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Volumn 11, Issue 3, 2008, Pages 233-241

Epigenetic drugs in the treatment of skeletal muscle atrophy

Author keywords

Autophagy; Cachexia; Chromatin; Deacetylase inhibitors; Muscle atrophy; Sarcopenia

Indexed keywords

DEACETYLASE INHIBITOR; ENZYME INHIBITOR; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR FOXO; UNCLASSIFIED DRUG;

EID: 42149098394     PISSN: 13631950     EISSN: 15353885     Source Type: Journal    
DOI: 10.1097/MCO.0b013e3282fa1810     Document Type: Review
Times cited : (25)

References (117)
  • 1
    • 0037318822 scopus 로고    scopus 로고
    • Signalling pathways that mediate skeletal muscle hypertrophy and atrophy
    • Glass DJ. Signalling pathways that mediate skeletal muscle hypertrophy and atrophy. Nat Cell Biol 2003; 5:87-90.
    • (2003) Nat Cell Biol , vol.5 , pp. 87-90
    • Glass, D.J.1
  • 2
    • 0035350530 scopus 로고    scopus 로고
    • What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?
    • Jagoe RT, Goldberg AL. What do we really know about the ubiquitin-proteasome pathway in muscle atrophy? Curr Opin Clin Nutr Metab Care 2001; 4:183-190.
    • (2001) Curr Opin Clin Nutr Metab Care , vol.4 , pp. 183-190
    • Jagoe, R.T.1    Goldberg, A.L.2
  • 3
    • 0020660874 scopus 로고
    • Protein turnover measured in vivo and in vitro in muscles undergoing compensatory growth and subsequent denervation atrophy
    • Goldspink DF, Garlick PJ, McNurlan MA. Protein turnover measured in vivo and in vitro in muscles undergoing compensatory growth and subsequent denervation atrophy. Biochem J 1983; 210:89-98.
    • (1983) Biochem J , vol.210 , pp. 89-98
    • Goldspink, D.F.1    Garlick, P.J.2    McNurlan, M.A.3
  • 4
    • 0035136062 scopus 로고    scopus 로고
    • Localized Igf-1 transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle
    • Musarò A, McCullagh K, Paul A, Localized Igf-1 transgene expression sustains hypertrophy and regeneration in senescent skeletal muscle. Nat Genet 2001; 27:195-200.
    • (2001) Nat Genet , vol.27 , pp. 195-200
    • Musarò, A.1    McCullagh, K.2    Paul, A.3
  • 5
    • 0025362896 scopus 로고
    • Activation of insulin-like growth factor gene expression during work-induced skeletal muscle growth
    • DeVol DL, Rotwein P, Sadow JL, et al. Activation of insulin-like growth factor gene expression during work-induced skeletal muscle growth. Am J Physiol 1990; 259 (1 Pt 1):E89-95.
    • (1990) Am J Physiol , vol.259 , Issue.1 PART 1
    • DeVol, D.L.1    Rotwein, P.2    Sadow, J.L.3
  • 6
    • 33847638108 scopus 로고    scopus 로고
    • The role of the insulin-like growth factor 1 (IGF-1) in skeletal muscle physiology
    • Philippou A, Maridaki M, Halapas A, Koutsilieris M. The role of the insulin-like growth factor 1 (IGF-1) in skeletal muscle physiology. In Vivo 2007; 21:45-54.
    • (2007) In Vivo , vol.21 , pp. 45-54
    • Philippou, A.1    Maridaki, M.2    Halapas, A.3    Koutsilieris, M.4
  • 7
    • 0035736260 scopus 로고    scopus 로고
    • Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo
    • Bodine SC, Stitt TN, Gonzalez M, et al. Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo. Nat Cell Biol 2001; 3:1014-1019.
    • (2001) Nat Cell Biol , vol.3 , pp. 1014-1019
    • Bodine, S.C.1    Stitt, T.N.2    Gonzalez, M.3
  • 8
    • 0035735902 scopus 로고    scopus 로고
    • Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways
    • Rommel C, Bodine SC, Clarke BA, et al. Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways. Nat Cell Biol 2001; 3:1009-1013.
    • (2001) Nat Cell Biol , vol.3 , pp. 1009-1013
    • Rommel, C.1    Bodine, S.C.2    Clarke, B.A.3
  • 9
    • 0032560521 scopus 로고    scopus 로고
    • Evidence of insulin-stimulated phosphorylation and activation of the mammalian target of rapamycin mediated by a protein kinase B signaling pathway
    • Scott PH, Brunn GJ, Kohn AD, et al. Evidence of insulin-stimulated phosphorylation and activation of the mammalian target of rapamycin mediated by a protein kinase B signaling pathway. Proc Natl Acad Sci USA 1998; 95:7772-7777.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7772-7777
    • Scott, P.H.1    Brunn, G.J.2    Kohn, A.D.3
  • 10
    • 0029984354 scopus 로고    scopus 로고
    • 4E-BP1 phosphorylation is mediated by the FRAP-p70s6k pathway and is independent of mitogen-activated protein kinase
    • von Manteuffel SR, Gingras AC, Ming XF, et al. 4E-BP1 phosphorylation is mediated by the FRAP-p70s6k pathway and is independent of mitogen-activated protein kinase. Proc Natl Acad Sci USA 1996; 93:4076-4080.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4076-4080
    • von Manteuffel, S.R.1    Gingras, A.C.2    Ming, X.F.3
  • 11
    • 0030716488 scopus 로고    scopus 로고
    • Regulation of eIF-4E BP1 phosphorylation by mTOR
    • Hara K, Yonezawa K, Kozlowski MT, et al. Regulation of eIF-4E BP1 phosphorylation by mTOR. J Biol Chem 1997; 272:26457-26463.
    • (1997) J Biol Chem , vol.272 , pp. 26457-26463
    • Hara, K.1    Yonezawa, K.2    Kozlowski, M.T.3
  • 12
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross DA, Alessi DR, Cohen P, et al. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature 1995; 378:785-789.
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3
  • 13
    • 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; 117:399-412.
    • (2004) Cell , vol.117 , pp. 399-412
    • Sandri, M.1    Sandri, C.2    Gilbert, A.3
  • 14
    • 2042425906 scopus 로고    scopus 로고
    • The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors
    • Stitt TN, Drujan D, Clarke BA, et al. The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. Mol Cell 2004; 14:395-403.
    • (2004) Mol Cell , vol.14 , pp. 395-403
    • Stitt, T.N.1    Drujan, D.2    Clarke, B.A.3
  • 15
    • 0037018145 scopus 로고    scopus 로고
    • NFAT: Ubiquitous regulator of cell differentiation and adaptation
    • Horsley V, Pavlath GK. NFAT: ubiquitous regulator of cell differentiation and adaptation. J Cell Biol 2002; 156:771-774.
    • (2002) J Cell Biol , vol.156 , pp. 771-774
    • Horsley, V.1    Pavlath, G.K.2
  • 16
    • 0033526991 scopus 로고    scopus 로고
    • IGF-1 induces skeletal myocyte hypertrophy through calcineurin in association with GATA-2 and NF-ATc1
    • Musarò A, McCullagh KJ, Naya FJ, et al. IGF-1 induces skeletal myocyte hypertrophy through calcineurin in association with GATA-2 and NF-ATc1. Nature 1999; 400:581-585.
    • (1999) Nature , vol.400 , pp. 581-585
    • Musarò, A.1    McCullagh, K.J.2    Naya, F.J.3
  • 17
    • 0033527021 scopus 로고    scopus 로고
    • 2+-dependent calcineurin signalling pathway
    • 2+-dependent calcineurin signalling pathway. Nature 1999; 400:576-581.
    • (1999) Nature , vol.400 , pp. 576-581
    • Semsarian, C.1    Wu, M.J.2    Ju, Y.K.3
  • 18
    • 0037163050 scopus 로고    scopus 로고
    • Regulation of Raf-Akt cross-talk
    • Moelling K, Schad K, Bosse M, et al. Regulation of Raf-Akt cross-talk. J Biol Chem 2002; 277:31099-31106.
    • (2002) J Biol Chem , vol.277 , pp. 31099-31106
    • Moelling, K.1    Schad, K.2    Bosse, M.3
  • 19
    • 0033607784 scopus 로고    scopus 로고
    • Rommel C, Clarke BA, Zimmermann S, et al. Differentiation stage-specific inhibition of the Raf-MEK-ERK pathway by Akt. Science 1999; 286:1738-1741.
    • Rommel C, Clarke BA, Zimmermann S, et al. Differentiation stage-specific inhibition of the Raf-MEK-ERK pathway by Akt. Science 1999; 286:1738-1741.
  • 20
    • 0033607633 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Raf by Akt (protein kinase B)
    • Zimmermann S, Moelling K. Phosphorylation and regulation of Raf by Akt (protein kinase B). Science 1999; 286:1741-1744.
    • (1999) Science , vol.286 , pp. 1741-1744
    • Zimmermann, S.1    Moelling, K.2
  • 21
    • 35348950607 scopus 로고    scopus 로고
    • Serra C, Palacios D, Mozzetta C, et al. Functional interdependence at the chromatin level between the MKK6/p38 and IGF1/PI3K/AKT pathways during muscle differentiation. Mol Cell 2007; 28:200-213. This manuscript reveals an essential role of inflammation-activated MKK6-p38 and the IGF1-induced PI3K/AKT pathways in the assembly of the muscle transcriptosome, by targeting distinct components at the chromatin level.
    • Serra C, Palacios D, Mozzetta C, et al. Functional interdependence at the chromatin level between the MKK6/p38 and IGF1/PI3K/AKT pathways during muscle differentiation. Mol Cell 2007; 28:200-213. This manuscript reveals an essential role of inflammation-activated MKK6-p38 and the IGF1-induced PI3K/AKT pathways in the assembly of the muscle transcriptosome, by targeting distinct components at the chromatin level.
  • 22
    • 0031010050 scopus 로고    scopus 로고
    • Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member
    • McPherron AC, Lawler AM, Lee SJ. Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member. Nature 1997; 387:83-90.
    • (1997) Nature , vol.387 , pp. 83-90
    • McPherron, A.C.1    Lawler, A.M.2    Lee, S.J.3
  • 23
    • 0037147210 scopus 로고    scopus 로고
    • Myostatin inhibits myoblast differentiation by down-regulating MyoD expression
    • Langley B, Thomas M, Bishop A, et al. Myostatin inhibits myoblast differentiation by down-regulating MyoD expression. J Biol Chem 2002; 277:49831-49840.
    • (2002) J Biol Chem , vol.277 , pp. 49831-49840
    • Langley, B.1    Thomas, M.2    Bishop, A.3
  • 24
    • 16944364045 scopus 로고    scopus 로고
    • A deletion in the bovine myostatin gene causes the double-muscled phenotype in cattle
    • Grobet L, Martin LJ, Poncelet D, et al. A deletion in the bovine myostatin gene causes the double-muscled phenotype in cattle. Nat Genet 1997; 17:71-74.
    • (1997) Nat Genet , vol.17 , pp. 71-74
    • Grobet, L.1    Martin, L.J.2    Poncelet, D.3
  • 25
    • 2942735123 scopus 로고    scopus 로고
    • Myostatin mutation associated with gross muscle hypertrophy in a child
    • Schuelke M, Wagner KR, Stolz LE, et al. Myostatin mutation associated with gross muscle hypertrophy in a child. N Engl J Med 2004; 350:2682-2688.
    • (2004) N Engl J Med , vol.350 , pp. 2682-2688
    • Schuelke, M.1    Wagner, K.R.2    Stolz, L.E.3
  • 26
    • 34249733201 scopus 로고    scopus 로고
    • A mutation in the myostatin gene increases muscle mass and enhances racing performance in heterozygote dogs
    • This paper describes a myostatin mutation found in a dog breed resulting in a double-muscled phenotype
    • Mosher DS, Quignon P, Bustamante CD, et al. A mutation in the myostatin gene increases muscle mass and enhances racing performance in heterozygote dogs. PLoS Genet 2007; 3:e79. This paper describes a myostatin mutation found in a dog breed resulting in a double-muscled phenotype.
    • (2007) PLoS Genet , vol.3
    • Mosher, D.S.1    Quignon, P.2    Bustamante, C.D.3
  • 27
    • 2342515391 scopus 로고    scopus 로고
    • Follistatin complexes myostatin and antagonises myostatin-mediated inhibition of myogenesis
    • Amthor H, Nicholas G, McKinnell I, et al. Follistatin complexes myostatin and antagonises myostatin-mediated inhibition of myogenesis. Dev Biol 2004; 270:19-30.
    • (2004) Dev Biol , vol.270 , pp. 19-30
    • Amthor, H.1    Nicholas, G.2    McKinnell, I.3
  • 28
    • 0037165983 scopus 로고    scopus 로고
    • Induction of cachexia in mice by systemically administered myostatin
    • Zimmers TA, Davies MV, Koniaris LG, et al. Induction of cachexia in mice by systemically administered myostatin. Science 2002; 296:1486-1488.
    • (2002) Science , vol.296 , pp. 1486-1488
    • Zimmers, T.A.1    Davies, M.V.2    Koniaris, L.G.3
  • 29
    • 24344443668 scopus 로고    scopus 로고
    • The regulation of Notch signaling in muscle stem cell activation and postnatal myogenesis
    • Luo D, Renault VM, Rando TA. The regulation of Notch signaling in muscle stem cell activation and postnatal myogenesis. Semin Cell Dev Biol 2005; 16:612-622.
    • (2005) Semin Cell Dev Biol , vol.16 , pp. 612-622
    • Luo, D.1    Renault, V.M.2    Rando, T.A.3
  • 30
    • 33746541115 scopus 로고    scopus 로고
    • Inhibition of Notch signaling induces myotube hypertrophy by recruiting a subpopulation of reserve cells
    • Kitzmann M, Bonnieu A, Duret C, et al. Inhibition of Notch signaling induces myotube hypertrophy by recruiting a subpopulation of reserve cells. J Cell Physiol 2006; 208:538-548.
    • (2006) J Cell Physiol , vol.208 , pp. 538-548
    • Kitzmann, M.1    Bonnieu, A.2    Duret, C.3
  • 31
    • 0037726553 scopus 로고    scopus 로고
    • IL-4 acts as a myoblast recruitment factor during mammalian muscle growth
    • Horsley V, Jansen KM, Mills ST, Pavlath GK. IL-4 acts as a myoblast recruitment factor during mammalian muscle growth. Cell 2003; 113:483-494.
    • (2003) Cell , vol.113 , pp. 483-494
    • Horsley, V.1    Jansen, K.M.2    Mills, S.T.3    Pavlath, G.K.4
  • 32
    • 33751520727 scopus 로고    scopus 로고
    • Modifying muscle mass: The endocrine perspective
    • Solomon AM, Bouloux PM. Modifying muscle mass: the endocrine perspective. J Endocrinol 2006; 2:349-360.
    • (2006) J Endocrinol , vol.2 , pp. 349-360
    • Solomon, A.M.1    Bouloux, P.M.2
  • 33
    • 27144512111 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system and skeletal muscle wasting
    • Attaix D, Ventadour S, Codran A, et al. The ubiquitin-proteasome system and skeletal muscle wasting. Essays Biochem 2005; 41:173-186.
    • (2005) Essays Biochem , vol.41 , pp. 173-186
    • Attaix, D.1    Ventadour, S.2    Codran, A.3
  • 34
    • 1842339868 scopus 로고    scopus 로고
    • Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles
    • Tawa NE Jr, Odessey R, Goldberg AL. Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles. J Clin Invest 1997; 100:197-203.
    • (1997) J Clin Invest , vol.100 , pp. 197-203
    • Tawa Jr, N.E.1    Odessey, R.2    Goldberg, A.L.3
  • 35
    • 0347285363 scopus 로고    scopus 로고
    • Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression
    • Lecker SH, Jagoe RT, Gilbert A, et al. Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression. FASEB J 2004; 18:39-51.
    • (2004) FASEB J , vol.18 , pp. 39-51
    • Lecker, S.H.1    Jagoe, R.T.2    Gilbert, A.3
  • 36
    • 0035941020 scopus 로고    scopus 로고
    • Identification of ubiquitin ligases required for skeletal muscle atrophy
    • Bodine SC, Latres E, Baumhueter S, et al. Identification of ubiquitin ligases required for skeletal muscle atrophy. Science 2001; 294:1704-1708.
    • (2001) Science , vol.294 , pp. 1704-1708
    • Bodine, S.C.1    Latres, E.2    Baumhueter, S.3
  • 37
    • 0035807969 scopus 로고    scopus 로고
    • Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
    • Gomes MD, Lecker SH, Jagoe RT, et al. Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proc Natl Acad Sci USA 2001; 98:14440-14445.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14440-14445
    • Gomes, M.D.1    Lecker, S.H.2    Jagoe, R.T.3
  • 38
    • 0035793703 scopus 로고    scopus 로고
    • Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain
    • Centner T, Yano J, Kimura E, et al. Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain. J Mol Biol 2001; 306:717-726.
    • (2001) J Mol Biol , vol.306 , pp. 717-726
    • Centner, T.1    Yano, J.2    Kimura, E.3
  • 39
    • 11144237310 scopus 로고    scopus 로고
    • Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I
    • Kedar V, McDonough H, Arya R, et al. Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I. Proc Natl Acad Sci USA 2004; 101:18135-18140.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 18135-18140
    • Kedar, V.1    McDonough, H.2    Arya, R.3
  • 40
    • 35548973391 scopus 로고    scopus 로고
    • The E3 ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle
    • Identification of the mechanism by which myosin heavy chain is degraded under atrophy conditions
    • Clarke BA, Drujan D, Willis MS, et al. The E3 ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle. Cell Metab 2007; 6:376-385. Identification of the mechanism by which myosin heavy chain is degraded under atrophy conditions.
    • (2007) Cell Metab , vol.6 , pp. 376-385
    • Clarke, B.A.1    Drujan, D.2    Willis, M.S.3
  • 41
    • 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 2004; 287:E591-E601.
    • (2004) Am J Physiol Endocrinol Metab , vol.287
    • Sacheck, J.M.1    Ohtsuka, A.2    McLary, S.C.3    Goldberg, A.L.4
  • 42
    • 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, 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 2004; 279:41114-41123.
    • (2004) J Biol Chem , vol.279 , pp. 41114-41123
    • Kamei, Y.1    Miura, S.2    Suzuki, M.3
  • 43
    • 35948935327 scopus 로고    scopus 로고
    • Ubiquitination, phosphorylation, and acetylation: Triple threat in muscle wasting
    • Interesting review underscoring the role of posttranslational modifications of proteins involved in muscle atrophy and in the modulation of their activity
    • Hasselgren P. Ubiquitination, phosphorylation, and acetylation: triple threat in muscle wasting. J Cell Physiol 2007; 213:679-689. Interesting review underscoring the role of posttranslational modifications of proteins involved in muscle atrophy and in the modulation of their activity.
    • (2007) J Cell Physiol , vol.213 , pp. 679-689
    • Hasselgren, P.1
  • 44
    • 0022178181 scopus 로고
    • Cachectin/tumor necrosis factor: Production, distribution, and metabolic fate in vivo
    • Beutler BA, Milsark IW, Cerami A. Cachectin/tumor necrosis factor: production, distribution, and metabolic fate in vivo. J Immunol 1985; 135:3972-3977.
    • (1985) J Immunol , vol.135 , pp. 3972-3977
    • Beutler, B.A.1    Milsark, I.W.2    Cerami, A.3
  • 45
    • 0035020963 scopus 로고    scopus 로고
    • Inflammatory cytokines inhibit myogenic differentiation through activation of nuclear factor-kappaB
    • Langen RC, Schols AM, Kelders MC, et al. Inflammatory cytokines inhibit myogenic differentiation through activation of nuclear factor-kappaB. FASEB J 2001; 15:1169-1180.
    • (2001) FASEB J , vol.15 , pp. 1169-1180
    • Langen, R.C.1    Schols, A.M.2    Kelders, M.C.3
  • 46
    • 5444262078 scopus 로고    scopus 로고
    • IKKbeta/NF-kappaB activation causes severe muscle wasting in mice
    • Cai D, Frantz JD, Tawa NE Jr, et al. IKKbeta/NF-kappaB activation causes severe muscle wasting in mice. Cell 2004; 119:285-298.
    • (2004) Cell , vol.119 , pp. 285-298
    • Cai, D.1    Frantz, J.D.2    Tawa Jr, N.E.3
  • 47
    • 33750595325 scopus 로고    scopus 로고
    • Targeted ablation of IKK2 improves skeletal muscle strength, maintains mass, and promotes regeneration
    • Mourkioti F, Kratsios P, Luedde T, et al. Targeted ablation of IKK2 improves skeletal muscle strength, maintains mass, and promotes regeneration. J Clin Invest 2006; 116:2945-2954.
    • (2006) J Clin Invest , vol.116 , pp. 2945-2954
    • Mourkioti, F.1    Kratsios, P.2    Luedde, T.3
  • 48
    • 0034730251 scopus 로고    scopus 로고
    • NF-kappaB-induced loss of MyoD messenger RNA: Possible role in muscle decay and cachexia
    • Guttridge DC, Mayo MW, Madrid LV, et al. NF-kappaB-induced loss of MyoD messenger RNA: possible role in muscle decay and cachexia. Science 2000; 289:2363-2366.
    • (2000) Science , vol.289 , pp. 2363-2366
    • Guttridge, D.C.1    Mayo, M.W.2    Madrid, L.V.3
  • 49
    • 14644400387 scopus 로고    scopus 로고
    • TNF-alpha acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle
    • Li YP, Chen Y, John J, et al. TNF-alpha acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle. FASEB J 2005; 19:362-370.
    • (2005) FASEB J , vol.19 , pp. 362-370
    • Li, Y.P.1    Chen, Y.2    John, J.3
  • 50
    • 2942662046 scopus 로고    scopus 로고
    • NF-kappaB activation and iNOS upregulation in skeletal muscle of patients with COPD and low body weight
    • Agust́ A, Morlá M, Sauleda J, et al. NF-kappaB activation and iNOS upregulation in skeletal muscle of patients with COPD and low body weight. Thorax 2004; 59:483-487.
    • (2004) Thorax , vol.59 , pp. 483-487
    • Agust́, A.1    Morlá, M.2    Sauleda, J.3
  • 51
    • 34848913758 scopus 로고    scopus 로고
    • NO production results in suspension-induced muscle atrophy through dislocation of neuronal NOS
    • Involvement of nNOS/NO in the regulation of FOXO in muscle atrophy
    • Suzuki N, Motohashi N, Uezumi A, et al. NO production results in suspension-induced muscle atrophy through dislocation of neuronal NOS. J Clin Invest 2007; 117:2468-2476. Involvement of nNOS/NO in the regulation of FOXO in muscle atrophy.
    • (2007) J Clin Invest , vol.117 , pp. 2468-2476
    • Suzuki, N.1    Motohashi, N.2    Uezumi, A.3
  • 52
    • 34547999356 scopus 로고    scopus 로고
    • Characterization of 5′-regulatory region of human myostatin gene: Regulation by dexamethasone in vitro
    • Ma K, Mallidis C, Artaza J, et al. Characterization of 5′-regulatory region of human myostatin gene: regulation by dexamethasone in vitro. Am J Physiol Endocrinol Metab 2001; 281:E1128-E1136.
    • (2001) Am J Physiol Endocrinol Metab , vol.281
    • Ma, K.1    Mallidis, C.2    Artaza, J.3
  • 53
    • 33845905819 scopus 로고    scopus 로고
    • Myostatin gene deletion prevents glucocorticoid-induced muscle atrophy
    • This paper suggests an important role of myostatin in muscle atrophy caused by glucocorticoids
    • Gilson H, Schakman O, Combaret L, et al. Myostatin gene deletion prevents glucocorticoid-induced muscle atrophy. Endocrinology 2007; 148:452-460. This paper suggests an important role of myostatin in muscle atrophy caused by glucocorticoids.
    • (2007) Endocrinology , vol.148 , pp. 452-460
    • Gilson, H.1    Schakman, O.2    Combaret, L.3
  • 54
    • 33846332013 scopus 로고    scopus 로고
    • Regulation of myostatin expression and myoblast differentiation by FoxO and SMAD transcription factors
    • Role of FOXO1 and SMAD transcription factors in the regulation of myostatin the expression
    • Allen DL, Unterman TG. Regulation of myostatin expression and myoblast differentiation by FoxO and SMAD transcription factors. Am J Physiol Cell Physiol 2007; 292:C188-C199. Role of FOXO1 and SMAD transcription factors in the regulation of myostatin the expression.
    • (2007) Am J Physiol Cell Physiol , vol.292
    • Allen, D.L.1    Unterman, T.G.2
  • 55
    • 34447628323 scopus 로고    scopus 로고
    • Loss of skeletal muscle mass in aging: Examining the relationship of starvation, sarcopenia and cachexia
    • Review examining how different forms of atrophy are linked
    • Thomas DR. Loss of skeletal muscle mass in aging: examining the relationship of starvation, sarcopenia and cachexia. Clin Nutr 2007; 26:389-399. Review examining how different forms of atrophy are linked.
    • (2007) Clin Nutr , vol.26 , pp. 389-399
    • Thomas, D.R.1
  • 56
    • 0041353459 scopus 로고    scopus 로고
    • Global analysis of gene expression patterns during disuse atrophy in rat skeletal muscle
    • Stevenson EJ, Giresi PG, Koncarevic A, Kandarian SC. Global analysis of gene expression patterns during disuse atrophy in rat skeletal muscle. J Physiol 2003; 551 (Pt 1):33-48.
    • (2003) J Physiol , vol.551 , Issue.PART 1 , pp. 33-48
    • Stevenson, E.J.1    Giresi, P.G.2    Koncarevic, A.3    Kandarian, S.C.4
  • 57
    • 19344372609 scopus 로고    scopus 로고
    • Response of the ubiquitin-proteasome pathway to changes in muscle activity
    • Reid MB. Response of the ubiquitin-proteasome pathway to changes in muscle activity. Am J Physiol Regul Integr Comp Physiol 2005; 288:R1423-R1431.
    • (2005) Am J Physiol Regul Integr Comp Physiol , vol.288
    • Reid, M.B.1
  • 58
    • 0036208356 scopus 로고    scopus 로고
    • Activation of an alternative NF-kappaB pathway in skeletal muscle during disuse atrophy
    • Hunter RB, Stevenson E, Koncarevic A, et al. Activation of an alternative NF-kappaB pathway in skeletal muscle during disuse atrophy. FASEB J 2002; 16:529-538.
    • (2002) FASEB J , vol.16 , pp. 529-538
    • Hunter, R.B.1    Stevenson, E.2    Koncarevic, A.3
  • 59
    • 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 2004; 114:1504-1511.
    • (2004) J Clin Invest , vol.114 , pp. 1504-1511
    • Hunter, R.B.1    Kandarian, S.C.2
  • 60
    • 0031802331 scopus 로고    scopus 로고
    • Skeletal muscle myocytes undergo protein loss and reactive oxygen-mediated NF-kappaB activation in response to tumor necrosis factor alpha
    • Li YP, Schwartz RJ, Waddell ID, et al. Skeletal muscle myocytes undergo protein loss and reactive oxygen-mediated NF-kappaB activation in response to tumor necrosis factor alpha. FASEB J 1998; 12:871-880.
    • (1998) FASEB J , vol.12 , pp. 871-880
    • Li, Y.P.1    Schwartz, R.J.2    Waddell, I.D.3
  • 61
    • 0037178789 scopus 로고    scopus 로고
    • FOXO forkhead transcription factors induce G(2)-M checkpoint in response to oxidative stress
    • Furukawa-Hibi Y, Yoshida-Araki K, Ohta T, et al. FOXO forkhead transcription factors induce G(2)-M checkpoint in response to oxidative stress. J Biol Chem 2002; 277:26729-26732.
    • (2002) J Biol Chem , vol.277 , pp. 26729-26732
    • Furukawa-Hibi, Y.1    Yoshida-Araki, K.2    Ohta, T.3
  • 62
    • 0030968884 scopus 로고    scopus 로고
    • Sarcopenia: Origins and clinical relevance
    • Rosenberg IH. Sarcopenia: origins and clinical relevance. J Nutr 1997; 127 (Suppl 5):990S-991S.
    • (1997) J Nutr , vol.127 , Issue.SUPPL. 5
    • Rosenberg, I.H.1
  • 63
    • 0027954066 scopus 로고
    • The ratio between serum levels of insulin-like growth factor (IGF)-I and the IGF binding proteins (IGFBP-1, 2 and 3) decreases with age in healthy adults and is increased in acromegalic patients
    • Juul A, Main K, Blum WF, et al. The ratio between serum levels of insulin-like growth factor (IGF)-I and the IGF binding proteins (IGFBP-1, 2 and 3) decreases with age in healthy adults and is increased in acromegalic patients. Clin Endocrinol (Oxf) 1994; 41:85-93.
    • (1994) Clin Endocrinol (Oxf) , vol.41 , pp. 85-93
    • Juul, A.1    Main, K.2    Blum, W.F.3
  • 64
    • 0036544519 scopus 로고    scopus 로고
    • Muscle-specific expression of insulin-like growth factor I counters muscle decline in mdx mice
    • Barton ER, Morris L, Musaro A, et al. Muscle-specific expression of insulin-like growth factor I counters muscle decline in mdx mice. J Cell Biol 2002; 157:137-148.
    • (2002) J Cell Biol , vol.157 , pp. 137-148
    • Barton, E.R.1    Morris, L.2    Musaro, A.3
  • 65
    • 0031030941 scopus 로고    scopus 로고
    • Effect of rhGH and rhIGF-I treatment on protein utilization in elderly women
    • Butterfield GE, Thompson J, Rennie MJ, et al. Effect of rhGH and rhIGF-I treatment on protein utilization in elderly women. Am J Physiol 1997; 272 (1 Pt 1):E94-E99.
    • (1997) Am J Physiol , vol.272 , Issue.1 PART 1
    • Butterfield, G.E.1    Thompson, J.2    Rennie, M.J.3
  • 66
    • 33845320200 scopus 로고    scopus 로고
    • Experience with testosterone replacement in the elderly. [discussion S82]
    • Tenover JL. Experience with testosterone replacement in the elderly. [discussion S82]. Mayo Clin Proc 2000; (Suppl 75):S77-S81.
    • (2000) Mayo Clin Proc , Issue.SUPPL. 75
    • Tenover, J.L.1
  • 67
    • 33747641590 scopus 로고    scopus 로고
    • Effects of testosterone supplementation on skeletal muscle fiber hypertrophy and satellite cells in community-dwelling older men
    • Sinha-Hikim I, Cornford M, Gaytan H, et al. Effects of testosterone supplementation on skeletal muscle fiber hypertrophy and satellite cells in community-dwelling older men. J Clin Endocrinol Metab 2006; 91:3024-3033.
    • (2006) J Clin Endocrinol Metab , vol.91 , pp. 3024-3033
    • Sinha-Hikim, I.1    Cornford, M.2    Gaytan, H.3
  • 68
    • 25444478907 scopus 로고    scopus 로고
    • