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Volumn 41, Issue 2, 2012, Pages 297-322

Multifaceted Role of Insulin-Like Growth Factors and Mammalian Target of Rapamycin in Skeletal Muscle

Author keywords

Insulin like growth factors; Mammalian target of rapamycin; Muscle mass; Skeletal muscle

Indexed keywords

ANDROGEN; ANDROGEN RECEPTOR; ANDROSTANOLONE; DEXAMETHASONE; FOLLISTATIN; GLUCOCORTICOID; INSULIN; MAMMALIAN TARGET OF RAPAMYCIN; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 1; MAMMALIAN TARGET OF RAPAMYCIN COMPLEX 2; MITOGEN ACTIVATED PROTEIN KINASE; MYOSTATIN; PRASTERONE; PROTEIN KINASE B; RAG1 PROTEIN; RAG2 PROTEIN; RHEB PROTEIN; SOMATOMEDIN; SOMATOMEDIN B; SOMATOMEDIN BINDING PROTEIN; SOMATOMEDIN RECEPTOR;

EID: 84861975535     PISSN: 08898529     EISSN: 15584410     Source Type: Journal    
DOI: 10.1016/j.ecl.2012.04.012     Document Type: Review
Times cited : (29)

References (218)
  • 2
    • 78049448432 scopus 로고    scopus 로고
    • Altered signalling from germline to intestine pushes daf-2;pept-1 Caenorhabditis elegans into extreme longevity
    • Spanier B., Rubio-Aliaga I., Hu H., et al. Altered signalling from germline to intestine pushes daf-2;pept-1 Caenorhabditis elegans into extreme longevity. Aging Cell 2010, 9:636.
    • (2010) Aging Cell , vol.9 , pp. 636
    • Spanier, B.1    Rubio-Aliaga, I.2    Hu, H.3
  • 3
    • 77956544551 scopus 로고    scopus 로고
    • Impaired muscle regeneration and myoblast differentiation in mice with a muscle-specific KO of IGF-IR
    • Heron-Milhavet L., Mamaeva D., LeRoith D., et al. Impaired muscle regeneration and myoblast differentiation in mice with a muscle-specific KO of IGF-IR. J Cell Physiol 2010, 225:1.
    • (2010) J Cell Physiol , vol.225 , pp. 1
    • Heron-Milhavet, L.1    Mamaeva, D.2    LeRoith, D.3
  • 4
    • 77952477337 scopus 로고    scopus 로고
    • Regulatory factors and cell populations involved in skeletal muscle regeneration
    • Ten Broek R.W., Grefte S., Von den Hoff J.W. Regulatory factors and cell populations involved in skeletal muscle regeneration. J Cell Physiol 2010, 224:7.
    • (2010) J Cell Physiol , vol.224 , pp. 7
    • Ten Broek, R.W.1    Grefte, S.2    Von den Hoff, J.W.3
  • 5
    • 0027496895 scopus 로고
    • Mice carrying null mutations of the genes encoding insulin-like growth factor I (Igf-1) and type 1 IGF receptor (Igf1r)
    • Liu J.P., Baker J., Perkins A.S., et al. Mice carrying null mutations of the genes encoding insulin-like growth factor I (Igf-1) and type 1 IGF receptor (Igf1r). Cell 1993, 75:59.
    • (1993) Cell , vol.75 , pp. 59
    • Liu, J.P.1    Baker, J.2    Perkins, A.S.3
  • 6
    • 0033303497 scopus 로고    scopus 로고
    • Insulin-like growth factor I is essential for postnatal growth in response to growth hormone
    • Liu J.L., LeRoith D. Insulin-like growth factor I is essential for postnatal growth in response to growth hormone. Endocrinology 1999, 140:5178.
    • (1999) Endocrinology , vol.140 , pp. 5178
    • Liu, J.L.1    LeRoith, D.2
  • 7
    • 78049429504 scopus 로고    scopus 로고
    • Distinct growth hormone receptor signaling modes regulate skeletal muscle development and insulin sensitivity in mice
    • Mavalli M.D., DiGirolamo D.J., Fan Y., et al. Distinct growth hormone receptor signaling modes regulate skeletal muscle development and insulin sensitivity in mice. J Clin Invest 2010, 120:4007.
    • (2010) J Clin Invest , vol.120 , pp. 4007
    • Mavalli, M.D.1    DiGirolamo, D.J.2    Fan, Y.3
  • 8
    • 69949091564 scopus 로고    scopus 로고
    • Role of IGF-I in skeletal muscle mass maintenance
    • Clemmons D.R. Role of IGF-I in skeletal muscle mass maintenance. Trends Endocrinol Metab 2009, 20:349.
    • (2009) Trends Endocrinol Metab , vol.20 , pp. 349
    • Clemmons, D.R.1
  • 10
    • 69249119937 scopus 로고    scopus 로고
    • Elevated levels of insulin-like growth factor (IGF)-I in serum rescue the severe growth retardation of IGF-I null mice
    • Wu Y., Sun H., Yakar S., et al. Elevated levels of insulin-like growth factor (IGF)-I in serum rescue the severe growth retardation of IGF-I null mice. Endocrinology 2009, 150:4395.
    • (2009) Endocrinology , vol.150 , pp. 4395
    • Wu, Y.1    Sun, H.2    Yakar, S.3
  • 11
    • 39049169099 scopus 로고    scopus 로고
    • Rat hindlimb unloading down-regulates insulin like growth factor-1 signaling and AMP-activated protein kinase, and leads to severe atrophy of the soleus muscle
    • Han B., Zhu M.J., Ma C., et al. Rat hindlimb unloading down-regulates insulin like growth factor-1 signaling and AMP-activated protein kinase, and leads to severe atrophy of the soleus muscle. Appl Physiol Nutr Metab 2007, 32:1115.
    • (2007) Appl Physiol Nutr Metab , vol.32 , pp. 1115
    • Han, B.1    Zhu, M.J.2    Ma, C.3
  • 12
    • 53949118974 scopus 로고    scopus 로고
    • Insulin-like growth factor-I analogue protects muscles of dystrophic mdx mice from contraction-mediated damage
    • Gehrig S.M., Ryall J.G., Schertzer J.D., et al. Insulin-like growth factor-I analogue protects muscles of dystrophic mdx mice from contraction-mediated damage. Exp Physiol 2008, 93:1190.
    • (2008) Exp Physiol , vol.93 , pp. 1190
    • Gehrig, S.M.1    Ryall, J.G.2    Schertzer, J.D.3
  • 13
    • 34447644976 scopus 로고    scopus 로고
    • Protein kinase B/Akt: a nexus of growth factor and cytokine signaling in determining muscle mass
    • Frost R.A., Lang C.H. Protein kinase B/Akt: a nexus of growth factor and cytokine signaling in determining muscle mass. J Appl Physiol 2007, 103:378.
    • (2007) J Appl Physiol , vol.103 , pp. 378
    • Frost, R.A.1    Lang, C.H.2
  • 14
    • 73649131977 scopus 로고    scopus 로고
    • Mechanisms of muscle atrophy induced by glucocorticoids
    • Schakman O., Gilson H., Kalista S., et al. Mechanisms of muscle atrophy induced by glucocorticoids. Horm Res 2009, 72(Suppl 1):36.
    • (2009) Horm Res , vol.72 , Issue.SUPPL. 1 , pp. 36
    • Schakman, O.1    Gilson, H.2    Kalista, S.3
  • 15
    • 77953743373 scopus 로고    scopus 로고
    • Dexamethasone administration inhibits skeletal muscle expression of the androgen receptor and IGF-1-implications for steroid-induced myopathy
    • Inder W.J., Jang C., Obeyesekere V.R., et al. Dexamethasone administration inhibits skeletal muscle expression of the androgen receptor and IGF-1-implications for steroid-induced myopathy. Clin Endocrinol (Oxf) 2010, 73:126.
    • (2010) Clin Endocrinol (Oxf) , vol.73 , pp. 126
    • Inder, W.J.1    Jang, C.2    Obeyesekere, V.R.3
  • 16
    • 29144513918 scopus 로고    scopus 로고
    • Prevention and treatment of cancer cachexia: new insights into an old problem
    • Muscaritoli M., Bossola M., Aversa Z., et al. Prevention and treatment of cancer cachexia: new insights into an old problem. Eur J Cancer 2006, 42:31.
    • (2006) Eur J Cancer , vol.42 , pp. 31
    • Muscaritoli, M.1    Bossola, M.2    Aversa, Z.3
  • 17
    • 0036067537 scopus 로고    scopus 로고
    • What is the role of the insulin-like growth factor system in the pathophysiology of cancer cachexia, and how is it regulated?
    • Crown A.L., Cottle K., Lightman S.L., et al. What is the role of the insulin-like growth factor system in the pathophysiology of cancer cachexia, and how is it regulated?. Clin Endocrinol (Oxf) 2002, 56:723.
    • (2002) Clin Endocrinol (Oxf) , vol.56 , pp. 723
    • Crown, A.L.1    Cottle, K.2    Lightman, S.L.3
  • 18
    • 0037636452 scopus 로고    scopus 로고
    • Regulation of insulin-like growth factor-I in skeletal muscle and muscle cells
    • Frost R.A., Lang C.H. Regulation of insulin-like growth factor-I in skeletal muscle and muscle cells. Minerva Endocrinol 2003, 28:53.
    • (2003) Minerva Endocrinol , vol.28 , pp. 53
    • Frost, R.A.1    Lang, C.H.2
  • 19
    • 33751184935 scopus 로고    scopus 로고
    • Comparative evaluation of IGF-I gene transfer and IGF-I protein administration for enhancing skeletal muscle regeneration after injury
    • Schertzer J.D., Lynch G.S. Comparative evaluation of IGF-I gene transfer and IGF-I protein administration for enhancing skeletal muscle regeneration after injury. Gene Ther 2006, 13:1657.
    • (2006) Gene Ther , vol.13 , pp. 1657
    • Schertzer, J.D.1    Lynch, G.S.2
  • 20
    • 78751683605 scopus 로고    scopus 로고
    • Impaired muscle growth and response to insulin-like growth factor 1 in dysferlin-mediated muscular dystrophy
    • Demonbreun A.R., Fahrenbach J.P., Deveaux K., et al. Impaired muscle growth and response to insulin-like growth factor 1 in dysferlin-mediated muscular dystrophy. Hum Mol Genet 2011, 20:779.
    • (2011) Hum Mol Genet , vol.20 , pp. 779
    • Demonbreun, A.R.1    Fahrenbach, J.P.2    Deveaux, K.3
  • 22
    • 35348909483 scopus 로고    scopus 로고
    • Modulation of insulin-like growth factor (IGF)-I and IGF-binding protein interactions enhances skeletal muscle regeneration and ameliorates the dystrophic pathology in mdx mice
    • Schertzer J.D., Gehrig S.M., Ryall J.G., et al. Modulation of insulin-like growth factor (IGF)-I and IGF-binding protein interactions enhances skeletal muscle regeneration and ameliorates the dystrophic pathology in mdx mice. Am J Pathol 2007, 171:1180.
    • (2007) Am J Pathol , vol.171 , pp. 1180
    • Schertzer, J.D.1    Gehrig, S.M.2    Ryall, J.G.3
  • 23
    • 0141625007 scopus 로고    scopus 로고
    • Effects of insulin-like growth factor-1/binding protein-3 complex on muscle atrophy in rats
    • Zdanowicz M.M., Teichberg S. Effects of insulin-like growth factor-1/binding protein-3 complex on muscle atrophy in rats. Exp Biol Med (Maywood) 2003, 228:891.
    • (2003) Exp Biol Med (Maywood) , vol.228 , pp. 891
    • Zdanowicz, M.M.1    Teichberg, S.2
  • 24
    • 0033504901 scopus 로고    scopus 로고
    • Muscle protein catabolism after severe burn: effects of IGF-1/IGFBP-3 treatment
    • Herndon D.N., Ramzy P.I., DebRoy M.A., et al. Muscle protein catabolism after severe burn: effects of IGF-1/IGFBP-3 treatment. Ann Surg 1999, 229:713.
    • (1999) Ann Surg , vol.229 , pp. 713
    • Herndon, D.N.1    Ramzy, P.I.2    DebRoy, M.A.3
  • 25
    • 1542374743 scopus 로고    scopus 로고
    • Activation of mTOR signaling by novel fluoromethylene phosphonate analogues of phosphatidic acid
    • Xu Y., Fang Y., Chen J., et al. Activation of mTOR signaling by novel fluoromethylene phosphonate analogues of phosphatidic acid. Bioorg Med Chem Lett 2004, 14:1461.
    • (2004) Bioorg Med Chem Lett , vol.14 , pp. 1461
    • Xu, Y.1    Fang, Y.2    Chen, J.3
  • 26
    • 78751485448 scopus 로고    scopus 로고
    • Insulin receptor substrates Irs1 and Irs2 coordinate skeletal muscle growth and metabolism via the Akt and AMPK pathways
    • Long Y.C., Cheng Z., Copps K.D., et al. Insulin receptor substrates Irs1 and Irs2 coordinate skeletal muscle growth and metabolism via the Akt and AMPK pathways. Mol Cell Biol 2011, 31:430.
    • (2011) Mol Cell Biol , vol.31 , pp. 430
    • Long, Y.C.1    Cheng, Z.2    Copps, K.D.3
  • 27
    • 77951444244 scopus 로고    scopus 로고
    • Anabolic and catabolic pathways regulating skeletal muscle mass
    • McCarthy J.J., Esser K.A. Anabolic and catabolic pathways regulating skeletal muscle mass. Curr Opin Clin Nutr Metab Care 2010, 13:230.
    • (2010) Curr Opin Clin Nutr Metab Care , vol.13 , pp. 230
    • McCarthy, J.J.1    Esser, K.A.2
  • 28
    • 74049088121 scopus 로고    scopus 로고
    • Muscle inactivation of mTOR causes metabolic and dystrophin defects leading to severe myopathy
    • Risson V., Mazelin L., Roceri M., et al. Muscle inactivation of mTOR causes metabolic and dystrophin defects leading to severe myopathy. J Cell Biol 2009, 187:859.
    • (2009) J Cell Biol , vol.187 , pp. 859
    • Risson, V.1    Mazelin, L.2    Roceri, M.3
  • 29
    • 54849426651 scopus 로고    scopus 로고
    • Skeletal muscle-specific ablation of raptor, but not of rictor, causes metabolic changes and results in muscle dystrophy
    • Bentzinger C.F., Romanino K., Cloetta D., et al. Skeletal muscle-specific ablation of raptor, but not of rictor, causes metabolic changes and results in muscle dystrophy. Cell Metab 2008, 8:411.
    • (2008) Cell Metab , vol.8 , pp. 411
    • Bentzinger, C.F.1    Romanino, K.2    Cloetta, D.3
  • 30
    • 70649088097 scopus 로고    scopus 로고
    • Changes in GH/IGF-1 axis in intrauterine growth retardation: consequences of fetal programming?
    • Setia S., Sridhar M.G. Changes in GH/IGF-1 axis in intrauterine growth retardation: consequences of fetal programming?. Horm Metab Res 2009, 41:791.
    • (2009) Horm Metab Res , vol.41 , pp. 791
    • Setia, S.1    Sridhar, M.G.2
  • 31
    • 58149461551 scopus 로고    scopus 로고
    • Early postnatal nutrition determines somatotropic function in mice
    • Kappeler L., De Magalhaes Filho C., Leneuve P., et al. Early postnatal nutrition determines somatotropic function in mice. Endocrinology 2009, 150:314.
    • (2009) Endocrinology , vol.150 , pp. 314
    • Kappeler, L.1    De Magalhaes Filho, C.2    Leneuve, P.3
  • 33
    • 71849109375 scopus 로고    scopus 로고
    • Growth hormone and protein metabolism
    • Moller N., Vendelbo M.H., Kampmann U., et al. Growth hormone and protein metabolism. Clin Nutr 2009, 28:597.
    • (2009) Clin Nutr , vol.28 , pp. 597
    • Moller, N.1    Vendelbo, M.H.2    Kampmann, U.3
  • 34
    • 38949126221 scopus 로고    scopus 로고
    • Leucine-enriched essential amino acid and carbohydrate ingestion following resistance exercise enhances mTOR signaling and protein synthesis in human muscle
    • Dreyer H.C., Drummond M.J., Pennings B., et al. Leucine-enriched essential amino acid and carbohydrate ingestion following resistance exercise enhances mTOR signaling and protein synthesis in human muscle. Am J Physiol Endocrinol Metab 2008, 294:E392.
    • (2008) Am J Physiol Endocrinol Metab , vol.294
    • Dreyer, H.C.1    Drummond, M.J.2    Pennings, B.3
  • 35
    • 79251499260 scopus 로고    scopus 로고
    • Dietary omega-3 fatty acid supplementation increases the rate of muscle protein synthesis in older adults: a randomized controlled trial
    • Smith G.I., Atherton P., Reeds D.N., et al. Dietary omega-3 fatty acid supplementation increases the rate of muscle protein synthesis in older adults: a randomized controlled trial. Am J Clin Nutr 2011, 93:402.
    • (2011) Am J Clin Nutr , vol.93 , pp. 402
    • Smith, G.I.1    Atherton, P.2    Reeds, D.N.3
  • 36
    • 4644305200 scopus 로고    scopus 로고
    • Muscle-specific overexpression of CD36 reverses the insulin resistance and diabetes of MKR mice
    • Heron-Milhavet L., Haluzik M., Yakar S., et al. Muscle-specific overexpression of CD36 reverses the insulin resistance and diabetes of MKR mice. Endocrinology 2004, 145:4667.
    • (2004) Endocrinology , vol.145 , pp. 4667
    • Heron-Milhavet, L.1    Haluzik, M.2    Yakar, S.3
  • 37
    • 33846999679 scopus 로고    scopus 로고
    • Long-chain omega-3 fatty acids regulate bovine whole-body protein metabolism by promoting muscle insulin signalling to the Akt-mTOR-S6K1 pathway and insulin sensitivity
    • Gingras A.A., White P.J., Chouinard P.Y., et al. Long-chain omega-3 fatty acids regulate bovine whole-body protein metabolism by promoting muscle insulin signalling to the Akt-mTOR-S6K1 pathway and insulin sensitivity. J Physiol 2007, 579:269.
    • (2007) J Physiol , vol.579 , pp. 269
    • Gingras, A.A.1    White, P.J.2    Chouinard, P.Y.3
  • 38
    • 36749104407 scopus 로고    scopus 로고
    • Exercise- and nutrient-controlled mechanisms involved in maintenance of the musculoskeletal mass
    • Rennie M.J. Exercise- and nutrient-controlled mechanisms involved in maintenance of the musculoskeletal mass. Biochem Soc Trans 2007, 35:1302.
    • (2007) Biochem Soc Trans , vol.35 , pp. 1302
    • Rennie, M.J.1
  • 39
    • 32444439996 scopus 로고    scopus 로고
    • Skeletal muscle protein metabolism and resistance exercise
    • Wolfe R.R. Skeletal muscle protein metabolism and resistance exercise. J Nutr 2006, 136:525S.
    • (2006) J Nutr , vol.136
    • Wolfe, R.R.1
  • 40
    • 0033808169 scopus 로고    scopus 로고
    • Leucine stimulates translation initiation in skeletal muscle of postabsorptive rats via a rapamycin-sensitive pathway
    • Anthony J.C., Yoshizawa F., Anthony T.G., et al. Leucine stimulates translation initiation in skeletal muscle of postabsorptive rats via a rapamycin-sensitive pathway. J Nutr 2000, 130:2413.
    • (2000) J Nutr , vol.130 , pp. 2413
    • Anthony, J.C.1    Yoshizawa, F.2    Anthony, T.G.3
  • 41
    • 79954448763 scopus 로고    scopus 로고
    • Mechanisms of insulin secretion in malnutrition: modulation by amino acids in rodent models
    • de Oliveira C.A., Latorraca M.Q., de Mello M.A., et al. Mechanisms of insulin secretion in malnutrition: modulation by amino acids in rodent models. Amino Acids 2011, 40:1027.
    • (2011) Amino Acids , vol.40 , pp. 1027
    • de Oliveira, C.A.1    Latorraca, M.Q.2    de Mello, M.A.3
  • 42
    • 78649242199 scopus 로고    scopus 로고
    • Influence of supplementation with branched-chain amino acids in combination with resistance exercise on p70S6 kinase phosphorylation in resting and exercising human skeletal muscle
    • Apro W., Blomstrand E. Influence of supplementation with branched-chain amino acids in combination with resistance exercise on p70S6 kinase phosphorylation in resting and exercising human skeletal muscle. Acta Physiol (Oxf) 2010, 200:237.
    • (2010) Acta Physiol (Oxf) , vol.200 , pp. 237
    • Apro, W.1    Blomstrand, E.2
  • 43
    • 33644886769 scopus 로고    scopus 로고
    • Nutrients suppress phosphatidylinositol 3-kinase/Akt signaling via raptor-dependent mTOR-mediated insulin receptor substrate 1 phosphorylation
    • Tzatsos A., Kandror K.V. Nutrients suppress phosphatidylinositol 3-kinase/Akt signaling via raptor-dependent mTOR-mediated insulin receptor substrate 1 phosphorylation. Mol Cell Biol 2006, 26:63.
    • (2006) Mol Cell Biol , vol.26 , pp. 63
    • Tzatsos, A.1    Kandror, K.V.2
  • 44
    • 77956677109 scopus 로고    scopus 로고
    • A phosphatidylinositol 3-kinase/protein kinase B-independent activation of mammalian target of rapamycin signaling is sufficient to induce skeletal muscle hypertrophy
    • Goodman C.A., Miu M.H., Frey J.W., et al. A phosphatidylinositol 3-kinase/protein kinase B-independent activation of mammalian target of rapamycin signaling is sufficient to induce skeletal muscle hypertrophy. Mol Biol Cell 2010, 21:3258.
    • (2010) Mol Biol Cell , vol.21 , pp. 3258
    • Goodman, C.A.1    Miu, M.H.2    Frey, J.W.3
  • 45
    • 21244456553 scopus 로고    scopus 로고
    • Rheb binding to mammalian target of rapamycin (mTOR) is regulated by amino acid sufficiency
    • Long X., Ortiz-Vega S., Lin Y., et al. Rheb binding to mammalian target of rapamycin (mTOR) is regulated by amino acid sufficiency. J Biol Chem 2005, 280:23433.
    • (2005) J Biol Chem , vol.280 , pp. 23433
    • Long, X.1    Ortiz-Vega, S.2    Lin, Y.3
  • 46
    • 59049087460 scopus 로고    scopus 로고
    • Bidirectional transport of amino acids regulates mTOR and autophagy
    • Nicklin P., Bergman P., Zhang B., et al. Bidirectional transport of amino acids regulates mTOR and autophagy. Cell 2009, 136:521.
    • (2009) Cell , vol.136 , pp. 521
    • Nicklin, P.1    Bergman, P.2    Zhang, B.3
  • 47
    • 79955013712 scopus 로고    scopus 로고
    • Regulation of protein synthesis by amino acids in muscle of neonates
    • Suryawan A., Davis T.A. Regulation of protein synthesis by amino acids in muscle of neonates. Front Biosci 2011, 16:1445.
    • (2011) Front Biosci , vol.16 , pp. 1445
    • Suryawan, A.1    Davis, T.A.2
  • 48
    • 0028817036 scopus 로고
    • Leucine activates system A amino acid transport in L6 rat skeletal muscle cells
    • McDowell H.E., Christie G.R., Stenhouse G., et al. Leucine activates system A amino acid transport in L6 rat skeletal muscle cells. Am J Physiol 1995, 269:C1287.
    • (1995) Am J Physiol , vol.269
    • McDowell, H.E.1    Christie, G.R.2    Stenhouse, G.3
  • 50
    • 45849105156 scopus 로고    scopus 로고
    • The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1
    • Sancak Y., Peterson T.R., Shaul Y.D., et al. The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1. Science 2008, 320:1496.
    • (2008) Science , vol.320 , pp. 1496
    • Sancak, Y.1    Peterson, T.R.2    Shaul, Y.D.3
  • 51
    • 77951768486 scopus 로고    scopus 로고
    • Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids
    • Sancak Y., Bar-Peled L., Zoncu R., et al. Ragulator-Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 2010, 141:290.
    • (2010) Cell , vol.141 , pp. 290
    • Sancak, Y.1    Bar-Peled, L.2    Zoncu, R.3
  • 52
    • 80555143078 scopus 로고    scopus 로고
    • MTORC1 senses lysosomal amino acids through an insideout mechanism that requires the vacuolar H(+)-ATPase
    • Zoncu R., Bar-Peled L., Efeyan A., et al. mTORC1 senses lysosomal amino acids through an insideout mechanism that requires the vacuolar H(+)-ATPase. Science 2011, 334:678.
    • (2011) Science , vol.334 , pp. 678
    • Zoncu, R.1    Bar-Peled, L.2    Efeyan, A.3
  • 53
    • 0035912839 scopus 로고    scopus 로고
    • Identification and characterization of a lysosomal transporter for small neutral amino acids
    • Sagne C., Agulhon C., Ravassard P., et al. Identification and characterization of a lysosomal transporter for small neutral amino acids. Proc Natl Acad Sci U S A 2001, 98:7206.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 7206
    • Sagne, C.1    Agulhon, C.2    Ravassard, P.3
  • 54
    • 79952774855 scopus 로고    scopus 로고
    • Intracellular amino acid sensing and mTORC1-regulated growth: new ways to block an old target?
    • Goberdhan D.C. Intracellular amino acid sensing and mTORC1-regulated growth: new ways to block an old target?. Curr Opin Investig Drugs 2010, 11:1360.
    • (2010) Curr Opin Investig Drugs , vol.11 , pp. 1360
    • Goberdhan, D.C.1
  • 55
    • 77954757143 scopus 로고    scopus 로고
    • Proton-assisted amino-acid transporters are conserved regulators of proliferation and amino-acid-dependent mTORC1 activation
    • Heublein S., Kazi S., Ogmundsdottir M.H., et al. Proton-assisted amino-acid transporters are conserved regulators of proliferation and amino-acid-dependent mTORC1 activation. Oncogene 2010, 29:4068.
    • (2010) Oncogene , vol.29 , pp. 4068
    • Heublein, S.1    Kazi, S.2    Ogmundsdottir, M.H.3
  • 56
    • 36448968532 scopus 로고    scopus 로고
    • FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells
    • Zhao J., Brault J.J., Schild A., et al. FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab 2007, 6:472.
    • (2007) Cell Metab , vol.6 , pp. 472
    • Zhao, J.1    Brault, J.J.2    Schild, A.3
  • 57
    • 78651300628 scopus 로고    scopus 로고
    • Autophagic-lysosomal pathway functions in the masseter and tongue muscles in the klotho mouse, a mouse model for aging
    • Iida R.H., Kanko S., Suga T., et al. Autophagic-lysosomal pathway functions in the masseter and tongue muscles in the klotho mouse, a mouse model for aging. Mol Cell Biochem 2011, 348:89.
    • (2011) Mol Cell Biochem , vol.348 , pp. 89
    • Iida, R.H.1    Kanko, S.2    Suga, T.3
  • 58
    • 33644507693 scopus 로고    scopus 로고
    • Long-lived Klotho mice: new insights into the roles of IGF-1 and insulin in aging
    • Bartke A. Long-lived Klotho mice: new insights into the roles of IGF-1 and insulin in aging. Trends Endocrinol Metab 2006, 17:33.
    • (2006) Trends Endocrinol Metab , vol.17 , pp. 33
    • Bartke, A.1
  • 59
    • 77953699711 scopus 로고    scopus 로고
    • Termination of autophagy and reformation of lysosomes regulated by mTOR
    • Yu L., McPhee C.K., Zheng L., et al. Termination of autophagy and reformation of lysosomes regulated by mTOR. Nature 2010, 465:942.
    • (2010) Nature , vol.465 , pp. 942
    • Yu, L.1    McPhee, C.K.2    Zheng, L.3
  • 60
    • 84857997408 scopus 로고    scopus 로고
    • A lysosome-to-nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEB
    • Settembre C., Zoncu R., Medina D.L., et al. A lysosome-to-nucleus signalling mechanism senses and regulates the lysosome via mTOR and TFEB. EMBO J 2012, 31:1095.
    • (2012) EMBO J , vol.31 , pp. 1095
    • Settembre, C.1    Zoncu, R.2    Medina, D.L.3
  • 61
    • 79953307234 scopus 로고    scopus 로고
    • Rac1 regulates the activity of mTORC1 and mTORC2 and controls cellular size
    • Saci A., Cantley L.C., Carpenter C.L. Rac1 regulates the activity of mTORC1 and mTORC2 and controls cellular size. Mol Cell 2011, 42:50.
    • (2011) Mol Cell , vol.42 , pp. 50
    • Saci, A.1    Cantley, L.C.2    Carpenter, C.L.3
  • 62
    • 77957567397 scopus 로고    scopus 로고
    • Downregulation of AMPK accompanies leucine- and glucose-induced increases in protein synthesis and insulin resistance in rat skeletal muscle
    • Saha A.K., Xu X.J., Lawson E., et al. Downregulation of AMPK accompanies leucine- and glucose-induced increases in protein synthesis and insulin resistance in rat skeletal muscle. Diabetes 2010, 59:2426.
    • (2010) Diabetes , vol.59 , pp. 2426
    • Saha, A.K.1    Xu, X.J.2    Lawson, E.3
  • 63
    • 33748153690 scopus 로고    scopus 로고
    • TSC2 integrates Wnt and energy signals via a coordinated phosphorylation by AMPK and GSK3 to regulate cell growth
    • Inoki K., Ouyang H., Zhu T., et al. TSC2 integrates Wnt and energy signals via a coordinated phosphorylation by AMPK and GSK3 to regulate cell growth. Cell 2006, 126:955.
    • (2006) Cell , vol.126 , pp. 955
    • Inoki, K.1    Ouyang, H.2    Zhu, T.3
  • 64
    • 13444252523 scopus 로고    scopus 로고
    • Recent advances in the regulation of the TOR pathway by insulin and nutrients
    • Avruch J., Lin Y., Long X., et al. Recent advances in the regulation of the TOR pathway by insulin and nutrients. Curr Opin Clin Nutr Metab Care 2005, 8:67.
    • (2005) Curr Opin Clin Nutr Metab Care , vol.8 , pp. 67
    • Avruch, J.1    Lin, Y.2    Long, X.3
  • 65
    • 79952281400 scopus 로고    scopus 로고
    • Inactivation of Rheb by PRAK-mediated phosphorylation is essential for energy-depletion-induced suppression of mTORC1
    • Zheng M., Wang Y.H., Wu X.N., et al. Inactivation of Rheb by PRAK-mediated phosphorylation is essential for energy-depletion-induced suppression of mTORC1. Nat Cell Biol 2011, 13:263.
    • (2011) Nat Cell Biol , vol.13 , pp. 263
    • Zheng, M.1    Wang, Y.H.2    Wu, X.N.3
  • 66
    • 77951213258 scopus 로고    scopus 로고
    • Insulin like growth factor-1-induced phosphorylation and altered distribution of tuberous sclerosis complex (TSC)1/TSC2 in C2C12 myotubes
    • Miyazaki M., McCarthy J.J., Esser K.A. Insulin like growth factor-1-induced phosphorylation and altered distribution of tuberous sclerosis complex (TSC)1/TSC2 in C2C12 myotubes. FEBS J 2010, 277:2180.
    • (2010) FEBS J , vol.277 , pp. 2180
    • Miyazaki, M.1    McCarthy, J.J.2    Esser, K.A.3
  • 67
    • 33749366334 scopus 로고    scopus 로고
    • Muscle atrophy in transgenic mice expressing a human TSC1 transgene
    • Wan M., Wu X., Guan K.L., et al. Muscle atrophy in transgenic mice expressing a human TSC1 transgene. FEBS Lett 2006, 580:5621.
    • (2006) FEBS Lett , vol.580 , pp. 5621
    • Wan, M.1    Wu, X.2    Guan, K.L.3
  • 68
    • 33750155593 scopus 로고    scopus 로고
    • Insulin and amino-acid regulation of mTOR signaling and kinase activity through the Rheb GTPase
    • Avruch J., Hara K., Lin Y., et al. Insulin and amino-acid regulation of mTOR signaling and kinase activity through the Rheb GTPase. Oncogene 2006, 25:6361.
    • (2006) Oncogene , vol.25 , pp. 6361
    • Avruch, J.1    Hara, K.2    Lin, Y.3
  • 69
    • 80051637832 scopus 로고    scopus 로고
    • MTORC1 signaling: what we still don't know
    • Wang X., Proud C.G. mTORC1 signaling: what we still don't know. J Mol Cell Biol 2011, 3(4):206-220.
    • (2011) J Mol Cell Biol , vol.3 , Issue.4 , pp. 206-220
    • Wang, X.1    Proud, C.G.2
  • 70
    • 46149098447 scopus 로고    scopus 로고
    • Phospholipase D1 is an effector of Rheb in the mTOR pathway
    • Sun Y., Fang Y., Yoon M.S., et al. Phospholipase D1 is an effector of Rheb in the mTOR pathway. Proc Natl Acad Sci U S A 2008, 105:8286.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 8286
    • Sun, Y.1    Fang, Y.2    Yoon, M.S.3
  • 71
    • 84863115883 scopus 로고    scopus 로고
    • Glycerolipid signals alter mTOR complex 2 (mTORC2) to diminish insulin signaling
    • Zhang C., Wendel A.A., Keogh M.R., et al. Glycerolipid signals alter mTOR complex 2 (mTORC2) to diminish insulin signaling. Proc Natl Acad Sci U S A 2012, 109:1667.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 1667
    • Zhang, C.1    Wendel, A.A.2    Keogh, M.R.3
  • 72
    • 78649348967 scopus 로고    scopus 로고
    • Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress
    • Sengupta S., Peterson T.R., Sabatini D.M. Regulation of the mTOR complex 1 pathway by nutrients, growth factors, and stress. Mol Cell 2010, 40:310.
    • (2010) Mol Cell , vol.40 , pp. 310
    • Sengupta, S.1    Peterson, T.R.2    Sabatini, D.M.3
  • 73
    • 0035976615 scopus 로고    scopus 로고
    • Phosphatidic acid-mediated mitogenic activation of mTOR signaling
    • Fang Y., Vilella-Bach M., Bachmann R., et al. Phosphatidic acid-mediated mitogenic activation of mTOR signaling. Science 2001, 294:1942.
    • (2001) Science , vol.294 , pp. 1942
    • Fang, Y.1    Vilella-Bach, M.2    Bachmann, R.3
  • 74
    • 67649823420 scopus 로고    scopus 로고
    • Specific activation of mTORC1 by Rheb G-protein in vitro involves enhanced recruitment of its substrate protein
    • Sato T., Nakashima A., Guo L., et al. Specific activation of mTORC1 by Rheb G-protein in vitro involves enhanced recruitment of its substrate protein. J Biol Chem 2009, 284:12783.
    • (2009) J Biol Chem , vol.284 , pp. 12783
    • Sato, T.1    Nakashima, A.2    Guo, L.3
  • 75
    • 62849111751 scopus 로고    scopus 로고
    • Regulation of mTORC1 and mTORC2 complex assembly by phosphatidic acid: competition with rapamycin
    • Toschi A., Lee E., Xu L., et al. Regulation of mTORC1 and mTORC2 complex assembly by phosphatidic acid: competition with rapamycin. Mol Cell Biol 2009, 29:1411.
    • (2009) Mol Cell Biol , vol.29 , pp. 1411
    • Toschi, A.1    Lee, E.2    Xu, L.3
  • 76
    • 79953140160 scopus 로고    scopus 로고
    • Mechanisms involved in the coordinate regulation of the mammalian target of rapamycin complex 1 (mTORC1) by insulin and amino acids
    • Dennis M.D., Baum J.I., Kimball S.R., et al. Mechanisms involved in the coordinate regulation of the mammalian target of rapamycin complex 1 (mTORC1) by insulin and amino acids. J Biol Chem 2011, 286(10):8287-8296.
    • (2011) J Biol Chem , vol.286 , Issue.10 , pp. 8287-8296
    • Dennis, M.D.1    Baum, J.I.2    Kimball, S.R.3
  • 77
    • 46549084953 scopus 로고    scopus 로고
    • Amino acids are necessary for the insulin-induced activation of mTOR/S6K1 signaling and protein synthesis in healthy and insulin resistant human skeletal muscle
    • Drummond M.J., Bell J.A., Fujita S., et al. Amino acids are necessary for the insulin-induced activation of mTOR/S6K1 signaling and protein synthesis in healthy and insulin resistant human skeletal muscle. Clin Nutr 2008, 27:447.
    • (2008) Clin Nutr , vol.27 , pp. 447
    • Drummond, M.J.1    Bell, J.A.2    Fujita, S.3
  • 78
    • 0034880429 scopus 로고    scopus 로고
    • Timing of amino acid-carbohydrate ingestion alters anabolic response of muscle to resistance exercise
    • Tipton K.D., Rasmussen B.B., Miller S.L., et al. Timing of amino acid-carbohydrate ingestion alters anabolic response of muscle to resistance exercise. Am J Physiol Endocrinol Metab 2001, 281:E197.
    • (2001) Am J Physiol Endocrinol Metab , vol.281
    • Tipton, K.D.1    Rasmussen, B.B.2    Miller, S.L.3
  • 79
    • 0035895766 scopus 로고    scopus 로고
    • Insulin-like growth factor-I stimulates amino acid transport in a glutamine-deprived human neuroblastoma cell line
    • Wasa M., Wang H.S., Tazuke Y., et al. Insulin-like growth factor-I stimulates amino acid transport in a glutamine-deprived human neuroblastoma cell line. Biochim Biophys Acta 2001, 1525:118.
    • (2001) Biochim Biophys Acta , vol.1525 , pp. 118
    • Wasa, M.1    Wang, H.S.2    Tazuke, Y.3
  • 80
    • 0028807373 scopus 로고
    • Insulin and insulin-like growth factor-I enhance human skeletal muscle protein anabolism during hyperaminoacidemia by different mechanisms
    • Fryburg D.A., Jahn L.A., Hill S.A., et al. Insulin and insulin-like growth factor-I enhance human skeletal muscle protein anabolism during hyperaminoacidemia by different mechanisms. J Clin Invest 1995, 96:1722.
    • (1995) J Clin Invest , vol.96 , pp. 1722
    • Fryburg, D.A.1    Jahn, L.A.2    Hill, S.A.3
  • 81
    • 0026670049 scopus 로고
    • Effects of prior exercise on the action of insulin-like growth factor I in skeletal muscle
    • Henriksen E.J., Louters L.L., Stump C.S., et al. Effects of prior exercise on the action of insulin-like growth factor I in skeletal muscle. Am J Physiol 1992, 263:E340.
    • (1992) Am J Physiol , vol.263
    • Henriksen, E.J.1    Louters, L.L.2    Stump, C.S.3
  • 82
    • 45549083411 scopus 로고    scopus 로고
    • Effect of acute physiological hyperinsulinemia on gene expression in human skeletal muscle in vivo
    • Coletta D.K., Balas B., Chavez A.O., et al. Effect of acute physiological hyperinsulinemia on gene expression in human skeletal muscle in vivo. Am J Physiol Endocrinol Metab 2008, 294:E910.
    • (2008) Am J Physiol Endocrinol Metab , vol.294
    • Coletta, D.K.1    Balas, B.2    Chavez, A.O.3
  • 83
    • 77957725489 scopus 로고    scopus 로고
    • JunB transcription factor maintains skeletal muscle mass and promotes hypertrophy
    • Raffaello A., Milan G., Masiero E., et al. JunB transcription factor maintains skeletal muscle mass and promotes hypertrophy. J Cell Biol 2010, 191:101.
    • (2010) J Cell Biol , vol.191 , pp. 101
    • Raffaello, A.1    Milan, G.2    Masiero, E.3
  • 84
    • 34147191715 scopus 로고    scopus 로고
    • STAT3 signaling is activated in human skeletal muscle following acute resistance exercise
    • Trenerry M.K., Carey K.A., Ward A.C., et al. STAT3 signaling is activated in human skeletal muscle following acute resistance exercise. J Appl Physiol 2007, 102:1483.
    • (2007) J Appl Physiol , vol.102 , pp. 1483
    • Trenerry, M.K.1    Carey, K.A.2    Ward, A.C.3
  • 85
    • 33846332013 scopus 로고    scopus 로고
    • Regulation of myostatin expression and myoblast differentiation by FoxO and SMAD transcription factors
    • Allen D.L., Unterman T.G. Regulation of myostatin expression and myoblast differentiation by FoxO and SMAD transcription factors. Am J Physiol Cell Physiol 2007, 292:C188.
    • (2007) Am J Physiol Cell Physiol , vol.292
    • Allen, D.L.1    Unterman, T.G.2
  • 86
    • 0031856578 scopus 로고    scopus 로고
    • Increased protein synthesis after acute IGF-I or insulin infusion is localized to muscle in mice
    • Bark T.H., McNurlan M.A., Lang C.H., et al. Increased protein synthesis after acute IGF-I or insulin infusion is localized to muscle in mice. Am J Physiol 1998, 275:E118.
    • (1998) Am J Physiol , vol.275
    • Bark, T.H.1    McNurlan, M.A.2    Lang, C.H.3
  • 87
    • 77955415069 scopus 로고    scopus 로고
    • Brief, high intensity exercise alters serum ghrelin and growth hormone concentrations but not IGF-I, IGF-II or IGF-I bioactivity
    • Stokes K.A., Sykes D., Gilbert K.L., et al. Brief, high intensity exercise alters serum ghrelin and growth hormone concentrations but not IGF-I, IGF-II or IGF-I bioactivity. Growth Horm IGF Res 2010, 20:289.
    • (2010) Growth Horm IGF Res , vol.20 , pp. 289
    • Stokes, K.A.1    Sykes, D.2    Gilbert, K.L.3
  • 88
    • 73449139411 scopus 로고    scopus 로고
    • Insulin-like growth factor I as a biomarker of health, fitness, and training status
    • Nindl B.C., Pierce J.R. Insulin-like growth factor I as a biomarker of health, fitness, and training status. Med Sci Sports Exerc 2010, 42:39.
    • (2010) Med Sci Sports Exerc , vol.42 , pp. 39
    • Nindl, B.C.1    Pierce, J.R.2
  • 89
    • 33846858634 scopus 로고    scopus 로고
    • Short-term strength training and the expression of myostatin and IGF-I isoforms in rat muscle and tendon: differential effects of specific contraction types
    • Heinemeier K.M., Olesen J.L., Schjerling P., et al. Short-term strength training and the expression of myostatin and IGF-I isoforms in rat muscle and tendon: differential effects of specific contraction types. J Appl Physiol 2007, 102:573.
    • (2007) J Appl Physiol , vol.102 , pp. 573
    • Heinemeier, K.M.1    Olesen, J.L.2    Schjerling, P.3
  • 90
    • 77956587382 scopus 로고    scopus 로고
    • Exercise and fasting activate growth hormone-dependent myocellular signal transducer and activator of transcription-5b phosphorylation and insulin-like growth factor-I messenger ribonucleic acid expression in humans
    • Vendelbo M.H., Jorgensen J.O., Pedersen S.B., et al. Exercise and fasting activate growth hormone-dependent myocellular signal transducer and activator of transcription-5b phosphorylation and insulin-like growth factor-I messenger ribonucleic acid expression in humans. J Clin Endocrinol Metab 2010, 95:E64.
    • (2010) J Clin Endocrinol Metab , vol.95
    • Vendelbo, M.H.1    Jorgensen, J.O.2    Pedersen, S.B.3
  • 91
    • 35549001418 scopus 로고    scopus 로고
    • Interstitial IGF-I in exercising skeletal muscle in women
    • Berg U., Gustafsson T., Sundberg C.J., et al. Interstitial IGF-I in exercising skeletal muscle in women. Eur J Endocrinol 2007, 157:427.
    • (2007) Eur J Endocrinol , vol.157 , pp. 427
    • Berg, U.1    Gustafsson, T.2    Sundberg, C.J.3
  • 92
    • 0034987615 scopus 로고    scopus 로고
    • Immunization against IGF-I prevents increases in protein synthesis in diabetic rats after resistance exercise
    • Fedele M.J., Lang C.H., Farrell P.A. Immunization against IGF-I prevents increases in protein synthesis in diabetic rats after resistance exercise. Am J Physiol Endocrinol Metab 2001, 280:E877.
    • (2001) Am J Physiol Endocrinol Metab , vol.280
    • Fedele, M.J.1    Lang, C.H.2    Farrell, P.A.3
  • 93
    • 37749027195 scopus 로고    scopus 로고
    • A functional insulin-like growth factor receptor is not necessary for load-induced skeletal muscle hypertrophy
    • Spangenburg E.E., Le Roith D., Ward C.W., et al. A functional insulin-like growth factor receptor is not necessary for load-induced skeletal muscle hypertrophy. J Physiol 2008, 586:283.
    • (2008) J Physiol , vol.586 , pp. 283
    • Spangenburg, E.E.1    Le Roith, D.2    Ward, C.W.3
  • 94
    • 77951945432 scopus 로고    scopus 로고
    • The insulin-like growth factor (IGF)-I E-peptides are required for isoform-specific gene expression and muscle hypertrophy after local IGF-I production
    • Barton E.R., DeMeo J., Lei H. The insulin-like growth factor (IGF)-I E-peptides are required for isoform-specific gene expression and muscle hypertrophy after local IGF-I production. J Appl Physiol 2010, 108:1069.
    • (2010) J Appl Physiol , vol.108 , pp. 1069
    • Barton, E.R.1    DeMeo, J.2    Lei, H.3
  • 95
    • 10644253597 scopus 로고    scopus 로고
    • Intracellular signaling specificity in response to uniaxial vs. multiaxial stretch: implications for mechanotransduction
    • Hornberger T.A., Armstrong D.D., Koh T.J., et al. Intracellular signaling specificity in response to uniaxial vs. multiaxial stretch: implications for mechanotransduction. Am J Physiol Cell Physiol 2005, 288:C185.
    • (2005) Am J Physiol Cell Physiol , vol.288
    • Hornberger, T.A.1    Armstrong, D.D.2    Koh, T.J.3
  • 96
    • 77955092459 scopus 로고    scopus 로고
    • Human exercise-mediated skeletal muscle hypertrophy is an intrinsic process
    • West D.W., Burd N.A., Staples A.W., et al. Human exercise-mediated skeletal muscle hypertrophy is an intrinsic process. Int J Biochem Cell Biol 2010, 42:1371.
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 1371
    • West, D.W.1    Burd, N.A.2    Staples, A.W.3
  • 97
    • 77953695333 scopus 로고    scopus 로고
    • High-frequency electrically stimulated skeletal muscle contractions increase p70s6k phosphorylation independent of known IGF-I sensitive signaling pathways
    • Witkowski S., Lovering R.M., Spangenburg E.E. High-frequency electrically stimulated skeletal muscle contractions increase p70s6k phosphorylation independent of known IGF-I sensitive signaling pathways. FEBS Lett 2010, 584:2891.
    • (2010) FEBS Lett , vol.584 , pp. 2891
    • Witkowski, S.1    Lovering, R.M.2    Spangenburg, E.E.3
  • 98
    • 77958042717 scopus 로고    scopus 로고
    • MKR mice have increased dynamic glucose disposal despite metabolic inflexibility, and hepatic and peripheral insulin insensitivity
    • Vaitheesvaran B., LeRoith D., Kurland I.J. MKR mice have increased dynamic glucose disposal despite metabolic inflexibility, and hepatic and peripheral insulin insensitivity. Diabetologia 2010, 53:2224.
    • (2010) Diabetologia , vol.53 , pp. 2224
    • Vaitheesvaran, B.1    LeRoith, D.2    Kurland, I.J.3
  • 99
    • 0036170286 scopus 로고    scopus 로고
    • Muscle-specific inactivation of the IGF-I receptor induces compensatory hyperplasia in skeletal muscle
    • Fernandez A.M., Dupont J., Farrar R.P., et al. Muscle-specific inactivation of the IGF-I receptor induces compensatory hyperplasia in skeletal muscle. J Clin Invest 2002, 109:347.
    • (2002) J Clin Invest , vol.109 , pp. 347
    • Fernandez, A.M.1    Dupont, J.2    Farrar, R.P.3
  • 100
    • 78650810413 scopus 로고    scopus 로고
    • The role of GH and IGF-I in mediating anabolic effects of testosterone on androgen-responsive muscle
    • Serra C., Bhasin S., Tangherlini F., et al. The role of GH and IGF-I in mediating anabolic effects of testosterone on androgen-responsive muscle. Endocrinology 2011, 152:193.
    • (2011) Endocrinology , vol.152 , pp. 193
    • Serra, C.1    Bhasin, S.2    Tangherlini, F.3
  • 101
    • 83455215759 scopus 로고    scopus 로고
    • Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models
    • Schiaffino S., Mammucari C. Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models. Skelet Muscle 2011, 1:4.
    • (2011) Skelet Muscle , vol.1 , pp. 4
    • Schiaffino, S.1    Mammucari, C.2
  • 102
    • 79151474979 scopus 로고    scopus 로고
    • Tyrosine kinase-independent activation of extracellular-regulated kinase (ERK) 1/2 by the insulin-like growth factor-1 receptor
    • Perrault R., Wright B., Storie B., et al. Tyrosine kinase-independent activation of extracellular-regulated kinase (ERK) 1/2 by the insulin-like growth factor-1 receptor. Cell Signal 2011, 23(4):739-746.
    • (2011) Cell Signal , vol.23 , Issue.4 , pp. 739-746
    • Perrault, R.1    Wright, B.2    Storie, B.3
  • 103
    • 69949177417 scopus 로고    scopus 로고
    • The direct binding of insulin-like growth factor-1 (IGF-1) to integrin alphavbeta3 is involved in IGF-1 signaling
    • Saegusa J., Yamaji S., Ieguchi K., et al. The direct binding of insulin-like growth factor-1 (IGF-1) to integrin alphavbeta3 is involved in IGF-1 signaling. J Biol Chem 2009, 284:24106.
    • (2009) J Biol Chem , vol.284 , pp. 24106
    • Saegusa, J.1    Yamaji, S.2    Ieguchi, K.3
  • 104
    • 77955900453 scopus 로고    scopus 로고
    • Phosphatidic acid mediates activation of mTORC1 through the ERK signaling pathway
    • Winter J.N., Fox T.E., Kester M., et al. Phosphatidic acid mediates activation of mTORC1 through the ERK signaling pathway. Am J Physiol Cell Physiol 2010, 299:C335.
    • (2010) Am J Physiol Cell Physiol , vol.299
    • Winter, J.N.1    Fox, T.E.2    Kester, M.3
  • 105
    • 0030833040 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase-1 and -2 respond differently to mitogenic and differentiative signaling pathways in myoblasts
    • Sarbassov D.D., Jones L.G., Peterson C.A. Extracellular signal-regulated kinase-1 and -2 respond differently to mitogenic and differentiative signaling pathways in myoblasts. Mol Endocrinol 1997, 11:2038.
    • (1997) Mol Endocrinol , vol.11 , pp. 2038
    • Sarbassov, D.D.1    Jones, L.G.2    Peterson, C.A.3
  • 106
    • 0035979253 scopus 로고    scopus 로고
    • Regulation of myostatin activity and muscle growth
    • Lee S.J., McPherron A.C. Regulation of myostatin activity and muscle growth. Proc Natl Acad Sci U S A 2001, 98:9306.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 9306
    • Lee, S.J.1    McPherron, A.C.2
  • 107
    • 84455185170 scopus 로고    scopus 로고
    • The type 1 insulin-like growth factor receptor (IGF-IR) pathway is mandatory for the follistatin-induced skeletal muscle hypertrophy
    • Kalista S., Schakman O., Gilson H., et al. The type 1 insulin-like growth factor receptor (IGF-IR) pathway is mandatory for the follistatin-induced skeletal muscle hypertrophy. Endocrinology 2012, 153:241.
    • (2012) Endocrinology , vol.153 , pp. 241
    • Kalista, S.1    Schakman, O.2    Gilson, H.3
  • 108
    • 67650071006 scopus 로고    scopus 로고
    • Follistatin induces muscle hypertrophy through satellite cell proliferation and inhibition of both myostatin and activin
    • Gilson H., Schakman O., Kalista S., et al. Follistatin induces muscle hypertrophy through satellite cell proliferation and inhibition of both myostatin and activin. Am J Physiol Endocrinol Metab 2009, 297:E157.
    • (2009) Am J Physiol Endocrinol Metab , vol.297
    • Gilson, H.1    Schakman, O.2    Kalista, S.3
  • 109
    • 84857737461 scopus 로고    scopus 로고
    • Is functional hypertrophy and specific force coupled with the addition of myonuclei at the single muscle fiber level?
    • Qaisar R., Renaud G., Morine K., et al. Is functional hypertrophy and specific force coupled with the addition of myonuclei at the single muscle fiber level?. FASEB J 2012, 26:1077.
    • (2012) FASEB J , vol.26 , pp. 1077
    • Qaisar, R.1    Renaud, G.2    Morine, K.3
  • 110
    • 77749260832 scopus 로고    scopus 로고
    • Follistatin gene delivery enhances muscle growth and strength in nonhuman primates
    • Kota J., Handy C.R., Haidet A.M., et al. Follistatin gene delivery enhances muscle growth and strength in nonhuman primates. Sci Transl Med 2009, 1:6ra15.
    • (2009) Sci Transl Med , vol.1
    • Kota, J.1    Handy, C.R.2    Haidet, A.M.3
  • 111
    • 80053272231 scopus 로고    scopus 로고
    • Recent progress toward understanding the molecular mechanisms that regulate skeletal muscle mass
    • Goodman C.A., Mayhew D.L., Hornberger T.A. Recent progress toward understanding the molecular mechanisms that regulate skeletal muscle mass. Cell Signal 2011, 23:1896.
    • (2011) Cell Signal , vol.23 , pp. 1896
    • Goodman, C.A.1    Mayhew, D.L.2    Hornberger, T.A.3
  • 112
    • 77953162950 scopus 로고    scopus 로고
    • Point: Counterpoint: IGF is/is not the major physiological regulator of muscle mass. Point: IGF is the major physiological regulator of muscle mass
    • Stewart C.E., Pell J.M. Point: Counterpoint: IGF is/is not the major physiological regulator of muscle mass. Point: IGF is the major physiological regulator of muscle mass. J Appl Physiol 2010, 108:1820.
    • (2010) J Appl Physiol , vol.108 , pp. 1820
    • Stewart, C.E.1    Pell, J.M.2
  • 113
    • 37349131288 scopus 로고    scopus 로고
    • Insulin-like growth factor-I receptor, E-cadherin and alpha v integrin form a dynamic complex under the control of alpha-catenin
    • Canonici A., Steelant W., Rigot V., et al. Insulin-like growth factor-I receptor, E-cadherin and alpha v integrin form a dynamic complex under the control of alpha-catenin. Int J Cancer 2008, 122:572.
    • (2008) Int J Cancer , vol.122 , pp. 572
    • Canonici, A.1    Steelant, W.2    Rigot, V.3
  • 114
    • 31444448603 scopus 로고    scopus 로고
    • Insulin-like growth factor-I signaling in smooth muscle cells is regulated by ligand binding to the 177CYDMKTTC184 sequence of the beta3-subunit of alphaVbeta3
    • Maile L.A., Busby W.H., Sitko K., et al. Insulin-like growth factor-I signaling in smooth muscle cells is regulated by ligand binding to the 177CYDMKTTC184 sequence of the beta3-subunit of alphaVbeta3. Mol Endocrinol 2006, 20:405.
    • (2006) Mol Endocrinol , vol.20 , pp. 405
    • Maile, L.A.1    Busby, W.H.2    Sitko, K.3
  • 115
    • 52449131366 scopus 로고    scopus 로고
    • Integrin alphavbeta3 acts downstream of insulin in normalization of interstitial fluid pressure in sepsis and in cell-mediated collagen gel contraction
    • Svendsen O.S., Liden A., Nedrebo T., et al. Integrin alphavbeta3 acts downstream of insulin in normalization of interstitial fluid pressure in sepsis and in cell-mediated collagen gel contraction. Am J Physiol Heart Circ Physiol 2008, 295:H555.
    • (2008) Am J Physiol Heart Circ Physiol , vol.295
    • Svendsen, O.S.1    Liden, A.2    Nedrebo, T.3
  • 116
    • 48749118716 scopus 로고    scopus 로고
    • Alpha v beta 3 and alpha v beta 5 integrins and their role in muscle precursor cell adhesion
    • Sinanan A.C., Machell J.R., Wynne-Hughes G.T., et al. Alpha v beta 3 and alpha v beta 5 integrins and their role in muscle precursor cell adhesion. Biol Cell 2008, 100:465.
    • (2008) Biol Cell , vol.100 , pp. 465
    • Sinanan, A.C.1    Machell, J.R.2    Wynne-Hughes, G.T.3
  • 117
    • 77950629143 scopus 로고    scopus 로고
    • IGF-1 increases macrophage motility via PKC/p38- dependent alphavbeta3-integrin inside-out signaling
    • Furundzija V., Fritzsche J., Kaufmann J., et al. IGF-1 increases macrophage motility via PKC/p38- dependent alphavbeta3-integrin inside-out signaling. Biochem Biophys Res Commun 2010, 394:786.
    • (2010) Biochem Biophys Res Commun , vol.394 , pp. 786
    • Furundzija, V.1    Fritzsche, J.2    Kaufmann, J.3
  • 118
    • 67651147931 scopus 로고    scopus 로고
    • Focal adhesion kinase (FAK) activates and stabilizes IGF-1 receptor
    • Andersson S., D'Arcy P., Larsson O., et al. Focal adhesion kinase (FAK) activates and stabilizes IGF-1 receptor. Biochem Biophys Res Commun 2009, 387:36.
    • (2009) Biochem Biophys Res Commun , vol.387 , pp. 36
    • Andersson, S.1    D'Arcy, P.2    Larsson, O.3
  • 119
    • 69249217669 scopus 로고    scopus 로고
    • Targeting of the protein interaction site between FAK and IGF-1R
    • Zheng D., Kurenova E., Ucar D., et al. Targeting of the protein interaction site between FAK and IGF-1R. Biochem Biophys Res Commun 2009, 388:301.
    • (2009) Biochem Biophys Res Commun , vol.388 , pp. 301
    • Zheng, D.1    Kurenova, E.2    Ucar, D.3
  • 120
    • 77951169963 scopus 로고    scopus 로고
    • A growth stimulus is needed for IGF-1 to induce skeletal muscle hypertrophy in vivo
    • Shavlakadze T., Chai J., Maley K., et al. A growth stimulus is needed for IGF-1 to induce skeletal muscle hypertrophy in vivo. J Cell Sci 2010, 123:960.
    • (2010) J Cell Sci , vol.123 , pp. 960
    • Shavlakadze, T.1    Chai, J.2    Maley, K.3
  • 121
    • 77149130495 scopus 로고    scopus 로고
    • Minireview: Mechano-growth factor: a putative product of IGF-I gene expression involved in tissue repair and regeneration
    • Matheny R.W., Nindl B.C., Adamo M.L. Minireview: Mechano-growth factor: a putative product of IGF-I gene expression involved in tissue repair and regeneration. Endocrinology 2010, 151:865.
    • (2010) Endocrinology , vol.151 , pp. 865
    • Matheny, R.W.1    Nindl, B.C.2    Adamo, M.L.3
  • 122
    • 33845649334 scopus 로고    scopus 로고
    • The protective role of exercise on stress system dysregulation and comorbidities
    • Tsatsoulis A., Fountoulakis S. The protective role of exercise on stress system dysregulation and comorbidities. Ann N Y Acad Sci 2006, 1083:196.
    • (2006) Ann N Y Acad Sci , vol.1083 , pp. 196
    • Tsatsoulis, A.1    Fountoulakis, S.2
  • 123
    • 18144370762 scopus 로고    scopus 로고
    • Effect of resistance exercise on skeletal muscle myopathy in heart transplant recipients
    • Braith R.W., Magyari P.M., Pierce G.L., et al. Effect of resistance exercise on skeletal muscle myopathy in heart transplant recipients. Am J Cardiol 2005, 95:1192.
    • (2005) Am J Cardiol , vol.95 , pp. 1192
    • Braith, R.W.1    Magyari, P.M.2    Pierce, G.L.3
  • 124
    • 77954581146 scopus 로고    scopus 로고
    • Nutritional recommendations for the management of sarcopenia
    • Morley J.E., Argiles J.M., Evans W.J., et al. Nutritional recommendations for the management of sarcopenia. J Am Med Dir Assoc 2010, 11:391.
    • (2010) J Am Med Dir Assoc , vol.11 , pp. 391
    • Morley, J.E.1    Argiles, J.M.2    Evans, W.J.3
  • 125
    • 77952485613 scopus 로고    scopus 로고
    • Ketogenic diet slows down mitochondrial myopathy progression in mice
    • Ahola-Erkkila S., Carroll C.J., Peltola-Mjosund K., et al. Ketogenic diet slows down mitochondrial myopathy progression in mice. Hum Mol Genet 2010, 19:1974.
    • (2010) Hum Mol Genet , vol.19 , pp. 1974
    • Ahola-Erkkila, S.1    Carroll, C.J.2    Peltola-Mjosund, K.3
  • 126
    • 46049113358 scopus 로고    scopus 로고
    • New strategies to overcome cancer cachexia: from molecular mechanisms to the 'Parallel Pathway'
    • Muscaritoli M., Costelli P., Aversa Z., et al. New strategies to overcome cancer cachexia: from molecular mechanisms to the 'Parallel Pathway'. Asia Pac J Clin Nutr 2008, 17(Suppl 1):387.
    • (2008) Asia Pac J Clin Nutr , vol.17 , Issue.SUPPL. 1 , pp. 387
    • Muscaritoli, M.1    Costelli, P.2    Aversa, Z.3
  • 127
    • 33746622168 scopus 로고    scopus 로고
    • Regulation of mTOR by mechanically induced signaling events in skeletal muscle
    • Hornberger T.A., Sukhija K.B., Chien S. Regulation of mTOR by mechanically induced signaling events in skeletal muscle. Cell Cycle 2006, 5:1391.
    • (2006) Cell Cycle , vol.5 , pp. 1391
    • Hornberger, T.A.1    Sukhija, K.B.2    Chien, S.3
  • 128
    • 77953745513 scopus 로고    scopus 로고
    • Molecular mechanisms in aging and current strategies to counteract sarcopenia
    • Sakuma K., Yamaguchi A. Molecular mechanisms in aging and current strategies to counteract sarcopenia. Curr Aging Sci 2010, 3:90.
    • (2010) Curr Aging Sci , vol.3 , pp. 90
    • Sakuma, K.1    Yamaguchi, A.2
  • 129
    • 33846007729 scopus 로고    scopus 로고
    • Dexamethasone represses signaling through the mammalian target of rapamycin in muscle cells by enhancing expression of REDD1
    • Wang H., Kubica N., Ellisen L.W., et al. Dexamethasone represses signaling through the mammalian target of rapamycin in muscle cells by enhancing expression of REDD1. J Biol Chem 2006, 281:39128.
    • (2006) J Biol Chem , vol.281 , pp. 39128
    • Wang, H.1    Kubica, N.2    Ellisen, L.W.3
  • 130
    • 15444362044 scopus 로고    scopus 로고
    • The stress-inducted proteins RTP801 and RTP801L are negative regulators of the mammalian target of rapamycin pathway
    • Corradetti M.N., Inoki K., Guan K.L. The stress-inducted proteins RTP801 and RTP801L are negative regulators of the mammalian target of rapamycin pathway. J Biol Chem 2005, 280:9769.
    • (2005) J Biol Chem , vol.280 , pp. 9769
    • Corradetti, M.N.1    Inoki, K.2    Guan, K.L.3
  • 131
    • 38349056675 scopus 로고    scopus 로고
    • Hypoxia regulates TSC1/2-mTOR signaling and tumor suppression through REDD1-mediated 14-3-3 shuttling
    • DeYoung M.P., Horak P., Sofer A., et al. Hypoxia regulates TSC1/2-mTOR signaling and tumor suppression through REDD1-mediated 14-3-3 shuttling. Genes Dev 2008, 22:239.
    • (2008) Genes Dev , vol.22 , pp. 239
    • DeYoung, M.P.1    Horak, P.2    Sofer, A.3
  • 132
    • 65349086122 scopus 로고    scopus 로고
    • Elevated corticosterone associated with food deprivation upregulates expression in rat skeletal muscle of the mTORC1 repressor, REDD1
    • McGhee N.K., Jefferson L.S., Kimball S.R. Elevated corticosterone associated with food deprivation upregulates expression in rat skeletal muscle of the mTORC1 repressor, REDD1. J Nutr 2009, 139:828.
    • (2009) J Nutr , vol.139 , pp. 828
    • McGhee, N.K.1    Jefferson, L.S.2    Kimball, S.R.3
  • 133
    • 42549141544 scopus 로고    scopus 로고
    • Acute alcohol intoxication increases REDD1 in skeletal muscle
    • Lang C.H., Frost R.A., Vary T.C. Acute alcohol intoxication increases REDD1 in skeletal muscle. Alcohol Clin Exp Res 2008, 32:796.
    • (2008) Alcohol Clin Exp Res , vol.32 , pp. 796
    • Lang, C.H.1    Frost, R.A.2    Vary, T.C.3
  • 134
    • 79951958957 scopus 로고    scopus 로고
    • Rapid induction of REDD1 expression by endurance exercise in rat skeletal muscle
    • Murakami T., Hasegawa K., Yoshinaga M. Rapid induction of REDD1 expression by endurance exercise in rat skeletal muscle. Biochem Biophys Res Commun 2011, 405:615.
    • (2011) Biochem Biophys Res Commun , vol.405 , pp. 615
    • Murakami, T.1    Hasegawa, K.2    Yoshinaga, M.3
  • 135
    • 80052635943 scopus 로고    scopus 로고
    • REDD1 (regulated in development and DNA damage response 1) expression in skeletal muscle as a surrogate biomarker of the efficiency of glucocorticoid receptor blockade
    • Kumari R., Willing L.B., Jefferson L.S., et al. REDD1 (regulated in development and DNA damage response 1) expression in skeletal muscle as a surrogate biomarker of the efficiency of glucocorticoid receptor blockade. Biochem Biophys Res Commun 2011, 412:644.
    • (2011) Biochem Biophys Res Commun , vol.412 , pp. 644
    • Kumari, R.1    Willing, L.B.2    Jefferson, L.S.3
  • 136
    • 72449201711 scopus 로고    scopus 로고
    • Regulation of REDD1 by insulin-like growth factor-I in skeletal muscle and myotubes
    • Frost R.A., Huber D., Pruznak A., et al. Regulation of REDD1 by insulin-like growth factor-I in skeletal muscle and myotubes. J Cell Biochem 2009, 108:1192.
    • (2009) J Cell Biochem , vol.108 , pp. 1192
    • Frost, R.A.1    Huber, D.2    Pruznak, A.3
  • 137
    • 77949315518 scopus 로고    scopus 로고
    • Insulin induces REDD1 expression through hypoxia-inducible factor 1 activation in adipocytes
    • Regazzetti C., Bost F., Le Marchand-Brustel Y., et al. Insulin induces REDD1 expression through hypoxia-inducible factor 1 activation in adipocytes. J Biol Chem 2010, 285:5157.
    • (2010) J Biol Chem , vol.285 , pp. 5157
    • Regazzetti, C.1    Bost, F.2    Le Marchand-Brustel, Y.3
  • 138
    • 77949535410 scopus 로고    scopus 로고
    • Negative feedback control of HIF-1 through REDD1-regulated ROS suppresses tumorigenesis
    • Horak P., Crawford A.R., Vadysirisack D.D., et al. Negative feedback control of HIF-1 through REDD1-regulated ROS suppresses tumorigenesis. Proc Natl Acad Sci U S A 2010, 107:4675.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 4675
    • Horak, P.1    Crawford, A.R.2    Vadysirisack, D.D.3
  • 139
    • 0036863624 scopus 로고    scopus 로고
    • REDD1, a developmentally regulated transcriptional target of p63 and p53, links p63 to regulation of reactive oxygen species
    • Ellisen L.W., Ramsayer K.D., Johannessen C.M., et al. REDD1, a developmentally regulated transcriptional target of p63 and p53, links p63 to regulation of reactive oxygen species. Mol Cell 2002, 10:995.
    • (2002) Mol Cell , vol.10 , pp. 995
    • Ellisen, L.W.1    Ramsayer, K.D.2    Johannessen, C.M.3
  • 140
    • 0036615021 scopus 로고    scopus 로고
    • Rats with a glucocorticoid-induced catabolic state show symptoms of oxidative stress and spleen atrophy: the effects of age and recovery
    • Orzechowski A., Ostaszewski P., Wilczak J., et al. Rats with a glucocorticoid-induced catabolic state show symptoms of oxidative stress and spleen atrophy: the effects of age and recovery. J Vet Med A Physiol Pathol Clin Med 2002, 49:256.
    • (2002) J Vet Med A Physiol Pathol Clin Med , vol.49 , pp. 256
    • Orzechowski, A.1    Ostaszewski, P.2    Wilczak, J.3
  • 141
    • 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
    • Handayaningsih A.E., Iguchi G., Fukuoka H., et al. Reactive oxygen species play an essential role in IGF-I signaling and IGF-I-induced myocyte hypertrophy in C2C12 myocytes. Endocrinology 2011, 152(3):912-921.
    • (2011) Endocrinology , vol.152 , Issue.3 , pp. 912-921
    • Handayaningsih, A.E.1    Iguchi, G.2    Fukuoka, H.3
  • 142
    • 78650809483 scopus 로고    scopus 로고
    • Ethyl pyruvate preserves IGF-I sensitivity toward mTOR substrates and protein synthesis in C2C12 myotubes
    • Frost R.A., Pereyra E., Lang C.H. Ethyl pyruvate preserves IGF-I sensitivity toward mTOR substrates and protein synthesis in C2C12 myotubes. Endocrinology 2011, 152:151.
    • (2011) Endocrinology , vol.152 , pp. 151
    • Frost, R.A.1    Pereyra, E.2    Lang, C.H.3
  • 143
    • 79551559572 scopus 로고    scopus 로고
    • Crosstalk between glucocorticoid receptor and nutritional sensor mTOR in skeletal muscle
    • Shimizu N., Yoshikawa N., Ito N., et al. Crosstalk between glucocorticoid receptor and nutritional sensor mTOR in skeletal muscle. Cell Metab 2011, 13:170.
    • (2011) Cell Metab , vol.13 , pp. 170
    • Shimizu, N.1    Yoshikawa, N.2    Ito, N.3
  • 144
    • 34848818486 scopus 로고    scopus 로고
    • Myosin accumulation and striated muscle myopathy result from the loss of muscle RING finger 1 and 3
    • Fielitz J., Kim M.S., Shelton J.M., et al. Myosin accumulation and striated muscle myopathy result from the loss of muscle RING finger 1 and 3. J Clin Invest 2007, 117:2486.
    • (2007) J Clin Invest , vol.117 , pp. 2486
    • Fielitz, J.1    Kim, M.S.2    Shelton, J.M.3
  • 145
    • 35548973391 scopus 로고    scopus 로고
    • The E3 ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle
    • Clarke B.A., Drujan D., Willis M.S., et al. The E3 ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle. Cell Metab 2007, 6:376.
    • (2007) Cell Metab , vol.6 , pp. 376
    • Clarke, B.A.1    Drujan, D.2    Willis, M.S.3
  • 146
    • 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., et al. During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation. J Cell Biol 2009, 185:1083.
    • (2009) J Cell Biol , vol.185 , pp. 1083
    • Cohen, S.1    Brault, J.J.2    Gygi, S.P.3
  • 147
    • 56049123409 scopus 로고    scopus 로고
    • The glucocorticoid receptor and FOXO1 synergistically activate the skeletal muscle atrophy-associated MuRF1 gene
    • Waddell D.S., Baehr L.M., van den Brandt J., et al. The glucocorticoid receptor and FOXO1 synergistically activate the skeletal muscle atrophy-associated MuRF1 gene. Am J Physiol Endocrinol Metab 2008, 295:E785.
    • (2008) Am J Physiol Endocrinol Metab , vol.295
    • Waddell, D.S.1    Baehr, L.M.2    van den Brandt, J.3
  • 148
    • 56249100986 scopus 로고    scopus 로고
    • A fasting inducible switch modulates gluconeogenesis via activator/coactivator exchange
    • Liu Y., Dentin R., Chen D., et al. A fasting inducible switch modulates gluconeogenesis via activator/coactivator exchange. Nature 2008, 456:269.
    • (2008) Nature , vol.456 , pp. 269
    • Liu, Y.1    Dentin, R.2    Chen, D.3
  • 149
    • 41449113346 scopus 로고    scopus 로고
    • Coordinate activation of autophagy and the proteasome pathway by FoxO transcription factor
    • Zhao J., Brault J.J., Schild A., et al. Coordinate activation of autophagy and the proteasome pathway by FoxO transcription factor. Autophagy 2008, 4:378.
    • (2008) Autophagy , vol.4 , pp. 378
    • Zhao, J.1    Brault, J.J.2    Schild, A.3
  • 150
    • 78650918920 scopus 로고    scopus 로고
    • FOXO/4E-BP signaling in Drosophila muscles regulates organism-wide proteostasis during aging
    • Demontis F., Perrimon N. FOXO/4E-BP signaling in Drosophila muscles regulates organism-wide proteostasis during aging. Cell 2010, 143:813.
    • (2010) Cell , vol.143 , pp. 813
    • Demontis, F.1    Perrimon, N.2
  • 151
    • 23944525416 scopus 로고    scopus 로고
    • 4E-BP functions as a metabolic brake used under stress conditions but not during normal growth
    • Teleman A.A., Chen Y.W., Cohen S.M. 4E-BP functions as a metabolic brake used under stress conditions but not during normal growth. Genes Dev 2005, 19:1844.
    • (2005) Genes Dev , vol.19 , pp. 1844
    • Teleman, A.A.1    Chen, Y.W.2    Cohen, S.M.3
  • 152
    • 67349212865 scopus 로고    scopus 로고
    • Overexpression of FOXO1 in skeletal muscle does not alter longevity in mice
    • Chiba T., Kamei Y., Shimizu T., et al. Overexpression of FOXO1 in skeletal muscle does not alter longevity in mice. Mech Ageing Dev 2009, 130:420.
    • (2009) Mech Ageing Dev , vol.130 , pp. 420
    • Chiba, T.1    Kamei, Y.2    Shimizu, T.3
  • 153
    • 77955290360 scopus 로고    scopus 로고
    • MTORC1 regulates cardiac function and myocyte survival through 4E-BP1 inhibition in mice
    • Zhang D., Contu R., Latronico M.V., et al. MTORC1 regulates cardiac function and myocyte survival through 4E-BP1 inhibition in mice. J Clin Invest 2010, 120:2805.
    • (2010) J Clin Invest , vol.120 , pp. 2805
    • Zhang, D.1    Contu, R.2    Latronico, M.V.3
  • 154
    • 79954618679 scopus 로고    scopus 로고
    • Novel insights into the regulation of skeletal muscle protein synthesis as revealed by a new nonradioactive in vivo technique
    • Goodman C.A., Mabrey D.M., Frey J.W., et al. Novel insights into the regulation of skeletal muscle protein synthesis as revealed by a new nonradioactive in vivo technique. FASEB J 2011, 25:1028.
    • (2011) FASEB J , vol.25 , pp. 1028
    • Goodman, C.A.1    Mabrey, D.M.2    Frey, J.W.3
  • 155
    • 0033672938 scopus 로고    scopus 로고
    • Glucocorticoids oppose translational control by leucine in skeletal muscle
    • Shah O.J., Anthony J.C., Kimball S.R., et al. Glucocorticoids oppose translational control by leucine in skeletal muscle. Am J Physiol Endocrinol Metab 2000, 279:E1185.
    • (2000) Am J Physiol Endocrinol Metab , vol.279
    • Shah, O.J.1    Anthony, J.C.2    Kimball, S.R.3
  • 156
    • 15444367412 scopus 로고    scopus 로고
    • Insulin-like growth factor-I gene transfer by electroporation prevents skeletal muscle atrophy in glucocorticoid-treated rats
    • Schakman O., Gilson H., de Coninck V., et al. Insulin-like growth factor-I gene transfer by electroporation prevents skeletal muscle atrophy in glucocorticoid-treated rats. Endocrinology 2005, 146:1789.
    • (2005) Endocrinology , vol.146 , pp. 1789
    • Schakman, O.1    Gilson, H.2    de Coninck, V.3
  • 157
    • 77956679005 scopus 로고    scopus 로고
    • BCATm deficiency ameliorates endotoxin-induced decrease in muscle protein synthesis and improves survival in septic mice
    • Lang C.H., Lynch C.J., Vary T.C. BCATm deficiency ameliorates endotoxin-induced decrease in muscle protein synthesis and improves survival in septic mice. Am J Physiol Regul Integr Comp Physiol 2010, 299:R935.
    • (2010) Am J Physiol Regul Integr Comp Physiol , vol.299
    • Lang, C.H.1    Lynch, C.J.2    Vary, T.C.3
  • 158
    • 77149138796 scopus 로고    scopus 로고
    • REDD1 is a major target of testosterone action in preventing dexamethasone-induced muscle loss
    • Wu Y., Zhao W., Zhao J., et al. REDD1 is a major target of testosterone action in preventing dexamethasone-induced muscle loss. Endocrinology 2010, 151:1050.
    • (2010) Endocrinology , vol.151 , pp. 1050
    • Wu, Y.1    Zhao, W.2    Zhao, J.3
  • 159
    • 78650176538 scopus 로고    scopus 로고
    • Protection against dexamethasone-induced muscle atrophy is related to modulation by testosterone of FOXO1 and PGC-1alpha
    • Qin W., Pan J., Wu Y., et al. Protection against dexamethasone-induced muscle atrophy is related to modulation by testosterone of FOXO1 and PGC-1alpha. Biochem Biophys Res Commun 2010, 403:473.
    • (2010) Biochem Biophys Res Commun , vol.403 , pp. 473
    • Qin, W.1    Pan, J.2    Wu, Y.3
  • 160
    • 0033307232 scopus 로고    scopus 로고
    • Effect of testosterone treatment on body composition and muscle strength in men over 65 years of age
    • Snyder P.J., Peachey H., Hannoush P., et al. Effect of testosterone treatment on body composition and muscle strength in men over 65 years of age. J Clin Endocrinol Metab 1999, 84:2647.
    • (1999) J Clin Endocrinol Metab , vol.84 , pp. 2647
    • Snyder, P.J.1    Peachey, H.2    Hannoush, P.3
  • 161
    • 78449280651 scopus 로고    scopus 로고
    • Characteristics of muscle fiber type are predictive of skeletal muscle mass and strength in elderly men
    • Verdijk L.B., Snijders T., Beelen M., et al. Characteristics of muscle fiber type are predictive of skeletal muscle mass and strength in elderly men. J Am Geriatr Soc 2010, 58:2069.
    • (2010) J Am Geriatr Soc , vol.58 , pp. 2069
    • Verdijk, L.B.1    Snijders, T.2    Beelen, M.3
  • 162
    • 77952557041 scopus 로고    scopus 로고
    • The GH/IGF1 axis and signaling pathways in the muscle and bone: mechanisms underlying age-related skeletal muscle wasting and osteoporosis
    • Perrini S., Laviola L., Carreira M.C., et al. The GH/IGF1 axis and signaling pathways in the muscle and bone: mechanisms underlying age-related skeletal muscle wasting and osteoporosis. J Endocrinol 2010, 205:201.
    • (2010) J Endocrinol , vol.205 , pp. 201
    • Perrini, S.1    Laviola, L.2    Carreira, M.C.3
  • 163
    • 78650318458 scopus 로고    scopus 로고
    • Anabolic processes in human skeletal muscle: restoring the identities of growth hormone and testosterone
    • West D.W., Phillips S.M. Anabolic processes in human skeletal muscle: restoring the identities of growth hormone and testosterone. Phys Sportsmed 2010, 38:97.
    • (2010) Phys Sportsmed , vol.38 , pp. 97
    • West, D.W.1    Phillips, S.M.2
  • 165
    • 20044388344 scopus 로고    scopus 로고
    • Older men are as responsive as young men to the anabolic effects of graded doses of testosterone on the skeletal muscle
    • Bhasin S., Woodhouse L., Casaburi R., et al. Older men are as responsive as young men to the anabolic effects of graded doses of testosterone on the skeletal muscle. J Clin Endocrinol Metab 2005, 90:678.
    • (2005) J Clin Endocrinol Metab , vol.90 , pp. 678
    • Bhasin, S.1    Woodhouse, L.2    Casaburi, R.3
  • 166
    • 70849117428 scopus 로고    scopus 로고
    • Testosterone deficiency, insulin resistance and the metabolic syndrome
    • Zitzmann M. Testosterone deficiency, insulin resistance and the metabolic syndrome. Nat Rev Endocrinol 2009, 5:673.
    • (2009) Nat Rev Endocrinol , vol.5 , pp. 673
    • Zitzmann, M.1
  • 167
    • 70350455712 scopus 로고    scopus 로고
    • Castration differentially alters basal and leucine-stimulated tissue protein synthesis in skeletal muscle and adipose tissue
    • Jiao Q., Pruznak A.M., Huber D., et al. Castration differentially alters basal and leucine-stimulated tissue protein synthesis in skeletal muscle and adipose tissue. Am J Physiol Endocrinol Metab 2009, 297(5):E1222-E1232.
    • (2009) Am J Physiol Endocrinol Metab , vol.297 , Issue.5
    • Jiao, Q.1    Pruznak, A.M.2    Huber, D.3
  • 168
    • 79251474705 scopus 로고    scopus 로고
    • Exercising before protein intake allows for greater use of dietary protein-derived amino acids for de novo muscle protein synthesis in both young and elderly men
    • Pennings B., Koopman R., Beelen M., et al. Exercising before protein intake allows for greater use of dietary protein-derived amino acids for de novo muscle protein synthesis in both young and elderly men. Am J Clin Nutr 2011, 93:322.
    • (2011) Am J Clin Nutr , vol.93 , pp. 322
    • Pennings, B.1    Koopman, R.2    Beelen, M.3
  • 169
    • 34548577038 scopus 로고    scopus 로고
    • Androgen receptor expression in the levator ani muscle of male mice
    • Johansen J.A., Breedlove S.M., Jordan C.L. Androgen receptor expression in the levator ani muscle of male mice. J Neuroendocrinol 2007, 19:823.
    • (2007) J Neuroendocrinol , vol.19 , pp. 823
    • Johansen, J.A.1    Breedlove, S.M.2    Jordan, C.L.3
  • 170
    • 45549109873 scopus 로고    scopus 로고
    • Testosterone and DHEA activate the glucose metabolism-related signaling pathway in skeletal muscle
    • Sato K., Iemitsu M., Aizawa K., et al. Testosterone and DHEA activate the glucose metabolism-related signaling pathway in skeletal muscle. Am J Physiol Endocrinol Metab 2008, 294:E961.
    • (2008) Am J Physiol Endocrinol Metab , vol.294
    • Sato, K.1    Iemitsu, M.2    Aizawa, K.3
  • 171
    • 76349111558 scopus 로고    scopus 로고
    • Acute exercise activates local bioactive androgen metabolism in skeletal muscle
    • Aizawa K., Iemitsu M., Maeda S., et al. Acute exercise activates local bioactive androgen metabolism in skeletal muscle. Steroids 2010, 75:219.
    • (2010) Steroids , vol.75 , pp. 219
    • Aizawa, K.1    Iemitsu, M.2    Maeda, S.3
  • 172
    • 16644402976 scopus 로고    scopus 로고
    • Inhibition of 5alpha-reductase blocks prostate effects of testosterone without blocking anabolic effects
    • Borst S.E., Lee J.H., Conover C.F. Inhibition of 5alpha-reductase blocks prostate effects of testosterone without blocking anabolic effects. Am J Physiol Endocrinol Metab 2005, 288:E222.
    • (2005) Am J Physiol Endocrinol Metab , vol.288
    • Borst, S.E.1    Lee, J.H.2    Conover, C.F.3
  • 173
    • 48749114487 scopus 로고    scopus 로고
    • Impaired skeletal muscle development and function in male, but not female, genomic androgen receptor knockout mice
    • MacLean H.E., Chiu W.S., Notini A.J., et al. Impaired skeletal muscle development and function in male, but not female, genomic androgen receptor knockout mice. FASEB J 2008, 22:2676.
    • (2008) FASEB J , vol.22 , pp. 2676
    • MacLean, H.E.1    Chiu, W.S.2    Notini, A.J.3
  • 174
    • 77956275729 scopus 로고    scopus 로고
    • Myocytic androgen receptor controls the strength but not the mass of limb muscles
    • Chambon C., Duteil D., Vignaud A., et al. Myocytic androgen receptor controls the strength but not the mass of limb muscles. Proc Natl Acad Sci U S A 2010, 107:14327.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 14327
    • Chambon, C.1    Duteil, D.2    Vignaud, A.3
  • 175
    • 70349315535 scopus 로고    scopus 로고
    • Skeletal muscle growth and fiber composition in mice are regulated through the transcription factors STAT5a/b: linking growth hormone to the androgen receptor
    • Klover P., Chen W., Zhu B.M., et al. Skeletal muscle growth and fiber composition in mice are regulated through the transcription factors STAT5a/b: linking growth hormone to the androgen receptor. FASEB J 2009, 23:3140.
    • (2009) FASEB J , vol.23 , pp. 3140
    • Klover, P.1    Chen, W.2    Zhu, B.M.3
  • 176
    • 79251538909 scopus 로고    scopus 로고
    • Voluntary running, skeletal muscle gene expression, and signaling inversely regulated by orchidectomy and testosterone replacement
    • Ibebunjo C., Eash J.K., Li C., et al. Voluntary running, skeletal muscle gene expression, and signaling inversely regulated by orchidectomy and testosterone replacement. Am J Physiol Endocrinol Metab 2011, 300:E327.
    • (2011) Am J Physiol Endocrinol Metab , vol.300
    • Ibebunjo, C.1    Eash, J.K.2    Li, C.3
  • 177
    • 77957661352 scopus 로고    scopus 로고
    • Branched-chain amino acid supplementation promotes survival and supports cardiac and skeletal muscle mitochondrial biogenesis in middle-aged mice
    • D'Antona G., Ragni M., Cardile A., et al. Branched-chain amino acid supplementation promotes survival and supports cardiac and skeletal muscle mitochondrial biogenesis in middle-aged mice. Cell Metab 2010, 12:362.
    • (2010) Cell Metab , vol.12 , pp. 362
    • D'Antona, G.1    Ragni, M.2    Cardile, A.3
  • 178
    • 59649120539 scopus 로고    scopus 로고
    • Signalling through RHEB-1 mediates intermittent fasting-induced longevity in C. elegans
    • Honjoh S., Yamamoto T., Uno M., et al. Signalling through RHEB-1 mediates intermittent fasting-induced longevity in C. elegans. Nature 2009, 457:726.
    • (2009) Nature , vol.457 , pp. 726
    • Honjoh, S.1    Yamamoto, T.2    Uno, M.3
  • 179
    • 4344674127 scopus 로고    scopus 로고
    • Hormonal and lifestyle determinants of appendicular skeletal muscle mass in men: the MINOS study
    • Szulc P., Duboeuf F., Marchand F., et al. Hormonal and lifestyle determinants of appendicular skeletal muscle mass in men: the MINOS study. Am J Clin Nutr 2004, 80:496.
    • (2004) Am J Clin Nutr , vol.80 , pp. 496
    • Szulc, P.1    Duboeuf, F.2    Marchand, F.3
  • 180
    • 65549120393 scopus 로고    scopus 로고
    • Conditional inactivation of androgen receptor gene in the nervous system: effects on male behavioral and neuroendocrine responses
    • Raskin K., de Gendt K., Duittoz A., et al. Conditional inactivation of androgen receptor gene in the nervous system: effects on male behavioral and neuroendocrine responses. J Neurosci 2009, 29:4461.
    • (2009) J Neurosci , vol.29 , pp. 4461
    • Raskin, K.1    de Gendt, K.2    Duittoz, A.3
  • 181
    • 34347327137 scopus 로고    scopus 로고
    • The pituitary function of androgen receptor constitutes a glucocorticoid production circuit
    • Miyamoto J., Matsumoto T., Shiina H., et al. The pituitary function of androgen receptor constitutes a glucocorticoid production circuit. Mol Cell Biol 2007, 27:4807.
    • (2007) Mol Cell Biol , vol.27 , pp. 4807
    • Miyamoto, J.1    Matsumoto, T.2    Shiina, H.3
  • 182
    • 77954935607 scopus 로고    scopus 로고
    • Effects of a novel selective androgen receptor modulator on dexamethasone-induced and hypogonadism-induced muscle atrophy
    • Jones A., Hwang D.J., Narayanan R., et al. Effects of a novel selective androgen receptor modulator on dexamethasone-induced and hypogonadism-induced muscle atrophy. Endocrinology 2010, 151:3706.
    • (2010) Endocrinology , vol.151 , pp. 3706
    • Jones, A.1    Hwang, D.J.2    Narayanan, R.3
  • 183
    • 70350300462 scopus 로고    scopus 로고
    • Differential atrophy of the lower-limb musculature during prolonged bed-rest
    • Belavy D.L., Miokovic T., Armbrecht G., et al. Differential atrophy of the lower-limb musculature during prolonged bed-rest. Eur J Appl Physiol 2009, 107:489.
    • (2009) Eur J Appl Physiol , vol.107 , pp. 489
    • Belavy, D.L.1    Miokovic, T.2    Armbrecht, G.3
  • 184
    • 70349660067 scopus 로고    scopus 로고
    • Muscle atrophy in immobilization and senescence in humans
    • Murton A.J., Greenhaff P.L. Muscle atrophy in immobilization and senescence in humans. Curr Opin Neurol 2009, 22:500.
    • (2009) Curr Opin Neurol , vol.22 , pp. 500
    • Murton, A.J.1    Greenhaff, P.L.2
  • 185
    • 0037378442 scopus 로고    scopus 로고
    • Branched-chain amino acid supplementation during bed rest: effect on recovery
    • Stein T.P., Donaldson M.R., Leskiw M.J., et al. Branched-chain amino acid supplementation during bed rest: effect on recovery. J Appl Physiol 2003, 94:1345.
    • (2003) J Appl Physiol , vol.94 , pp. 1345
    • Stein, T.P.1    Donaldson, M.R.2    Leskiw, M.J.3
  • 186
    • 50649116617 scopus 로고    scopus 로고
    • Resistance training and timed essential amino acids protect against the loss of muscle mass and strength during 28 days of bed rest and energy deficit
    • Brooks N., Cloutier G.J., Cadena S.M., et al. Resistance training and timed essential amino acids protect against the loss of muscle mass and strength during 28 days of bed rest and energy deficit. J Appl Physiol 2008, 105:241.
    • (2008) J Appl Physiol , vol.105 , pp. 241
    • Brooks, N.1    Cloutier, G.J.2    Cadena, S.M.3
  • 187
    • 78649639041 scopus 로고    scopus 로고
    • Effects of resistance exercise combined with essential amino acid supplementation and energy deficit on markers of skeletal muscle atrophy and regeneration during bed rest and active recovery
    • Brooks N.E., Cadena S.M., Vannier E., et al. Effects of resistance exercise combined with essential amino acid supplementation and energy deficit on markers of skeletal muscle atrophy and regeneration during bed rest and active recovery. Muscle Nerve 2010, 42:927.
    • (2010) Muscle Nerve , vol.42 , pp. 927
    • Brooks, N.E.1    Cadena, S.M.2    Vannier, E.3
  • 188
    • 1342310797 scopus 로고    scopus 로고
    • Ectopic expression of IGF-I and Shh by skeletal muscle inhibits disuse-mediated skeletal muscle atrophy and bone osteopenia in vivo
    • Alzghoul M.B., Gerrard D., Watkins B.A., et al. Ectopic expression of IGF-I and Shh by skeletal muscle inhibits disuse-mediated skeletal muscle atrophy and bone osteopenia in vivo. FASEB J 2004, 18:221.
    • (2004) FASEB J , vol.18 , pp. 221
    • Alzghoul, M.B.1    Gerrard, D.2    Watkins, B.A.3
  • 189
    • 5444262078 scopus 로고    scopus 로고
    • IKKbeta/NF-kappaB activation causes severe muscle wasting in mice
    • Cai D., Frantz J.D., Tawa N.E., et al. IKKbeta/NF-kappaB activation causes severe muscle wasting in mice. Cell 2004, 119:285.
    • (2004) Cell , vol.119 , pp. 285
    • Cai, D.1    Frantz, J.D.2    Tawa, N.E.3
  • 190
    • 11144356337 scopus 로고    scopus 로고
    • Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy
    • Sandri M., Sandri C., Gilbert A., et al. Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy. Cell 2004, 117:399.
    • (2004) Cell , vol.117 , pp. 399
    • Sandri, M.1    Sandri, C.2    Gilbert, A.3
  • 191
    • 77951916346 scopus 로고    scopus 로고
    • Effects of age and sedentary lifestyle on skeletal muscle NF-kappaB signaling in men
    • Buford T.W., Cooke M.B., Manini T.M., et al. Effects of age and sedentary lifestyle on skeletal muscle NF-kappaB signaling in men. J Gerontol A Biol Sci Med Sci 2010, 65:532.
    • (2010) J Gerontol A Biol Sci Med Sci , vol.65 , pp. 532
    • Buford, T.W.1    Cooke, M.B.2    Manini, T.M.3
  • 192
    • 79951581392 scopus 로고    scopus 로고
    • Inhibition of IkappaB kinase alpha (IKKα) or IKKbeta (IKKβ) plus forkhead box O (Foxo) abolishes skeletal muscle atrophy
    • Reed S.A., Senf S.M., Cornwell E.W., et al. Inhibition of IkappaB kinase alpha (IKKα) or IKKbeta (IKKβ) plus forkhead box O (Foxo) abolishes skeletal muscle atrophy. Biochem Biophys Res Commun 2011, 405:491.
    • (2011) Biochem Biophys Res Commun , vol.405 , pp. 491
    • Reed, S.A.1    Senf, S.M.2    Cornwell, E.W.3
  • 193
    • 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., et al. Ros-mediated activation of NF-kappaB and Foxo during muscle disuse. Muscle Nerve 2010, 41:110.
    • (2010) Muscle Nerve , vol.41 , pp. 110
    • Dodd, S.L.1    Gagnon, B.J.2    Senf, S.M.3
  • 194
    • 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.
    • (2008) Free Radic Biol Med , vol.44 , pp. 169
    • Reid, M.B.1
  • 195
    • 33847699369 scopus 로고    scopus 로고
    • Bowman-Birk inhibitor concentrate prevents atrophy, weakness, and oxidative stress in soleus muscle of hindlimb-unloaded mice
    • Arbogast S., Smith J., Matuszczak Y., et al. Bowman-Birk inhibitor concentrate prevents atrophy, weakness, and oxidative stress in soleus muscle of hindlimb-unloaded mice. J Appl Physiol 2007, 102:956.
    • (2007) J Appl Physiol , vol.102 , pp. 956
    • Arbogast, S.1    Smith, J.2    Matuszczak, Y.3
  • 196
    • 34147191693 scopus 로고    scopus 로고
    • Intermittent hyperthermia enhances skeletal muscle regrowth and attenuates oxidative damage following reloading
    • Selsby J.T., Rother S., Tsuda S., et al. Intermittent hyperthermia enhances skeletal muscle regrowth and attenuates oxidative damage following reloading. J Appl Physiol 2007, 102:1702.
    • (2007) J Appl Physiol , vol.102 , pp. 1702
    • Selsby, J.T.1    Rother, S.2    Tsuda, S.3
  • 197
    • 21044441687 scopus 로고    scopus 로고
    • Heat treatment reduces oxidative stress and protects muscle mass during immobilization
    • Selsby J.T., Dodd S.L. Heat treatment reduces oxidative stress and protects muscle mass during immobilization. Am J Physiol Regul Integr Comp Physiol 2005, 289:R134.
    • (2005) Am J Physiol Regul Integr Comp Physiol , vol.289
    • Selsby, J.T.1    Dodd, S.L.2
  • 198
    • 79956137343 scopus 로고    scopus 로고
    • Heat stress enhances mTOR signaling after resistance exercise in human skeletal muscle
    • Kakigi R., Naito H., Ogura Y., et al. Heat stress enhances mTOR signaling after resistance exercise in human skeletal muscle. J Physiol Sci 2011, 61:131.
    • (2011) J Physiol Sci , vol.61 , pp. 131
    • Kakigi, R.1    Naito, H.2    Ogura, Y.3
  • 199
    • 36248937816 scopus 로고    scopus 로고
    • Transcriptional pathways associated with skeletal muscle disuse atrophy in humans
    • Chen Y.W., Gregory C.M., Scarborough M.T., et al. Transcriptional pathways associated with skeletal muscle disuse atrophy in humans. Physiol Genomics 2007, 31:510.
    • (2007) Physiol Genomics , vol.31 , pp. 510
    • Chen, Y.W.1    Gregory, C.M.2    Scarborough, M.T.3
  • 200
    • 78349248267 scopus 로고    scopus 로고
    • Impact of viral-mediated IGF-I gene transfer on skeletal muscle following cast immobilization
    • Stevens-Lapsley J.E., Ye F., Liu M., et al. Impact of viral-mediated IGF-I gene transfer on skeletal muscle following cast immobilization. Am J Physiol Endocrinol Metab 2010, 299:E730.
    • (2010) Am J Physiol Endocrinol Metab , vol.299
    • Stevens-Lapsley, J.E.1    Ye, F.2    Liu, M.3
  • 201
    • 0031717854 scopus 로고    scopus 로고
    • Overexpression of IGF-I in skeletal muscle of transgenic mice does not prevent unloading-induced atrophy
    • Criswell D.S., Booth F.W., DeMayo F., et al. Overexpression of IGF-I in skeletal muscle of transgenic mice does not prevent unloading-induced atrophy. Am J Physiol 1998, 275:E373.
    • (1998) Am J Physiol , vol.275
    • Criswell, D.S.1    Booth, F.W.2    DeMayo, F.3
  • 202
    • 0033970668 scopus 로고    scopus 로고
    • Mutations in MCT1 cDNA in patients with symptomatic deficiency in lactate transport
    • Merezhinskaya N., Fishbein W.N., Davis J.I., et al. Mutations in MCT1 cDNA in patients with symptomatic deficiency in lactate transport. Muscle Nerve 2000, 23:90.
    • (2000) Muscle Nerve , vol.23 , pp. 90
    • Merezhinskaya, N.1    Fishbein, W.N.2    Davis, J.I.3
  • 203
    • 34248140159 scopus 로고    scopus 로고
    • Acidosis-sensing glutamine pump SNAT2 determines amino acid levels and mammalian target of rapamycin signalling to protein synthesis in L6 muscle cells
    • Evans K., Nasim Z., Brown J., et al. Acidosis-sensing glutamine pump SNAT2 determines amino acid levels and mammalian target of rapamycin signalling to protein synthesis in L6 muscle cells. J Am Soc Nephrol 2007, 18:1426.
    • (2007) J Am Soc Nephrol , vol.18 , pp. 1426
    • Evans, K.1    Nasim, Z.2    Brown, J.3
  • 204
    • 0022481384 scopus 로고
    • Intracellular pH controls growth factor-induced ribosomal protein S6 phosphorylation and protein synthesis in the G0-G1 transition of fibroblasts
    • Chambard J.C., Pouyssegur J. Intracellular pH controls growth factor-induced ribosomal protein S6 phosphorylation and protein synthesis in the G0-G1 transition of fibroblasts. Exp Cell Res 1986, 164:282.
    • (1986) Exp Cell Res , vol.164 , pp. 282
    • Chambard, J.C.1    Pouyssegur, J.2
  • 205
    • 0025346623 scopus 로고
    • Transmembrane Na+/H+ exchange in the rat thyroid cell strain FRTL-5: a possible role in insulin-like growth factor-I-mediated proliferation
    • Woods D.J., Soden J., Tomlinson S., et al. Transmembrane Na+/H+ exchange in the rat thyroid cell strain FRTL-5: a possible role in insulin-like growth factor-I-mediated proliferation. J Mol Endocrinol 1990, 4:177.
    • (1990) J Mol Endocrinol , vol.4 , pp. 177
    • Woods, D.J.1    Soden, J.2    Tomlinson, S.3
  • 206
    • 36348935585 scopus 로고    scopus 로고
    • Molecular and cellular events in alcohol-induced muscle disease
    • Fernandez-Sola J., Preedy V.R., Lang C.H., et al. Molecular and cellular events in alcohol-induced muscle disease. Alcohol Clin Exp Res 2007, 31:1953.
    • (2007) Alcohol Clin Exp Res , vol.31 , pp. 1953
    • Fernandez-Sola, J.1    Preedy, V.R.2    Lang, C.H.3
  • 207
    • 0035025348 scopus 로고    scopus 로고
    • Alcohol myopathy: impairment of protein synthesis and translation initiation
    • Lang C.H., Kimball S.R., Frost R.A., et al. Alcohol myopathy: impairment of protein synthesis and translation initiation. Int J Biochem Cell Biol 2001, 33:457.
    • (2001) Int J Biochem Cell Biol , vol.33 , pp. 457
    • Lang, C.H.1    Kimball, S.R.2    Frost, R.A.3
  • 208
    • 0036838513 scopus 로고    scopus 로고
    • Alcohol impairs insulin and IGF-I stimulation of S6K1 but not 4E-BP1 in skeletal muscle
    • Kumar V., Frost R.A., Lang C.H. Alcohol impairs insulin and IGF-I stimulation of S6K1 but not 4E-BP1 in skeletal muscle. Am J Physiol Endocrinol Metab 2002, 283:E917.
    • (2002) Am J Physiol Endocrinol Metab , vol.283
    • Kumar, V.1    Frost, R.A.2    Lang, C.H.3
  • 209
    • 0031844730 scopus 로고    scopus 로고
    • Modulation of the insulin-like growth factor system by chronic alcohol feeding
    • Lang C.H., Fan J., Lipton B.P., et al. Modulation of the insulin-like growth factor system by chronic alcohol feeding. Alcohol Clin Exp Res 1998, 22:823.
    • (1998) Alcohol Clin Exp Res , vol.22 , pp. 823
    • Lang, C.H.1    Fan, J.2    Lipton, B.P.3
  • 210
    • 2442658168 scopus 로고    scopus 로고
    • IGF-I/IGFBP-3 ameliorates alterations in protein synthesis, eIF4E availability, and myostatin in alcohol-fed rats
    • Lang C.H., Frost R.A., Svanberg E., et al. IGF-I/IGFBP-3 ameliorates alterations in protein synthesis, eIF4E availability, and myostatin in alcohol-fed rats. Am J Physiol Endocrinol Metab 2004, 286:E916.
    • (2004) Am J Physiol Endocrinol Metab , vol.286
    • Lang, C.H.1    Frost, R.A.2    Svanberg, E.3
  • 211
    • 0344464784 scopus 로고    scopus 로고
    • Alcohol impairs leucine-mediated phosphorylation of 4EBP1, S6K1, eIF4G, and mTOR in skeletal muscle
    • Lang C.H., Frost R.A., Deshpande N., et al. Alcohol impairs leucine-mediated phosphorylation of 4EBP1, S6K1, eIF4G, and mTOR in skeletal muscle. Am J Physiol Endocrinol Metab 2003, 285:E1205.
    • (2003) Am J Physiol Endocrinol Metab , vol.285
    • Lang, C.H.1    Frost, R.A.2    Deshpande, N.3
  • 212
    • 34447567479 scopus 로고    scopus 로고
    • Skeletal muscle protein synthesis and degradation exhibit sexual dimorphism after chronic alcohol consumption but not acute intoxication
    • Lang C.H., Frost R.A., Vary T.C. Skeletal muscle protein synthesis and degradation exhibit sexual dimorphism after chronic alcohol consumption but not acute intoxication. Am J Physiol Endocrinol Metab 2007, 292:E1497.
    • (2007) Am J Physiol Endocrinol Metab , vol.292
    • Lang, C.H.1    Frost, R.A.2    Vary, T.C.3
  • 213
    • 37348998877 scopus 로고    scopus 로고
    • Alcohol accelerates loss of muscle and impairs recovery of muscle mass resulting from disuse atrophy
    • Vargas R., Lang C.H. Alcohol accelerates loss of muscle and impairs recovery of muscle mass resulting from disuse atrophy. Alcohol Clin Exp Res 2008, 32:128.
    • (2008) Alcohol Clin Exp Res , vol.32 , pp. 128
    • Vargas, R.1    Lang, C.H.2
  • 214
    • 77951450185 scopus 로고    scopus 로고
    • Alcohol-induced IGF-I resistance is ameliorated in mice deficient for mitochondrial branched-chain aminotransferase
    • Lang C.H., Lynch C.J., Vary T.C. Alcohol-induced IGF-I resistance is ameliorated in mice deficient for mitochondrial branched-chain aminotransferase. J Nutr 2010, 140:932.
    • (2010) J Nutr , vol.140 , pp. 932
    • Lang, C.H.1    Lynch, C.J.2    Vary, T.C.3
  • 215
    • 68149162719 scopus 로고    scopus 로고
    • Leucine modulation of mitochondrial mass and oxygen consumption in skeletal muscle cells and adipocytes
    • Sun X., Zemel M.B. Leucine modulation of mitochondrial mass and oxygen consumption in skeletal muscle cells and adipocytes. Nutr Metab (Lond) 2009, 6:26.
    • (2009) Nutr Metab (Lond) , vol.6 , pp. 26
    • Sun, X.1    Zemel, M.B.2
  • 216
    • 34247241597 scopus 로고    scopus 로고
    • Leucine stimulates mammalian target of rapamycin signaling in C2C12 myoblasts in part through inhibition of adenosine monophosphate-activated protein kinase
    • Du M., Shen Q.W., Zhu M.J., et al. Leucine stimulates mammalian target of rapamycin signaling in C2C12 myoblasts in part through inhibition of adenosine monophosphate-activated protein kinase. J Anim Sci 2007, 85:919.
    • (2007) J Anim Sci , vol.85 , pp. 919
    • Du, M.1    Shen, Q.W.2    Zhu, M.J.3
  • 217
    • 79960646310 scopus 로고
    • Alcohol-induced modulation of rictor and mTORC2 activity in C2C12 myoblasts
    • Hong-Brown L.Q., Brown C.R., Navaratnarajah M., et al. Alcohol-induced modulation of rictor and mTORC2 activity in C2C12 myoblasts. Alcohol Clin Exp Res 1445, 35.
    • (1445) Alcohol Clin Exp Res , vol.35
    • Hong-Brown, L.Q.1    Brown, C.R.2    Navaratnarajah, M.3
  • 218
    • 84861172622 scopus 로고    scopus 로고
    • Rag GTPases and AMPK/TSC2/Rheb mediate the differential regulation of mTORC1 signaling in response to alcohol and leucine
    • [Epub ahead of print]
    • Hong-Brown L.Q., Brown C.R., Kazi A.A., et al. Rag GTPases and AMPK/TSC2/Rheb mediate the differential regulation of mTORC1 signaling in response to alcohol and leucine. Am J Physiol Cell Physiol 2012, [Epub ahead of print].
    • (2012) Am J Physiol Cell Physiol
    • Hong-Brown, L.Q.1    Brown, C.R.2    Kazi, A.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.