated receptor γ coactivators 1α and 1β (PGC-1α and PGC-1β) in muscle cells. J. Biol. Chem. 2003, 278, 26597-26603.
    • (2003) J. Biol. Chem , vol.278 , pp. 26597-26603
    • St-Pierre, J.1    Lin, J.2    Krauss, S.3    Tarr, P.T.4    Yang, R.5    Newgard, C.B.6    Spiegelman, B.M.7


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