메뉴 건너뛰기




Volumn 95, Issue 1, 2010, Pages 1-9

Reactive oxygen species are signalling molecules for skeletal muscle adaptation

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE 3; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PHOSPHATASE; PROTEASOME; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR; UBIQUITIN;

EID: 74049129489     PISSN: 09580670     EISSN: 1469445X     Source Type: Journal    
DOI: 10.1113/expphysiol.2009.050526     Document Type: Review
Times cited : (329)

References (68)
  • 1
    • 0033963704 scopus 로고    scopus 로고
    • Oxidative stress and gene regulation
    • Allen RG Tresini M (2000). Oxidative stress and gene regulation. Free Radic Biol Med 28, 463 499.
    • (2000) Free Radic Biol Med , vol.28 , pp. 463-499
    • Allen, R.G.1    Tresini, M.2
  • 3
    • 0030927378 scopus 로고    scopus 로고
    • Supplementation of vitamin e may attenuate skeletal muscle immobilization atrophy
    • Appell HJ, Duarte JA Soares JM (1997). Supplementation of vitamin E may attenuate skeletal muscle immobilization atrophy. Int J Sports Med 18, 157 160.
    • (1997) Int J Sports Med , vol.18 , pp. 157-160
    • Appell, H.J.1    Duarte, J.A.2    Soares, J.M.3
  • 4
    • 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 (1999). 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 31, 347 366.
    • (1999) J Bioenerg Biomembr , vol.31 , pp. 347-366
    • Barja, G.1
  • 5
    • 33746328957 scopus 로고    scopus 로고
    • Signaling pathways in skeletal muscle remodeling
    • Bassel-Duby R Olson EN (2006). Signaling pathways in skeletal muscle remodeling. Annu Rev Biochem 75, 19 37.
    • (2006) Annu Rev Biochem , vol.75 , pp. 19-37
    • Bassel-Duby, R.1    Olson, E.N.2
  • 8
    • 0033970533 scopus 로고    scopus 로고
    • Dual specificity phosphatases: A gene family for control of MAP kinase function
    • Camps M, Nichols A Arkinstall S (2000). Dual specificity phosphatases: a gene family for control of MAP kinase function. FASEB J 14, 6 16.
    • (2000) FASEB J , vol.14 , pp. 6-16
    • Camps, M.1    Nichols, A.2    Arkinstall, S.3
  • 9
    • 40549097447 scopus 로고    scopus 로고
    • Methionine oxidation in the calmodulin-binding domain of calcineurin disrupts calmodulin binding and calcineurin activation
    • Carruthers NJ Stemmer PM (2008). Methionine oxidation in the calmodulin-binding domain of calcineurin disrupts calmodulin binding and calcineurin activation. Biochemistry 47, 3085 3095.
    • (2008) Biochemistry , vol.47 , pp. 3085-3095
    • Carruthers, N.J.1    Stemmer, P.M.2
  • 11
    • 0642276003 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatases during receptor tyrosine kinase signal transduction
    • Chiarugi P Cirri P (2003). Redox regulation of protein tyrosine phosphatases during receptor tyrosine kinase signal transduction. Trends Biochem Sci 28, 509 514.
    • (2003) Trends Biochem Sci , vol.28 , pp. 509-514
    • Chiarugi, P.1    Cirri, P.2
  • 12
    • 28944450314 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase (MAPK)
    • Cuschieri J Maier RV (2005). Mitogen-activated protein kinase (MAPK). Crit Care Med 33, S417 S419.
    • (2005) Crit Care Med , vol.33
    • Cuschieri, J.1    Maier, R.V.2
  • 14
    • 85047693596 scopus 로고    scopus 로고
    • Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions
    • Du J, Wang X, Miereles C, Bailey JL, Debigare R, Zheng B, Price SR Mitch WE (2004). Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions. J Clin Invest 113, 115 123.
    • (2004) J Clin Invest , vol.113 , pp. 115-123
    • Du, J.1    Wang, X.2    Miereles, C.3    Bailey, J.L.4    Debigare, R.5    Zheng, B.6    Price, S.R.7    Mitch, W.E.8
  • 15
    • 0033618462 scopus 로고    scopus 로고
    • Calcineurin is required for skeletal muscle hypertrophy
    • Dunn SE, Burns JL Michel RN (1999). Calcineurin is required for skeletal muscle hypertrophy. J Biol Chem 274, 21908 21912.
    • (1999) J Biol Chem , vol.274 , pp. 21908-21912
    • Dunn, S.E.1    Burns, J.L.2    Michel, R.N.3
  • 16
    • 0033231361 scopus 로고    scopus 로고
    • Regulation of antioxidant enzyme gene expression in response to oxidative stress and during differentiation of mouse skeletal muscle
    • Franco AA, Odom RS Rando TA (1999). Regulation of antioxidant enzyme gene expression in response to oxidative stress and during differentiation of mouse skeletal muscle. Free Radic Biol Med 27, 1122 1132.
    • (1999) Free Radic Biol Med , vol.27 , pp. 1122-1132
    • Franco, A.A.1    Odom, R.S.2    Rando, T.A.3
  • 19
    • 23844540597 scopus 로고    scopus 로고
    • Decreasing xanthine oxidase-mediated oxidative stress prevents useful cellular adaptations to exercise in rats
    • Gomez-Cabrera MC, Borrás C, Pallardó FV, Sastre J, Ji LL Viña J (2005). Decreasing xanthine oxidase-mediated oxidative stress prevents useful cellular adaptations to exercise in rats. J Physiol 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
  • 20
    • 38149131289 scopus 로고    scopus 로고
    • Oral administration of vitamin C decreases muscle mitochondrial biogenesis and hampers training-induced adaptations in endurance performance
    • Gomez-Cabrera MC, Domenech E, Romagnoli M, Arduini A, Borras C, Pallardo FV, Sastre J Viña J (2008). Oral administration of vitamin C decreases muscle mitochondrial biogenesis and hampers training-induced adaptations in endurance performance. Am J Clin Nutr 87, 142 149.
    • (2008) Am J Clin Nutr , vol.87 , pp. 142-149
    • Gomez-Cabrera, M.C.1    Domenech, E.2    Romagnoli, M.3    Arduini, A.4    Borras, C.5    Pallardo, F.V.6    Sastre, J.7    Viña, J.8
  • 22
    • 0038239701 scopus 로고    scopus 로고
    • Selective degradation of oxidatively modified protein substrates by the proteasome
    • Grune T, Merker K, Sandig G Davies KJ (2003). Selective degradation of oxidatively modified protein substrates by the proteasome. Biochem Biophys Res Commun 305, 709 718.
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 709-718
    • Grune, T.1    Merker, K.2    Sandig, G.3    Davies, K.J.4
  • 25
    • 34247473444 scopus 로고    scopus 로고
    • A reducing redox environment promotes C2C12 myogenesis: Implications for regeneration in aged muscle
    • Hansen JM, Klass M, Harris C Csete M (2007). A reducing redox environment promotes C2C12 myogenesis: implications for regeneration in aged muscle. Cell Biol Int 31, 546 553.
    • (2007) Cell Biol Int , vol.31 , pp. 546-553
    • Hansen, J.M.1    Klass, M.2    Harris, C.3    Csete, M.4
  • 26
    • 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 (2006). A transverse tubule NADPH oxidase activity stimulates calcium release from isolated triads via ryanodine receptor type 1 S-glutathionylation. J Biol Chem 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
  • 27
    • 58349118928 scopus 로고    scopus 로고
    • Interactions between ROS and AMP kinase activity in the regulation of PGc-1α transcription in skeletal muscle cells
    • Irrcher I, Ljubicic V Hood DA (2009). Interactions between ROS and AMP kinase activity in the regulation of PGc-1α transcription in skeletal muscle cells. Am J Physiol Cell Physiol 296, C116 C123.
    • (2009) Am J Physiol Cell Physiol , vol.296
    • Irrcher, I.1    Ljubicic, V.2    Hood, D.A.3
  • 30
    • 33744468523 scopus 로고    scopus 로고
    • Exercise and hormesis: Activation of cellular antioxidant signaling pathway
    • Ji LL, Gomez-Cabrera MC Vina J (2006). Exercise and hormesis: activation of cellular antioxidant signaling pathway. Ann NY Acad Sci 1067, 425 435.
    • (2006) Ann NY Acad Sci , vol.1067 , pp. 425-435
    • Ji, L.L.1    Gomez-Cabrera, M.C.2    Vina, J.3
  • 31
    • 33744962865 scopus 로고    scopus 로고
    • Redefining oxidative stress
    • Jones DP (2006). Redefining oxidative stress. Antioxid Redox Signal 8, 1865 1879.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 1865-1879
    • Jones, D.P.1
  • 32
    • 14044277556 scopus 로고    scopus 로고
    • Redox regulation of NF-κB activation: Distinct redox regulation between the cytoplasm and the nucleus
    • Kabe Y, Ando K, Hirao S, Yoshida M Handa H (2005). Redox regulation of NF-κB activation: distinct redox regulation between the cytoplasm and the nucleus. Antioxid Redox Signal 7, 395 403.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 395-403
    • Kabe, Y.1    Ando, K.2    Hirao, S.3    Yoshida, M.4    Handa, H.5
  • 33
    • 32144457727 scopus 로고    scopus 로고
    • Intracellular signaling during skeletal muscle atrophy
    • Kandarian SC Jackman RW (2006). Intracellular signaling during skeletal muscle atrophy. Muscle Nerve 33, 155 165.
    • (2006) Muscle Nerve , vol.33 , pp. 155-165
    • Kandarian, S.C.1    Jackman, R.W.2
  • 34
    • 0035990341 scopus 로고    scopus 로고
    • Molecular events in skeletal muscle during disuse atrophy
    • Kandarian SC Stevenson EJ (2002). Molecular events in skeletal muscle during disuse atrophy. Exerc Sport Sci Rev 30, 111 116.
    • (2002) Exerc Sport Sci Rev , vol.30 , pp. 111-116
    • Kandarian, S.C.1    Stevenson, E.J.2
  • 36
    • 0025733767 scopus 로고
    • Oxidative stress in skeletal muscle atrophied by immobilization
    • Kondo H, Miura M Itokawa Y (1991). Oxidative stress in skeletal muscle atrophied by immobilization. Acta Physiol Scand 142, 527 528.
    • (1991) Acta Physiol Scand , vol.142 , pp. 527-528
    • Kondo, H.1    Miura, M.2    Itokawa, Y.3
  • 37
    • 34447632877 scopus 로고    scopus 로고
    • Exercise, MAPK, and NF-κB signaling in skeletal muscle
    • Kramer HF Goodyear LJ (2007). Exercise, MAPK, and NF-κB signaling in skeletal muscle. J Appl Physiol 103, 388 395.
    • (2007) J Appl Physiol , vol.103 , pp. 388-395
    • Kramer, H.F.1    Goodyear, L.J.2
  • 39
    • 14644400387 scopus 로고    scopus 로고
    • TNF-α acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle
    • Li YP, Chen Y, John J, Moylan J, Jin B, Mann DL Reid MB (2005). TNF-α acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle. FASEB J 19, 362 370.
    • (2005) FASEB J , vol.19 , pp. 362-370
    • Li, Y.P.1    Chen, Y.2    John, J.3    Moylan, J.4    Jin, B.5    Mann, D.L.6    Reid, M.B.7
  • 40
    • 0141791457 scopus 로고    scopus 로고
    • Hydrogen peroxide stimulates ubiquitin-conjugating activity and expression of genes for specific E2 and E3 proteins in skeletal muscle myotubes
    • Li YP, Chen Y, Li AS Reid MB (2003). Hydrogen peroxide stimulates ubiquitin-conjugating activity and expression of genes for specific E2 and E3 proteins in skeletal muscle myotubes. Am J Physiol Cell Physiol 285, C806 C812.
    • (2003) Am J Physiol Cell Physiol , vol.285
    • Li, Y.P.1    Chen, Y.2    Li, A.S.3    Reid, M.B.4
  • 41
    • 0032785355 scopus 로고    scopus 로고
    • Cellular expression of xanthine oxidoreductase protein in normal human tissues
    • Linder N, Rapola J Raivio KO (1999). Cellular expression of xanthine oxidoreductase protein in normal human tissues. Lab Invest 79, 967 974.
    • (1999) Lab Invest , vol.79 , pp. 967-974
    • Linder, N.1    Rapola, J.2    Raivio, K.O.3
  • 42
    • 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 MJ (2004). Preconditioning of skeletal muscle against contraction-induced damage: the role of adaptations to oxidants in mice. J Physiol 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
  • 45
    • 36248950730 scopus 로고    scopus 로고
    • Antioxidant administration attenuates mechanical ventilation-induced rat diaphragm muscle atrophy independent of protein kinase B (PKB Akt) signalling
    • McClung JM, Kavazis AN, Whidden MA, DeRuisseau KC, Falk DJ, Criswell DS Powers SK (2007b). Antioxidant administration attenuates mechanical ventilation-induced rat diaphragm muscle atrophy independent of protein kinase B (PKB Akt) signalling. J Physiol 585, 203 215.
    • (2007) J Physiol , vol.585 , pp. 203-215
    • McClung, J.M.1    Kavazis, A.N.2    Whidden, M.A.3    Deruisseau, K.C.4    Falk, D.J.5    Criswell, D.S.6    Powers, S.K.7
  • 46
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
    • Maehama T Dixon JE (1998). The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J Biol Chem 273, 13375 13378.
    • (1998) J Biol Chem , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 48
    • 14044265068 scopus 로고    scopus 로고
    • Stress-responsive protein kinases in redox-regulated apoptosis signaling
    • Matsuzawa A Ichijo H (2005). Stress-responsive protein kinases in redox-regulated apoptosis signaling. Antioxid Redox Signal 7, 472 481.
    • (2005) Antioxid Redox Signal , vol.7 , pp. 472-481
    • Matsuzawa, A.1    Ichijo, H.2
  • 49
    • 34248563290 scopus 로고    scopus 로고
    • The ERK1/2 mitogen-activated protein kinase pathway as a master regulator of the G1- to S-phase transition
    • Meloche S Pouyssegur J (2007). The ERK1/2 mitogen-activated protein kinase pathway as a master regulator of the G1- to S-phase transition. Oncogene 26, 3227 3239.
    • (2007) Oncogene , vol.26 , pp. 3227-3239
    • Meloche, S.1    Pouyssegur, J.2
  • 50
    • 2942754279 scopus 로고    scopus 로고
    • Calcineurin and skeletal muscle growth
    • Michel RN, Dunn SE Chin ER (2004). Calcineurin and skeletal muscle growth. Proc Nutr Soc 63, 341 349.
    • (2004) Proc Nutr Soc , vol.63 , pp. 341-349
    • Michel, R.N.1    Dunn, S.E.2    Chin, E.R.3
  • 51
    • 34047213532 scopus 로고    scopus 로고
    • Oxidative stress, chronic disease, and muscle wasting
    • Moylan JS Reid MB (2007). Oxidative stress, chronic disease, and muscle wasting. Muscle Nerve 35, 411 429.
    • (2007) Muscle Nerve , vol.35 , pp. 411-429
    • Moylan, J.S.1    Reid, M.B.2
  • 53
    • 55949118714 scopus 로고    scopus 로고
    • Exercise-induced oxidative stress: Cellular mechanisms and impact on muscle force production
    • Powers SK Jackson MJ (2008). Exercise-induced oxidative stress: cellular mechanisms and impact on muscle force production. Physiol Rev 88, 1243 1276.
    • (2008) Physiol Rev , vol.88 , pp. 1243-1276
    • Powers, S.K.1    Jackson, M.J.2
  • 57
    • 24944553549 scopus 로고    scopus 로고
    • MAP kinase pathways
    • Qi M Elion EA (2005). MAP kinase pathways. J Cell Sci 118, 3569 3572.
    • (2005) J Cell Sci , vol.118 , pp. 3569-3572
    • Qi, M.1    Elion, E.A.2
  • 59
    • 0029671057 scopus 로고    scopus 로고
    • Inhibition of NF-κB activation in human T-cell lines by anetholdithiolthione
    • Sen CK, Traber KE Packer L (1996). Inhibition of NF-κB activation in human T-cell lines by anetholdithiolthione. Biochem Biophys Res Commun 218, 148 153.
    • (1996) Biochem Biophys Res Commun , vol.218 , pp. 148-153
    • Sen, C.K.1    Traber, K.E.2    Packer, L.3
  • 60
    • 33644862368 scopus 로고    scopus 로고
    • JNK signaling pathway is a key modulator in cell death mediated by reactive oxygen and nitrogen species
    • Shen HM Liu ZG (2006). JNK signaling pathway is a key modulator in cell death mediated by reactive oxygen and nitrogen species. Free Radic Biol Med 40, 928 939.
    • (2006) Free Radic Biol Med , vol.40 , pp. 928-939
    • Shen, H.M.1    Liu, Z.G.2
  • 61
    • 0042232778 scopus 로고    scopus 로고
    • High sensitivity of plasma membrane ion transport ATPases from human neutrophils towards 4-hydroxy-2,3-trans-nonenal
    • Siems W, Capuozzo E, Lucano A, Salerno C Crifo C (2003). High sensitivity of plasma membrane ion transport ATPases from human neutrophils towards 4-hydroxy-2,3-trans-nonenal. Life Sci 73, 2583 2590.
    • (2003) Life Sci , vol.73 , pp. 2583-2590
    • Siems, W.1    Capuozzo, E.2    Lucano, A.3    Salerno, C.4    Crifo, C.5
  • 62
    • 33748313028 scopus 로고    scopus 로고
    • The contraction induced increase in gene expression of peroxisome proliferator-activated receptor (PPAR)-γ coactivator 1α (PGc-1α), mitochondrial uncoupling protein 3 (UCP3) and hexokinase II (HKII) in primary rat skeletal muscle cells is dependent on reactive oxygen species
    • Silveira LR, Pilegaard H, Kusuhara K, Curi R Hellsten Y (2006). The contraction induced increase in gene expression of peroxisome proliferator-activated receptor (PPAR)-γ coactivator 1α (PGc-1α), mitochondrial uncoupling protein 3 (UCP3) and hexokinase II (HKII) in primary rat skeletal muscle cells is dependent on reactive oxygen species. Biochim Biophys Acta 1763, 969 976.
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 969-976
    • Silveira, L.R.1    Pilegaard, H.2    Kusuhara, K.3    Curi, R.4    Hellsten, Y.5
  • 63
    • 20444400257 scopus 로고    scopus 로고
    • Redox redux: Revisiting PTPs and the control of cell signaling
    • Tonks NK (2005). Redox redux: revisiting PTPs and the control of cell signaling. Cell 121, 667 670.
    • (2005) Cell , vol.121 , pp. 667-670
    • Tonks, N.K.1
  • 64
    • 0142043984 scopus 로고    scopus 로고
    • Redox signaling and the MAP kinase pathways
    • Torres M Forman HJ (2003). Redox signaling and the MAP kinase pathways. Biofactors 17, 287 296.
    • (2003) Biofactors , vol.17 , pp. 287-296
    • Torres, M.1    Forman, H.J.2
  • 66
    • 34147210988 scopus 로고    scopus 로고
    • Hydrogen peroxide sensing and signaling
    • Veal EA, Day AM Morgan BA (2007). Hydrogen peroxide sensing and signaling. Mol Cell 26, 1 14.
    • (2007) Mol Cell , vol.26 , pp. 1-14
    • Veal, E.A.1    Day, A.M.2    Morgan, B.A.3
  • 68
    • 61949421164 scopus 로고    scopus 로고
    • Xanthine oxidase contributes to mechanical ventilation-induced diaphragmatic oxidative stress and contractile dysfunction
    • Whidden MA, McClung JM, Falk DJ, Hudson MB, Smuder AJ, Nelson WB Powers SK (2009). Xanthine oxidase contributes to mechanical ventilation-induced diaphragmatic oxidative stress and contractile dysfunction. J Appl Physiol 106, 385 394.
    • (2009) J Appl Physiol , vol.106 , pp. 385-394
    • Whidden, M.A.1    McClung, J.M.2    Falk, D.J.3    Hudson, M.B.4    Smuder, A.J.5    Nelson, W.B.6    Powers, S.K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.