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Volumn 23, Issue 3, 2008, Pages 160-170

Signaling in muscle atrophy and hypertrophy

Author keywords

[No Author keywords available]

Indexed keywords

CONTRACTILE PROTEIN;

EID: 49049083353     PISSN: 15489213     EISSN: 15489221     Source Type: Journal    
DOI: 10.1152/physiol.00041.2007     Document Type: Review
Times cited : (650)

References (113)
  • 3
    • 34447121352 scopus 로고    scopus 로고
    • Role of the transcription factor ATF4 in the anabolic actions of insulin and the anti-anabolic actions of glucocorticoids
    • Adams CM. Role of the transcription factor ATF4 in the anabolic actions of insulin and the anti-anabolic actions of glucocorticoids. J Biol Chem 282: 16744-16753, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 16744-16753
    • Adams, C.M.1
  • 5
    • 33846332013 scopus 로고    scopus 로고
    • Regulation of myostatin expression and myoblast differentiation by FoxO and SMAD transcription factors
    • Allen DL, Unterman TG. Regulation of myostatin expression and myoblast differentiation by FoxO and SMAD transcription factors. Am J Physiol Cell Physiol 292: C188-C199, 2007.
    • (2007) Am J Physiol Cell Physiol , vol.292
    • Allen, D.L.1    Unterman, T.G.2
  • 6
    • 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 MB, Gerrard D, Watkins BA, Hannon K. Ectopic expression of IGF-I and Shh by skeletal muscle inhibits disuse-mediated skeletal muscle atrophy and bone osteopenia in vivo. FASEB J 18: 221-223, 2004.
    • (2004) FASEB J , vol.18 , pp. 221-223
    • Alzghoul, M.B.1    Gerrard, D.2    Watkins, B.A.3    Hannon, K.4
  • 8
    • 0036079364 scopus 로고    scopus 로고
    • Role of IGF-I and IGFBPs in the changes of mass and phenotype induced in rat soleus muscle by clenbuterol
    • Awede BL, Thissen JP, Lebacq J. Role of IGF-I and IGFBPs in the changes of mass and phenotype induced in rat soleus muscle by clenbuterol. Am J Physiol Endocrinol Metab 282: E31-E37, 2002.
    • (2002) Am J Physiol Endocrinol Metab , vol.282
    • Awede, B.L.1    Thissen, J.P.2    Lebacq, J.3
  • 12
    • 0036784164 scopus 로고    scopus 로고
    • Aging-related satellite cell differentiation defect occurs prematurely after Ski-induced muscle hypertrophy
    • Charge SB, Brack AS, Hughes SM. Aging-related satellite cell differentiation defect occurs prematurely after Ski-induced muscle hypertrophy. Am J Physiol Cell Physiol 283: C1228-C1241, 2002.
    • (2002) Am J Physiol Cell Physiol , vol.283
    • Charge, S.B.1    Brack, A.S.2    Hughes, S.M.3
  • 16
  • 17
    • 2342428466 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha produces insulin resistance in skeletal muscle by activation of inhibitor kappaB kinase in a p38 MAPK-dependent manner
    • de Alvaro C, Teruel T, Hernandez R, Lorenzo M. Tumor necrosis factor alpha produces insulin resistance in skeletal muscle by activation of inhibitor kappaB kinase in a p38 MAPK-dependent manner. J Biol Chem 279: 17070-17078, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 17070-17078
    • de Alvaro, C.1    Teruel, T.2    Hernandez, R.3    Lorenzo, M.4
  • 18
    • 0035890654 scopus 로고    scopus 로고
    • Identification of cathepsin L as a differentially expressed message associated with skeletal muscle wasting
    • Deval C, Mordier S, Obled C, Bechet D, Combaret L, Attaix D, Ferrara M. Identification of cathepsin L as a differentially expressed message associated with skeletal muscle wasting. Biochem J 360: 143-150, 2001.
