메뉴 건너뛰기




Volumn 62, Issue , 2015, Pages 72-79

Differential thiol oxidation of the signaling proteins Akt, PTEN or PP2A determines whether Akt phosphorylation is enhanced or inhibited by oxidative stress in C2C12 myotubes derived from skeletal muscle

Author keywords

Akt; Hydrogen peroxide; Oxidative stress; Protein thiol oxidation; Reactive oxygen species

Indexed keywords

ANTIOXIDANT; CATALASE; GLUCOSE OXIDASE; HYDROGEN PEROXIDE; OXIDIZING AGENT; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEIN KINASE B; THIOL; PHOSPHOPROTEIN PHOSPHATASE 2; REACTIVE OXYGEN METABOLITE; THIOL DERIVATIVE;

EID: 84924528082     PISSN: 13572725     EISSN: 18785875     Source Type: Journal    
DOI: 10.1016/j.biocel.2015.02.015     Document Type: Article
Times cited : (50)

References (67)
  • 1
    • 0029804116 scopus 로고    scopus 로고
    • Mechanism of activation of protein kinase B by insulin and IGF-1
    • D.R. Alessi, M. Andjelkovic, B. Caudwell, P. Cron, N. Morrice, and P. Cohen Mechanism of activation of protein kinase B by insulin and IGF-1 EMBO J 15 23 1996 6541 6551
    • (1996) EMBO J , vol.15 , Issue.23 , pp. 6541-6551
    • Alessi, D.R.1    Andjelkovic, M.2    Caudwell, B.3    Cron, P.4    Morrice, N.5    Cohen, P.6
  • 2
    • 84866133072 scopus 로고    scopus 로고
    • Reactive oxygen species in health and disease
    • A.A. Alfadda, and R.M. Sallam Reactive oxygen species in health and disease J Biomed Biotechnol 2012 2012 936486
    • (2012) J Biomed Biotechnol , vol.2012 , pp. 936486
    • Alfadda, A.A.1    Sallam, R.M.2
  • 3
    • 82755166890 scopus 로고    scopus 로고
    • Inhibition of pyruvate kinase M2 by reactive oxygen species contributes to cellular antioxidant responses
    • D. Anastasiou, G. Poulogiannis, J.M. Asara, M.B. Boxer, Jiang J.-K., and M. Shen Inhibition of pyruvate kinase M2 by reactive oxygen species contributes to cellular antioxidant responses Science 334 6060 2011 1278 1283
    • (2011) Science , vol.334 , Issue.6060 , pp. 1278-1283
    • Anastasiou, D.1    Poulogiannis, G.2    Asara, J.M.3    Boxer, M.B.4    Jiang, J.-K.5    Shen, M.6
  • 4
    • 79251609052 scopus 로고    scopus 로고
    • A fluorescent dual labeling technique for the quantitative measurement of reduced and oxidized protein thiols in tissue samples
    • A.E. Armstrong, R. Zerbes, P.A. Fournier, and P.G. Arthur A fluorescent dual labeling technique for the quantitative measurement of reduced and oxidized protein thiols in tissue samples Free Radic Biol Med 50 4 2011 510 517
    • (2011) Free Radic Biol Med , vol.50 , Issue.4 , pp. 510-517
    • Armstrong, A.E.1    Zerbes, R.2    Fournier, P.A.3    Arthur, P.G.4
  • 5
    • 54049086602 scopus 로고    scopus 로고
    • Oxidative stress as a therapeutic target during muscle wasting: Considering the complex interactions
    • P.G. Arthur, M.D. Grounds, and T. Shavlakadze Oxidative stress as a therapeutic target during muscle wasting: considering the complex interactions Curr Opin Clin Nutr Metab Care 11 4 2008 408 416
    • (2008) Curr Opin Clin Nutr Metab Care , vol.11 , Issue.4 , pp. 408-416
    • Arthur, P.G.1    Grounds, M.D.2    Shavlakadze, T.3
  • 6
    • 84857288275 scopus 로고    scopus 로고
    • Reactive oxygen species in skeletal muscle signaling
    • E. Barbieri, and P. Sestili Reactive oxygen species in skeletal muscle signaling J Signal Transduct 2012 2012 982794
    • (2012) J Signal Transduct , vol.2012 , pp. 982794
    • Barbieri, E.1    Sestili, P.2
  • 7
    • 33744938902 scopus 로고    scopus 로고
    • Viral expression of insulin-like growth factor-I isoforms promotes different responses in skeletal muscle
    • E.R. Barton Viral expression of insulin-like growth factor-I isoforms promotes different responses in skeletal muscle J Appl Physiol 100 6 2006 1778 1784
    • (2006) J Appl Physiol , vol.100 , Issue.6 , pp. 1778-1784
    • Barton, E.R.1
  • 8
    • 77954370180 scopus 로고    scopus 로고
    • Acute oxidative stress can reverse insulin resistance by inactivation of cytoplasmic JNK
    • A. Berdichevsky, L. Guarente, and A. Bose Acute oxidative stress can reverse insulin resistance by inactivation of cytoplasmic JNK J Biol Chem 285 28 2010 21581 21589
    • (2010) J Biol Chem , vol.285 , Issue.28 , pp. 21581-21589
    • Berdichevsky, A.1    Guarente, L.2    Bose, A.3
  • 10
    • 0035499454 scopus 로고    scopus 로고
    • Ten years of protein kinase B signalling: A hard Akt to follow
    • D.P. Brazil, and B.A. Hemmings Ten years of protein kinase B signalling: a hard Akt to follow Trends Biochem Sci 26 11 2001 657 664
    • (2001) Trends Biochem Sci , vol.26 , Issue.11 , pp. 657-664
    • Brazil, D.P.1    Hemmings, B.A.2
  • 11
    • 0018776894 scopus 로고
    • Hydroperoxide metabolism in mammalian organs
    • B. Chance, H. Sies, and A. Boveris Hydroperoxide metabolism in mammalian organs Physiol Rev 59 3 1979 527 605
    • (1979) Physiol Rev , vol.59 , Issue.3 , pp. 527-605
    • Chance, B.1    Sies, H.2    Boveris, A.3
  • 12
    • 0842309140 scopus 로고    scopus 로고
    • Diversity of structures and properties among catalases
    • P. Chelikani, I. Fita, and P.C. Loewen Diversity of structures and properties among catalases Cell Mol Life Sci 61 2 2004 192 208
    • (2004) Cell Mol Life Sci , vol.61 , Issue.2 , pp. 192-208
    • Chelikani, P.1    Fita, I.2    Loewen, P.C.3
  • 13
    • 51349166119 scopus 로고    scopus 로고
    • Cadmium activates the mitogen-activated protein kinase (MAPK) pathway via induction of reactive oxygen species and inhibition of protein phosphatases 2A and 5
    • L. Chen, L. Liu, and S. Huang Cadmium activates the mitogen-activated protein kinase (MAPK) pathway via induction of reactive oxygen species and inhibition of protein phosphatases 2A and 5 Free Radic Biol Med 45 7 2008 1035 1044
    • (2008) Free Radic Biol Med , vol.45 , Issue.7 , pp. 1035-1044
    • Chen, L.1    Liu, L.2    Huang, S.3
  • 14
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three Akts
    • S.R. Datta, A. Brunet, and M.E. Greenberg Cellular survival: a play in three Akts Genes Dev 13 22 1999 2905 2927
    • (1999) Genes Dev , vol.13 , Issue.22 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 15
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals. I. General aspects
    • K.J. Davies Protein damage and degradation by oxygen radicals. I. General aspects J Biol Chem 262 20 1987 9895 9901
    • (1987) J Biol Chem , vol.262 , Issue.20 , pp. 9895-9901
    • Davies, K.J.1
  • 16
    • 0030988742 scopus 로고    scopus 로고
    • Biochemistry and pathology of radical-mediated protein oxidation
    • R.T. Dean, S. Fu, R. Stocker, and M.J. Davies Biochemistry and pathology of radical-mediated protein oxidation Biochem J 324 Pt 1 1997 1 18
    • (1997) Biochem J , vol.324 , pp. 1-18
    • Dean, R.T.1    Fu, S.2    Stocker, R.3    Davies, M.J.4
  • 17
    • 84862288438 scopus 로고    scopus 로고
    • Relationship between human aging muscle and oxidative system pathway
    • E. Doria, D. Buonocore, A. Focarelli, and F. Marzatico Relationship between human aging muscle and oxidative system pathway Oxid Med Cell Longev 2012 2012 830257
    • (2012) Oxid Med Cell Longev , vol.2012 , pp. 830257
    • Doria, E.1    Buonocore, D.2    Focarelli, A.3    Marzatico, F.4
  • 18
    • 84860908312 scopus 로고    scopus 로고
    • Redox modification of Akt mediated by the dopaminergic neurotoxin MPTP, in mouse midbrain, leads to down-regulation of pAkt
    • L. Durgadoss, P. Nidadavolu, R.K. Valli, U. Saeed, M. Mishra, and P. Seth Redox modification of Akt mediated by the dopaminergic neurotoxin MPTP, in mouse midbrain, leads to down-regulation of pAkt FASEB J 26 4 2012 1473 1483
    • (2012) FASEB J , vol.26 , Issue.4 , pp. 1473-1483
    • Durgadoss, L.1    Nidadavolu, P.2    Valli, R.K.3    Saeed, U.4    Mishra, M.5    Seth, P.6
  • 19
    • 77955125672 scopus 로고    scopus 로고
    • A stress survival response in retinal cells mediated through inhibition of the serine/threonine phosphatase PP2A
    • S. Finnegan, A.M. Mackey, and T.G. Cotter A stress survival response in retinal cells mediated through inhibition of the serine/threonine phosphatase PP2A Eur J Neurosci 32 3 2010 322 334
    • (2010) Eur J Neurosci , vol.32 , Issue.3 , pp. 322-334
    • Finnegan, S.1    Mackey, A.M.2    Cotter, T.G.3
  • 20
    • 34848914455 scopus 로고    scopus 로고
    • Oxidative inhibition of protein phosphatase 2A activity: Role of catalytic subunit disulfides
    • T. Foley, L. Petro, C. Stredny, and T. Coppa Oxidative inhibition of protein phosphatase 2A activity: role of catalytic subunit disulfides Neurochem Res 32 11 2007 1957 1964
    • (2007) Neurochem Res , vol.32 , Issue.11 , pp. 1957-1964
    • Foley, T.1    Petro, L.2    Stredny, C.3    Coppa, T.4
  • 22
    • 23944456384 scopus 로고    scopus 로고
    • Skeletal muscle hypertrophy and atrophy signaling pathways
    • D.J. Glass Skeletal muscle hypertrophy and atrophy signaling pathways Int J Biochem Cell Biol 37 10 2005 1974 1984
    • (2005) Int J Biochem Cell Biol , vol.37 , Issue.10 , pp. 1974-1984
    • Glass, D.J.1
  • 23
    • 0037030584 scopus 로고    scopus 로고
    • Induction of protein catabolism and the ubiquitin-proteasome pathway by mild oxidative stress
    • M.C. Gomes-Marcondes, and M.J. Tisdale Induction of protein catabolism and the ubiquitin-proteasome pathway by mild oxidative stress Cancer Lett 180 1 2002 69 74
    • (2002) Cancer Lett , vol.180 , Issue.1 , pp. 69-74
    • Gomes-Marcondes, M.C.1    Tisdale, M.J.2
  • 24
    • 0037430971 scopus 로고    scopus 로고
    • Oxidative stress in cell culture: An under-appreciated problem?
    • B. Halliwell Oxidative stress in cell culture: an under-appreciated problem? FEBS Lett 540 1-3 2003 3 6
    • (2003) FEBS Lett , vol.540 , Issue.13 , pp. 3-6
    • Halliwell, B.1
  • 25
    • 79951936969 scopus 로고    scopus 로고
    • Reactive oxygen species play an essential role in IGF-I signaling and IGF-I-induced myocyte hypertrophy in C2C12 myocytes
    • A.E. Handayaningsih, G. Iguchi, H. Fukuoka, H. Nishizawa, M. Takahashi, and M. Yamamoto Reactive oxygen species play an essential role in IGF-I signaling and IGF-I-induced myocyte hypertrophy in C2C12 myocytes Endocrinology 152 3 2011 912 921
    • (2011) Endocrinology , vol.152 , Issue.3 , pp. 912-921
    • Handayaningsih, A.E.1    Iguchi, G.2    Fukuoka, H.3    Nishizawa, H.4    Takahashi, M.5    Yamamoto, M.6
  • 27
    • 4544235672 scopus 로고    scopus 로고
    • The molecular basis of skeletal muscle atrophy
    • R.W. Jackman, and S.C. Kandarian The molecular basis of skeletal muscle atrophy Am J Physiol Cell Physiol 287 4 2004 C834 C843
    • (2004) Am J Physiol Cell Physiol , vol.287 , Issue.4 , pp. C834-C843
    • Jackman, R.W.1    Kandarian, S.C.2
  • 28
    • 84872858018 scopus 로고    scopus 로고
    • Contribution of oxidative stress to pathology in diaphragm and limb muscles with Duchenne muscular dystrophy
    • J.H. Kim, H.B. Kwak, L.V. Thompson, and J.M. Lawler Contribution of oxidative stress to pathology in diaphragm and limb muscles with Duchenne muscular dystrophy J Muscle Res Cell Motil 34 1 2013 1 13
    • (2013) J Muscle Res Cell Motil , vol.34 , Issue.1 , pp. 1-13
    • Kim, J.H.1    Kwak, H.B.2    Thompson, L.V.3    Lawler, J.M.4
  • 29
    • 0030785701 scopus 로고    scopus 로고
    • Activation of protein kinase B (Akt/RAC-protein kinase) by cellular stress and its association with heat shock protein Hsp27
    • H. Konishi, H. Matsuzaki, M. Tanaka, Y. Takemura, S. Kuroda, and Y. Ono Activation of protein kinase B (Akt/RAC-protein kinase) by cellular stress and its association with heat shock protein Hsp27 FEBS Lett 410 2-3 1997 493 498
    • (1997) FEBS Lett , vol.410 , Issue.23 , pp. 493-498
    • Konishi, H.1    Matsuzaki, H.2    Tanaka, M.3    Takemura, Y.4    Kuroda, S.5    Ono, Y.6
  • 33
    • 33750906556 scopus 로고    scopus 로고
    • The redox regulation of PI 3-kinase-dependent signaling
    • N.R. Leslie The redox regulation of PI 3-kinase-dependent signaling Antioxid Redox Signal 8 9-10 2006 1765 1774
    • (2006) Antioxid Redox Signal , vol.8 , Issue.910 , pp. 1765-1774
    • Leslie, N.R.1
  • 34
    • 0142137134 scopus 로고    scopus 로고
    • Redox regulation of PI 3-kinase signalling via inactivation of PTEN
    • N.R. Leslie, D. Bennett, Y.E. Lindsay, H. Stewart, A. Gray, and C.P. Downes Redox regulation of PI 3-kinase signalling via inactivation of PTEN EMBO J 22 20 2003 5501 5510
    • (2003) EMBO J , vol.22 , Issue.20 , pp. 5501-5510
    • Leslie, N.R.1    Bennett, D.2    Lindsay, Y.E.3    Stewart, H.4    Gray, A.5    Downes, C.P.6
  • 35
    • 0036181869 scopus 로고    scopus 로고
    • PTEN: The down side of PI 3-kinase signalling
    • N.R. Leslie, and C.P. Downes PTEN: the down side of PI 3-kinase signalling Cell Signal 14 4 2002 285 295
    • (2002) Cell Signal , vol.14 , Issue.4 , pp. 285-295
    • Leslie, N.R.1    Downes, C.P.2
  • 36
    • 73649141725 scopus 로고    scopus 로고
    • Detecting changes in the thiol redox state of proteins following a decrease in oxygen concentration using a dual labeling technique
    • J.K. Lui, R. Lipscombe, and P.G. Arthur Detecting changes in the thiol redox state of proteins following a decrease in oxygen concentration using a dual labeling technique J Proteome Res 9 1 2010 383 392
    • (2010) J Proteome Res , vol.9 , Issue.1 , pp. 383-392
    • Lui, J.K.1    Lipscombe, R.2    Arthur, P.G.3
  • 38
    • 34047213532 scopus 로고    scopus 로고
    • Oxidative stress, chronic disease, and muscle wasting
    • J.S. Moylan, and M.B. Reid Oxidative stress, chronic disease, and muscle wasting Muscle Nerve 35 4 2007 411 429
    • (2007) Muscle Nerve , vol.35 , Issue.4 , pp. 411-429
    • Moylan, J.S.1    Reid, M.B.2
  • 39
    • 33646588683 scopus 로고    scopus 로고
    • Absence of CuZn superoxide dismutase leads to elevated oxidative stress and acceleration of age-dependent skeletal muscle atrophy
    • F.L. Muller, W. Song, Y. Liu, A. Chaudhuri, S. Pieke-Dahl, and R. Strong Absence of CuZn superoxide dismutase leads to elevated oxidative stress and acceleration of age-dependent skeletal muscle atrophy Free Radic Biol Med 40 11 2006 1993 2004
    • (2006) Free Radic Biol Med , vol.40 , Issue.11 , pp. 1993-2004
    • Muller, F.L.1    Song, W.2    Liu, Y.3    Chaudhuri, A.4    Pieke-Dahl, S.5    Strong, R.6
  • 40
    • 0346749513 scopus 로고    scopus 로고
    • Glutaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt
    • H. Murata, Y. Ihara, H. Nakamura, J. Yodoi, K. Sumikawa, and T. Kondo Glutaredoxin exerts an antiapoptotic effect by regulating the redox state of Akt J Biol Chem 278 50 2003 50226 50233
    • (2003) J Biol Chem , vol.278 , Issue.50 , pp. 50226-50233
    • Murata, H.1    Ihara, Y.2    Nakamura, H.3    Yodoi, J.4    Sumikawa, K.5    Kondo, T.6
  • 41
    • 0035136062 scopus 로고    scopus 로고
    • Localized Igf-1 transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle
    • A. Musaro, K. McCullagh, A. Paul, L. Houghton, G. Dobrowolny, and M. Molinaro Localized Igf-1 transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle Nat Genet 27 2 2001 195 200
    • (2001) Nat Genet , vol.27 , Issue.2 , pp. 195-200
    • Musaro, A.1    McCullagh, K.2    Paul, A.3    Houghton, L.4    Dobrowolny, G.5    Molinaro, M.6
  • 42
    • 84901757447 scopus 로고    scopus 로고
    • Inflammation based regulation of cancer cachexia
    • 2014
    • J.K. Onesti, and D.C. Guttridge Inflammation based regulation of cancer cachexia BioMed Res Int 2014 168407 2014
    • (2014) BioMed Res Int , pp. 168407
    • Onesti, J.K.1    Guttridge, D.C.2
  • 44
    • 0028818999 scopus 로고
    • Glucose oxidase as an analytical reagent
    • J. Raba, and H.A. Mottola Glucose oxidase as an analytical reagent Crit Rev Anal Chem 25 1 1995 1 42
    • (1995) Crit Rev Anal Chem , vol.25 , Issue.1 , pp. 1-42
    • Raba, J.1    Mottola, H.A.2
  • 45
    • 0036291166 scopus 로고    scopus 로고
    • Regulation of protein phosphatase 2A by hydrogen peroxide and glutathionylation
    • R.K. Rao, and L.W. Clayton Regulation of protein phosphatase 2A by hydrogen peroxide and glutathionylation Biochem Biophys Res Commun 293 1 2002 610 616
    • (2002) Biochem Biophys Res Commun , vol.293 , Issue.1 , pp. 610-616
    • Rao, R.K.1    Clayton, L.W.2
  • 46
    • 0036154215 scopus 로고    scopus 로고
    • Protein phosphatase 2A is the main phosphatase involved in the regulation of protein kinase B in rat adipocytes
    • S. Resjo, O. Goransson, L. Harndahl, S. Zolnierowicz, V. Manganiello, and E. Degerman Protein phosphatase 2A is the main phosphatase involved in the regulation of protein kinase B in rat adipocytes Cell Signal 14 3 2002 231 238
    • (2002) Cell Signal , vol.14 , Issue.3 , pp. 231-238
    • Resjo, S.1    Goransson, O.2    Harndahl, L.3    Zolnierowicz, S.4    Manganiello, V.5    Degerman, E.6
  • 47
    • 33645932912 scopus 로고    scopus 로고
    • Human skeletal muscle intracellular oxygenation: The impact of ambient oxygen availability
    • R.S. Richardson, S. Duteil, C. Wary, D.W. Wray, J. Hoff, and P.G. Carlier Human skeletal muscle intracellular oxygenation: the impact of ambient oxygen availability J Physiol 571 Pt 2 2006 415 424
    • (2006) J Physiol , vol.571 , pp. 415-424
    • Richardson, R.S.1    Duteil, S.2    Wary, C.3    Wray, D.W.4    Hoff, J.5    Carlier, P.G.6
  • 48
    • 0033607784 scopus 로고    scopus 로고
    • Differentiation stage-specific inhibition of the Raf-MEK-ERK pathway by Akt
    • C. Rommel, B.A. Clarke, S. Zimmermann, L. Nunez, R. Rossman, and K. Reid Differentiation stage-specific inhibition of the Raf-MEK-ERK pathway by Akt Science 286 5445 1999 1738 1741
    • (1999) Science , vol.286 , Issue.5445 , pp. 1738-1741
    • Rommel, C.1    Clarke, B.A.2    Zimmermann, S.3    Nunez, L.4    Rossman, R.5    Reid, K.6
  • 49
    • 64049100188 scopus 로고    scopus 로고
    • Hydrogen peroxide-induced Akt phosphorylation regulates Bax activation
    • M. Sadidi, S.I. Lentz, and E.L. Feldman Hydrogen peroxide-induced Akt phosphorylation regulates Bax activation Biochimie 91 5 2009 577 585
    • (2009) Biochimie , vol.91 , Issue.5 , pp. 577-585
    • Sadidi, M.1    Lentz, S.I.2    Feldman, E.L.3
  • 50
    • 84866549876 scopus 로고    scopus 로고
    • Sarcopenia and cachexia: The adaptations of negative regulators of skeletal muscle mass
    • K. Sakuma, and A. Yamaguchi Sarcopenia and cachexia: the adaptations of negative regulators of skeletal muscle mass J Cachex Sarcopenia Muscle 3 2 2012 77 94
    • (2012) J Cachex Sarcopenia Muscle , vol.3 , Issue.2 , pp. 77-94
    • Sakuma, K.1    Yamaguchi, A.2
  • 51
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex
    • D.D. Sarbassov, D.A. Guertin, S.M. Ali, and D.M. Sabatini Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex Science 307 5712 2005 1098 1101
    • (2005) Science , vol.307 , Issue.5712 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 52
    • 84863205849 scopus 로고    scopus 로고
    • NIH Image to ImageJ: 25 years of image analysis
    • C.A. Schneider, W.S. Rasband, and K.W. Eliceiri NIH Image to ImageJ: 25 years of image analysis Nat Methods 9 7 2012 671 675
    • (2012) Nat Methods , vol.9 , Issue.7 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 53
    • 84866033111 scopus 로고    scopus 로고
    • Maintenance of higher H(2)O(2) levels, and its mechanism of action to induce growth in breast cancer cells: Important roles of bioactive catalase and PP2A
    • S. Sen, B. Kawahara, and G. Chaudhuri Maintenance of higher H(2)O(2) levels, and its mechanism of action to induce growth in breast cancer cells: important roles of bioactive catalase and PP2A Free Radic Biol Med 53 8 2012 1541 1551
    • (2012) Free Radic Biol Med , vol.53 , Issue.8 , pp. 1541-1551
    • Sen, S.1    Kawahara, B.2    Chaudhuri, G.3
  • 54
    • 77951169963 scopus 로고    scopus 로고
    • A growth stimulus is needed for IGF-1 to induce skeletal muscle hypertrophy in vivo
    • T. Shavlakadze, J. Chai, K. Maley, G. Cozens, G. Grounds, and N. Winn A growth stimulus is needed for IGF-1 to induce skeletal muscle hypertrophy in vivo J Cell Sci 123 Pt 6 2010 960 971
    • (2010) J Cell Sci , vol.123 , pp. 960-971
    • Shavlakadze, T.1    Chai, J.2    Maley, K.3    Cozens, G.4    Grounds, G.5    Winn, N.6
  • 55
    • 33750026980 scopus 로고    scopus 로고
    • Of bears, frogs, meat, mice and men: Complexity of factors affecting skeletal muscle mass and fat
    • T. Shavlakadze, and M. Grounds Of bears, frogs, meat, mice and men: complexity of factors affecting skeletal muscle mass and fat Bioessays 28 10 2006 994 1009
    • (2006) Bioessays , vol.28 , Issue.10 , pp. 994-1009
    • Shavlakadze, T.1    Grounds, M.2
  • 56
    • 0032533546 scopus 로고    scopus 로고
    • 2 or heat shock is mediated by phosphoinositide 3-kinase and not by mitogen-activated protein kinase-activated protein kinase-2
    • 2 or heat shock is mediated by phosphoinositide 3-kinase and not by mitogen-activated protein kinase-activated protein kinase-2 Biochem J 336 Pt 1 1998 241 246
    • (1998) Biochem J , vol.336 , pp. 241-246
    • Shaw, M.1    Cohen, P.2    Alessi, D.R.3
  • 57
    • 0037102481 scopus 로고    scopus 로고
    • Differential susceptibilities of serine/threonine phosphatases to oxidative and nitrosative stress
    • D. Sommer, S. Coleman, S.A. Swanson, and P.M. Stemmer Differential susceptibilities of serine/threonine phosphatases to oxidative and nitrosative stress Arch Biochem Biophys 404 2 2002 271 278
    • (2002) Arch Biochem Biophys , vol.404 , Issue.2 , pp. 271-278
    • Sommer, D.1    Coleman, S.2    Swanson, S.A.3    Stemmer, P.M.4
  • 58
    • 0142011466 scopus 로고    scopus 로고
    • PTEN: From pathology to biology
    • M.L. Sulis, and R. Parsons PTEN: from pathology to biology Trends Cell Biol 13 9 2003 478 483
    • (2003) Trends Cell Biol , vol.13 , Issue.9 , pp. 478-483
    • Sulis, M.L.1    Parsons, R.2
  • 59
    • 23944501319 scopus 로고    scopus 로고
    • Signal-transduction networks and the regulation of muscle protein degradation
    • N.J. Szewczyk, and L.A. Jacobson Signal-transduction networks and the regulation of muscle protein degradation Int J Biochem Cell Biol 37 10 2005 1997 2011
    • (2005) Int J Biochem Cell Biol , vol.37 , Issue.10 , pp. 1997-2011
    • Szewczyk, N.J.1    Jacobson, L.A.2
  • 60
    • 33244464562 scopus 로고    scopus 로고
    • Critical nodes in signalling pathways: Insights into insulin action
    • C.M. Taniguchi, B. Emanuelli, and C.R. Kahn Critical nodes in signalling pathways: insights into insulin action Nat Rev Mol Cell Biol 7 2 2006 85 96
    • (2006) Nat Rev Mol Cell Biol , vol.7 , Issue.2 , pp. 85-96
    • Taniguchi, C.M.1    Emanuelli, B.2    Kahn, C.R.3
  • 61
    • 84881160375 scopus 로고    scopus 로고
    • Treatment with the cysteine precursor l-2-oxothiazolidine-4-carboxylate (OTC) implicates taurine deficiency in severity of dystropathology in mdx mice
    • J.R. Terrill, A. Boyatzis, M.D. Grounds, and P.G. Arthur Treatment with the cysteine precursor l-2-oxothiazolidine-4-carboxylate (OTC) implicates taurine deficiency in severity of dystropathology in mdx mice Int J Biochem Cell Biol 45 9 2013 2097 2108
    • (2013) Int J Biochem Cell Biol , vol.45 , Issue.9 , pp. 2097-2108
    • Terrill, J.R.1    Boyatzis, A.2    Grounds, M.D.3    Arthur, P.G.4
  • 62
    • 0033529675 scopus 로고    scopus 로고
    • Reactive oxygen species mediate the activation of Akt/protein kinase B by angiotensin II in vascular smooth muscle cells
    • M. Ushio-Fukai, R.W. Alexander, M. Akers, Q. Yin, Y. Fujio, and K. Walsh Reactive oxygen species mediate the activation of Akt/protein kinase B by angiotensin II in vascular smooth muscle cells J Biol Chem 274 32 1999 22699 22704
    • (1999) J Biol Chem , vol.274 , Issue.32 , pp. 22699-22704
    • Ushio-Fukai, M.1    Alexander, R.W.2    Akers, M.3    Yin, Q.4    Fujio, Y.5    Walsh, K.6
  • 63
    • 48449107159 scopus 로고    scopus 로고
    • Thiol chemistry and specificity in redox signaling
    • C.C. Winterbourn, and M.B. Hampton Thiol chemistry and specificity in redox signaling Free Radic Biol Med 45 5 2008 549 561
    • (2008) Free Radic Biol Med , vol.45 , Issue.5 , pp. 549-561
    • Winterbourn, C.C.1    Hampton, M.B.2
  • 64
    • 32944481494 scopus 로고    scopus 로고
    • Optimization, application, and interpretation of lactate dehydrogenase measurements in microwell determination of cell number and toxicity
    • H.T. Wolterbeek, and A.J. van der Meer Optimization, application, and interpretation of lactate dehydrogenase measurements in microwell determination of cell number and toxicity Assay Drug Dev Technol 3 6 2005 675 682
    • (2005) Assay Drug Dev Technol , vol.3 , Issue.6 , pp. 675-682
    • Wolterbeek, H.T.1    Van Der Meer, A.J.2
  • 65
    • 0034306245 scopus 로고    scopus 로고
    • P53 protein oxidation in cultured cells in response to pyrrolidine dithiocarbamate: A novel method for relating the amount of p53 oxidation in vivo to the regulation of p53-responsive genes
    • H.H. Wu, J.A. Thomas, and J. Momand p53 protein oxidation in cultured cells in response to pyrrolidine dithiocarbamate: a novel method for relating the amount of p53 oxidation in vivo to the regulation of p53-responsive genes Biochem J 351 Pt 1 2000 87 93
    • (2000) Biochem J , vol.351 , pp. 87-93
    • Wu, H.H.1    Thomas, J.A.2    Momand, J.3
  • 66
    • 84870478286 scopus 로고    scopus 로고
    • Redox-sensitive oxidation and phosphorylation of PTEN contribute to enhanced activation of PI3K/Akt signaling in rostral ventrolateral medulla and neurogenic hypertension in spontaneously hypertensive rats
    • K.L. Wu, C.A. Wu, C.W. Wu, S.H. Chan, A.Y. Chang, and J.Y. Chan Redox-sensitive oxidation and phosphorylation of PTEN contribute to enhanced activation of PI3K/Akt signaling in rostral ventrolateral medulla and neurogenic hypertension in spontaneously hypertensive rats Antioxid Redox Signal 18 1 2012 36 50
    • (2012) Antioxid Redox Signal , vol.18 , Issue.1 , pp. 36-50
    • Wu, K.L.1    Wu, C.A.2    Wu, C.W.3    Chan, S.H.4    Chang, A.Y.5    Chan, J.Y.6
  • 67
    • 33847617937 scopus 로고    scopus 로고
    • Distinct signalling pathways for induction of MAP kinase activities by cadmium and copper in rice roots
    • C.M. Yeh, P.S. Chien, and H.J. Huang Distinct signalling pathways for induction of MAP kinase activities by cadmium and copper in rice roots J Exp Bot 58 3 2007 659 671
    • (2007) J Exp Bot , vol.58 , Issue.3 , pp. 659-671
    • Yeh, C.M.1    Chien, P.S.2    Huang, H.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.