    • (2001) Biochem J , vol.360 , pp. 143-150
    • Deval, C.1    Mordier, S.2    Obled, C.3    Bechet, D.4    Combaret, L.5    Attaix, D.6    Ferrara, M.7
  • 19
    • 34249775509 scopus 로고    scopus 로고
    • TNF-related weak inducer of apoptosis (TWEAK) is a potent skeletal muscle-wasting cytokine
    • Dogra C, Changotra H, Wedhas N, Qin X, Wergedal JE, Kumar A. TNF-related weak inducer of apoptosis (TWEAK) is a potent skeletal muscle-wasting cytokine. FASEB J 21: 1857-1869, 2007.
    • (2007) FASEB J , vol.21 , pp. 1857-1869
    • Dogra, C.1    Changotra, H.2    Wedhas, N.3    Qin, X.4    Wergedal, J.E.5    Kumar, A.6
  • 20
    • 85047693596 scopus 로고    scopus 로고
    • Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions
    • Du J, Wang X, Miereles C, Bailey JL, Debigare R, Zheng B, Price SR, Mitch WE. Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions. J Clin Invest 113: 115-123, 2004.
    • (2004) J Clin Invest , vol.113 , pp. 115-123
    • Du, J.1    Wang, X.2    Miereles, C.3    Bailey, J.L.4    Debigare, R.5    Zheng, B.6    Price, S.R.7    Mitch, W.E.8
  • 24
    • 0025287267 scopus 로고
    • Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy
    • Furuno K, Goodman MN, Goldberg AL. Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy. J Biol Chem 265: 8550-8557, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 8550-8557
    • Furuno, K.1    Goodman, M.N.2    Goldberg, A.L.3
  • 25
    • 0032973277 scopus 로고    scopus 로고
    • Changes in muscle mass and phenotype and the expression of autocrine and systemic growth factors by muscle in response to stretch and overload
    • Goldspink G. Changes in muscle mass and phenotype and the expression of autocrine and systemic growth factors by muscle in response to stretch and overload. J Anat 194: 323-334, 1999.
    • (1999) J Anat , vol.194 , pp. 323-334
    • Goldspink, G.1
  • 28
    • 18844398202 scopus 로고    scopus 로고
    • Mechanically induced titin kinase activation studied by force-probe molecular dynamics simulations
    • Grater F, Shen J, Jiang H, Gautel M, Grubmuller H. Mechanically induced titin kinase activation studied by force-probe molecular dynamics simulations. Biophys J 88: 790-804, 2005.
    • (2005) Biophys J , vol.88 , pp. 790-804
    • Grater, F.1    Shen, J.2    Jiang, H.3    Gautel, M.4    Grubmuller, H.5
  • 30
    • 34848861463 scopus 로고    scopus 로고
    • The energy sensor AMP-activated protein kinase directly regulates the mammalian FOXO3 transcription factor
    • Greer EL, Oskoui PR, Banko MR, Maniar JM, Gygi MP, Gygi SP, Brunet A. The energy sensor AMP-activated protein kinase directly regulates the mammalian FOXO3 transcription factor. J Biol Chem 282: 30107-30119, 2007.
    • (2007) J Biol Chem , vol.282 , pp. 30107-30119
    • Greer, E.L.1    Oskoui, P.R.2    Banko, M.R.3    Maniar, J.M.4    Gygi, M.P.5    Gygi, S.P.6    Brunet, A.7
  • 32
    • 4043171462 scopus 로고    scopus 로고
    • Upstream and downstream of mTOR
    • Hay N, Sonenberg N. Upstream and downstream of mTOR. Genes Dev 18: 1926-1945, 2004.
    • (2004) Genes Dev , vol.18 , pp. 1926-1945
    • Hay, N.1    Sonenberg, N.2
  • 34
    • 34548289502 scopus 로고    scopus 로고
    • Dynamic FoxO transcription factors
    • Huang H, Tindall DJ. Dynamic FoxO transcription factors. J Cell Sci 120: 2479-2487, 2007.
    • (2007) J Cell Sci , vol.120 , pp. 2479-2487
    • Huang, H.1    Tindall, D.J.2
  • 35
    • 11144317940 scopus 로고    scopus 로고
    • Disruption of either the Nfkb1 or the Bcl3 gene inhibits skeletal muscle atrophy
    • Hunter RB, Kandarian SC. Disruption of either the Nfkb1 or the Bcl3 gene inhibits skeletal muscle atrophy. J Clin Invest 114: 1504-1511, 2004.
    • (2004) J Clin Invest , vol.114 , pp. 1504-1511
    • Hunter, R.B.1    Kandarian, S.C.2
  • 39
    • 4544358547 scopus 로고    scopus 로고
    • Skeletal muscle FOXO1 (FKHR) transgenic mice have less skeletal muscle mass, down-regulated type I (slow twitch/red muscle) fiber genes, and impaired glycemic control
    • Kamei Y, Miura S, Suzuki M, Kai Y, Mizukami J, Taniguchi T, Mochida K, Hata T, Matsuda J, Aburatani H, Nishino I, Ezaki O. Skeletal muscle FOXO1 (FKHR) transgenic mice have less skeletal muscle mass, down-regulated type I (slow twitch/red muscle) fiber genes, and impaired glycemic control. J Biol Chem 279: 41114-41123, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 41114-41123
    • Kamei, Y.1    Miura, S.2    Suzuki, M.3    Kai, Y.4    Mizukami, J.5    Taniguchi, T.6    Mochida, K.7    Hata, T.8    Matsuda, J.9    Aburatani, H.10    Nishino, I.11    Ezaki, O.12
  • 40
    • 33846885682 scopus 로고    scopus 로고
    • Rapamycin inhibits the growth and muscle-sparing effects of clenbuterol
    • Kline WO, Panaro FJ, Yang H, Bodine SC. Rapamycin inhibits the growth and muscle-sparing effects of clenbuterol. J Appl Physiol 102: 740-747, 2007.
    • (2007) J Appl Physiol , vol.102 , pp. 740-747
    • Kline, W.O.1    Panaro, F.J.2    Yang, H.3    Bodine, S.C.4
  • 42
    • 30444458378 scopus 로고    scopus 로고
    • From A to Z and back? Multicompartment proteins in the sarcomere
    • Lange S, Ehler E, Gautel M. From A to Z and back? Multicompartment proteins in the sarcomere. Trends Cell Biol 16: 11-18, 2006.
    • (2006) Trends Cell Biol , vol.16 , pp. 11-18
    • Lange, S.1    Ehler, E.2    Gautel, M.3
  • 44
    • 13244298415 scopus 로고    scopus 로고
    • Insulin-like growth factor-1 (IGF1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway
    • Latres E, Amini AR, Amini AA, Griffiths J, Martin FJ, Wei Y, Lin HC, Yancopoulos GD, Glass DJ. Insulin-like growth factor-1 (IGF1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway. J Biol Chem 280: 2737-2744, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 2737-2744
    • Latres, E.1    Amini, A.R.2    Amini, A.A.3    Griffiths, J.4    Martin, F.J.5    Wei, Y.6    Lin, H.C.7    Yancopoulos, G.D.8    Glass, D.J.9
  • 46
    • 38349145459 scopus 로고    scopus 로고
    • Quadrupling muscle mass in mice by targeting TGF-beta signaling pathways
    • Lee SJ. Quadrupling muscle mass in mice by targeting TGF-beta signaling pathways. PLoS ONE 2: e789, 2007.
    • (2007) PLoS ONE , vol.2
    • Lee, S.J.1
  • 47
    • 0035979253 scopus 로고    scopus 로고
    • Regulation of myostatin activity and muscle growth
    • Lee SJ, McPherron AC. Regulation of myostatin activity and muscle growth. Proc Natl Acad Sci USA 98: 9306-9311, 2001.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9306-9311
    • Lee, S.J.1    McPherron, A.C.2
  • 49
    • 2542496898 scopus 로고    scopus 로고
    • Regulation of muscle protein degradation: Coordinated control of apoptotic and ubiquitin-proteasome systems by phosphatidylinositol 3 kinase
    • Lee SW, Dai G, Hu Z, Wang X, Du J, Mitch WE. Regulation of muscle protein degradation: coordinated control of apoptotic and ubiquitin-proteasome systems by phosphatidylinositol 3 kinase. J Am Soc Nephrol 15: 1537-1545, 2004.
    • (2004) J Am Soc Nephrol , vol.15 , pp. 1537-1545
    • Lee, S.W.1    Dai, G.2    Hu, Z.3    Wang, X.4    Du, J.5    Mitch, W.E.6
  • 50
    • 33947504481 scopus 로고    scopus 로고
    • Oxidative phenotype protects myofibers from pathological insults induced by chronic heart failure in mice
    • Li P, Waters RE, Redfern SI, Zhang M, Mao L, Annex BH, Yan Z. Oxidative phenotype protects myofibers from pathological insults induced by chronic heart failure in mice. Am J Pathol 170: 599-608, 2007.
    • (2007) Am J Pathol , vol.170 , pp. 599-608
    • Li, P.1    Waters, R.E.2    Redfern, S.I.3    Zhang, M.4    Mao, L.5    Annex, B.H.6    Yan, Z.7
  • 52
    • 36148967254 scopus 로고    scopus 로고
    • Effect of RNA oligonucleotide targeting Foxo-1 on muscle growth in normal and cancer cachexia mice
    • Liu CM, Yang Z, Liu CW, Wang R, Tien P, Dale R, Sun LQ. Effect of RNA oligonucleotide targeting Foxo-1 on muscle growth in normal and cancer cachexia mice. Cancer Gene Ther 14: 945-952, 2007.
    • (2007) Cancer Gene Ther , vol.14 , pp. 945-952
    • Liu, C.M.1    Yang, Z.2    Liu, C.W.3    Wang, R.4    Tien, P.5    Dale, R.6    Sun, L.Q.7
  • 54
  • 56
    • 38449084570 scopus 로고    scopus 로고
    • Counterpoint: Satellite cell addition is not obligatory for skeletal muscle hypertrophy
    • McCarthy JJ, Esser KA. Counterpoint: Satellite cell addition is not obligatory for skeletal muscle hypertrophy. J Appl Physiol 103: 1100-1102, 2007.
    • (2007) J Appl Physiol , vol.103 , pp. 1100-1102
    • McCarthy, J.J.1    Esser, K.A.2
  • 58
    • 33749254273 scopus 로고    scopus 로고
    • Myostatin induces cachexia by activating the ubiquitin proteolytic system through an NFkappaB-independent, FoxO1-dependent mechanism
    • McFarlane C, Plummer E, Thomas M, Hennebry A, Ashby M, Ling N, Smith H, Sharma M, Kambadur R. Myostatin induces cachexia by activating the ubiquitin proteolytic system through an NFkappaB-independent, FoxO1-dependent mechanism. J Cell Physiol 209: 501-514, 2006.
    • (2006) J Cell Physiol , vol.209 , pp. 501-514
    • McFarlane, C.1    Plummer, E.2    Thomas, M.3    Hennebry, A.4    Ashby, M.5    Ling, N.6    Smith, H.7    Sharma, M.8    Kambadur, R.9
  • 59
    • 0030840359 scopus 로고    scopus 로고
    • Double muscling in cattle due to mutations in the myostatin gene
    • McPherron AC, Lee SJ. Double muscling in cattle due to mutations in the myostatin gene. Proc Natl Acad Sci USA 94: 12457-12461, 1997.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12457-12461
    • McPherron, A.C.1    Lee, S.J.2
  • 62
    • 1542283812 scopus 로고    scopus 로고
    • In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker
    • Mizushima N, Yamamoto A, Matsui M, Yoshimori T, Ohsumi Y. In vivo analysis of autophagy in response to nutrient starvation using transgenic mice expressing a fluorescent autophagosome marker. Mol Biol Cell 15: 1101-1111, 2004.
    • (2004) Mol Biol Cell , vol.15 , pp. 1101-1111
    • Mizushima, N.1    Yamamoto, A.2    Matsui, M.3    Yoshimori, T.4    Ohsumi, Y.5
  • 63
    • 0034703021 scopus 로고    scopus 로고
    • Leucine limitation induces autophagy and activation of lysosome-dependent proteolysis in C2C12 myotubes through a mammalian target of rapamycin-independent signaling pathway
    • Mordier S, Deval C, Bechet D, Tassa A, Ferrara M. Leucine limitation induces autophagy and activation of lysosome-dependent proteolysis in C2C12 myotubes through a mammalian target of rapamycin-independent signaling pathway. J Biol Chem 275: 29900-29906, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 29900-29906
    • Mordier, S.1    Deval, C.2    Bechet, D.3    Tassa, A.4    Ferrara, M.5
  • 65
    • 0015102314 scopus 로고
    • Satellite cells as the source of nuclei in muscles of growing rats
    • Moss FP, Leblond CP. Satellite cells as the source of nuclei in muscles of growing rats. Anat Rec 170: 421-435, 1971.
    • (1971) Anat Rec , vol.170 , pp. 421-435
    • Moss, F.P.1    Leblond, C.P.2
  • 69
    • 0035055777 scopus 로고    scopus 로고
    • Intracellular signaling specificity in skeletal muscle in response to different modes of exercise
    • Nader GA, Esser KA. Intracellular signaling specificity in skeletal muscle in response to different modes of exercise. J Appl Physiol 90: 1936-1942, 2001.
    • (2001) J Appl Physiol , vol.90 , pp. 1936-1942
    • Nader, G.A.1    Esser, K.A.2
  • 70
    • 34548450714 scopus 로고    scopus 로고
    • AMPK activation stimulates myofibrillar protein degradation and expression of atrophy-related ubiquitin ligases by increasing FOXO transcription factors in C2C12 myotubes
    • Nakashima K, Yakabe Y. AMPK activation stimulates myofibrillar protein degradation and expression of atrophy-related ubiquitin ligases by increasing FOXO transcription factors in C2C12 myotubes. Biosci Biotechnol Biochem 71: 1650-1656, 2007.
    • (2007) Biosci Biotechnol Biochem , vol.71 , pp. 1650-1656
    • Nakashima, K.1    Yakabe, Y.2
  • 72
    • 0037047098 scopus 로고    scopus 로고
    • A protein kinase B-dependent and rapamycin-sensitive pathway controls skeletal muscle growth but not fiber type specification
    • Pallafacchina G, Calabria E, Serrano AL, Kalhovde JM, Schiaffino S. A protein kinase B-dependent and rapamycin-sensitive pathway controls skeletal muscle growth but not fiber type specification. Proc Natl Acad Sci USA 99: 9213-9218, 2002.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 9213-9218
    • Pallafacchina, G.1    Calabria, E.2    Serrano, A.L.3    Kalhovde, J.M.4    Schiaffino, S.5
  • 76
    • 33846015010 scopus 로고    scopus 로고
    • Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases
    • Sacheck JM, Hyatt JP, Raffaello A, Jagoe RT, Roy RR, Edgerton VR, Lecker SH, Goldberg AL. Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases. FASEB J 21: 140-155, 2007.
    • (2007) FASEB J , vol.21 , pp. 140-155
    • Sacheck, J.M.1    Hyatt, J.P.2    Raffaello, A.3    Jagoe, R.T.4    Roy, R.R.5    Edgerton, V.R.6    Lecker, S.H.7    Goldberg, A.L.8
  • 77
    • 4544293878 scopus 로고    scopus 로고
    • IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1
    • Sacheck JM, Ohtsuka A, McLary SC, Goldberg AL. IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1. Am J Physiol Endocrinol Metab 287: E591-E601, 2004.
    • (2004) Am J Physiol Endocrinol Metab , vol.287
    • Sacheck, J.M.1    Ohtsuka, A.2    McLary, S.C.3    Goldberg, A.L.4
  • 83
    • 4043140199 scopus 로고    scopus 로고
    • Molecular and cellular determinants of skeletal muscle atrophy and hypertrophy
    • Sartorelli V, Fulco M. Molecular and cellular determinants of skeletal muscle atrophy and hypertrophy. Sci STKE 2004: re11, 2004.
    • (2004) Sci STKE , vol.2004
    • Sartorelli, V.1    Fulco, M.2
  • 84
    • 42449133390 scopus 로고    scopus 로고
    • Mechanisms of glucocorticoid-induced myopathy
    • Schakman O, Gilson H, Thissen JP. Mechanisms of glucocorticoid-induced myopathy. J Endocrinol 197: 1-10, 2008.
    • (2008) J Endocrinol , vol.197 , pp. 1-10
    • Schakman, O.1    Gilson, H.2    Thissen, J.P.3
  • 85
    • 0017179024 scopus 로고
    • The fate of newly formed satellite cells during compensatory muscle hypertrophy
    • Schiaffino S, Bormioli SP, Aloisi M. The fate of newly formed satellite cells during compensatory muscle hypertrophy. Virchows Arch B Cell Pathol 21: 113-118, 1976.
    • (1976) Virchows Arch B Cell Pathol , vol.21 , pp. 113-118
    • Schiaffino, S.1    Bormioli, S.P.2    Aloisi, M.3
  • 86
    • 0015319006 scopus 로고
    • Studies on the effect of denervation in developing muscle. II. The lysosomal system
    • Schiaffino S, Hanzlikova V. Studies on the effect of denervation in developing muscle. II. The lysosomal system. J Ultrastruct Res 39: 1-14, 1972.
    • (1972) J Ultrastruct Res , vol.39 , pp. 1-14
    • Schiaffino, S.1    Hanzlikova, V.2
  • 88
    • 24744446252 scopus 로고    scopus 로고
    • Transgenic overexpression of locally acting insulin-like growth factor-1 inhibits ubiquitin-mediated muscle atrophy in chronic left-ventricular dysfunction
    • Schulze PC, Fang J, Kassik KA, Gannon J, Cupesi M, MacGillivray C, Lee RT, Rosenthal N. Transgenic overexpression of locally acting insulin-like growth factor-1 inhibits ubiquitin-mediated muscle atrophy in chronic left-ventricular dysfunction. Circ Res 97: 418-426, 2005.
    • (2005) Circ Res , vol.97 , pp. 418-426
    • Schulze, P.C.1    Fang, J.2    Kassik, K.A.3    Gannon, J.4    Cupesi, M.5    MacGillivray, C.6    Lee, R.T.7    Rosenthal, N.8
  • 89
    • 8344242220 scopus 로고    scopus 로고
    • Autophagy in health and disease: A double-edged sword
    • Shintani T, Klionsky DJ. Autophagy in health and disease: a double-edged sword. Science 306: 990-995, 2004.
    • (2004) Science , vol.306 , pp. 990-995
    • Shintani, T.1    Klionsky, D.J.2
  • 90
    • 0034786073 scopus 로고    scopus 로고
    • Elevated IGF-II mRNA and phosphorylation of 4E-BP1 and p70(S6k) in muscle showing clenbuterol-induced anabolism
    • Sneddon AA, Delday MI, Steven J, Maltin CA. Elevated IGF-II mRNA and phosphorylation of 4E-BP1 and p70(S6k) in muscle showing clenbuterol-induced anabolism. Am J Physiol Endocrinol Metab 281: E676-E682, 2001.
    • (2001) Am J Physiol Endocrinol Metab , vol.281
    • Sneddon, A.A.1    Delday, M.I.2    Steven, J.3    Maltin, C.A.4
  • 91
    • 14844336534 scopus 로고    scopus 로고
    • Muscle-specific expression of IGF1 blocks angiotensin II-induced skeletal muscle wasting
    • Song YH, Li Y, Du J, Mitch WE, Rosenthal N, Delafontaine P. Muscle-specific expression of IGF1 blocks angiotensin II-induced skeletal muscle wasting. J Clin Invest 115: 451-458, 2005.
    • (2005) J Clin Invest , vol.115 , pp. 451-458
    • Song, Y.H.1    Li, Y.2    Du, J.3    Mitch, W.E.4    Rosenthal, N.5    Delafontaine, P.6
  • 94
    • 42149146095 scopus 로고    scopus 로고
    • Glucocorticoids differentially regulate degradation of MyoD and Id1 by N-terminal ubiquitination to promote muscle protein catabolism
    • Sun L, Trausch-Azar JS, Muglia LJ, Schwartz AL. Glucocorticoids differentially regulate degradation of MyoD and Id1 by N-terminal ubiquitination to promote muscle protein catabolism. Proc Natl Acad Sci USA 105: 3339-3344, 2008.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 3339-3344
    • Sun, L.1    Trausch-Azar, J.S.2    Muglia, L.J.3    Schwartz, A.L.4
  • 96
    • 0347986620 scopus 로고    scopus 로고
    • Class III phosphoinositide 3-kinase: Beclin1 complex mediates the amino acid-dependent regulation of autophagy in C2C12 myotubes
    • Tassa A, Roux MP, Attaix D, Bechet DM. Class III phosphoinositide 3-kinase: beclin1 complex mediates the amino acid-dependent regulation of autophagy in C2C12 myotubes. Biochem J 376: 577-586, 2003.
    • (2003) Biochem J , vol.376 , pp. 577-586
    • Tassa, A.1    Roux, M.P.2    Attaix, D.3    Bechet, D.M.4
  • 97
    • 37449029143 scopus 로고    scopus 로고
    • Nutritional control of protein biosynthetic capacity by insulin via Myc in Drosophila
    • Teleman AA, Hietakangas V, Sayadian AC, Cohen SM. Nutritional control of protein biosynthetic capacity by insulin via Myc in Drosophila. Cell Metab 7: 21-32, 2008.
    • (2008) Cell Metab , vol.7 , pp. 21-32
    • Teleman, A.A.1    Hietakangas, V.2    Sayadian, A.C.3    Cohen, S.M.4
  • 99
    • 0032891637 scopus 로고    scopus 로고
    • Akt kinases and 2-deoxyglucose uptake in rat skeletal muscles in vivo: Study with insulin and exercise
    • Turinsky J, Damrau-Abney A. Akt kinases and 2-deoxyglucose uptake in rat skeletal muscles in vivo: study with insulin and exercise. Am J Physiol Regul Integr Comp Physiol 276: R277-R282, 1999.
    • (1999) Am J Physiol Regul Integr Comp Physiol , vol.276
    • Turinsky, J.1    Damrau-Abney, A.2
  • 102
    • 0036895736 scopus 로고    scopus 로고
    • Loss of myostatin attenuates severity of muscular dystrophy in mdx mice
    • Wagner KR, McPherron AC, Winik N, Lee SJ. Loss of myostatin attenuates severity of muscular dystrophy in mdx mice. Ann Neurol 52: 832-836, 2002.
    • (2002) Ann Neurol , vol.52 , pp. 832-836
    • Wagner, K.R.1    McPherron, A.C.2    Winik, N.3    Lee, S.J.4
  • 103
    • 33749366334 scopus 로고    scopus 로고
    • Muscle atrophy in transgenic mice expressing a human TSC1 transgene
    • Wan M, Wu X, Guan KL, Han M, Zhuang Y, Xu T. Muscle atrophy in transgenic mice expressing a human TSC1 transgene. FEBS Lett 580: 5621-5627, 2006.
    • (2006) FEBS Lett , vol.580 , pp. 5621-5627
    • Wan, M.1    Wu, X.2    Guan, K.L.3    Han, M.4    Zhuang, Y.5    Xu, T.6
  • 104
    • 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 LW, Jefferson LS, Kimball SR. Dexamethasone represses signaling through the mammalian target of rapamycin in muscle cells by enhancing expression of REDD1. J Biol Chem 281: 39128-39134, 2006.
    • (2006) J Biol Chem , vol.281 , pp. 39128-39134
    • Wang, H.1    Kubica, N.2    Ellisen, L.W.3    Jefferson, L.S.4    Kimball, S.R.5
  • 105
  • 106
    • 34247096092 scopus 로고    scopus 로고
    • X-chromosome linked inhibitor of apoptosis protein inhibits muscle proteolysis in insulin-deficient mice
    • Wang XH, Hu J, Du J, Klein JD. X-chromosome linked inhibitor of apoptosis protein inhibits muscle proteolysis in insulin-deficient mice. Gene Ther 14: 711-720, 2007.
    • (2007) Gene Ther , vol.14 , pp. 711-720
    • Wang, X.H.1    Hu, J.2    Du, J.3    Klein, J.D.4
  • 112
    • 36448968532 scopus 로고    scopus 로고
    • FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells
    • Zhao J, Brault JJ, Schild A, Cao P, Sandri M, Schiaffino S, Lecker SH, Goldberg AL. FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab 6: 472-483, 2007.
    • (2007) Cell Metab , vol.6 , pp. 472-483
    • Zhao, J.1    Brault, J.J.2    Schild, A.3    Cao, P.4    Sandri, M.5    Schiaffino, S.6    Lecker, S.H.7    Goldberg, A.L.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.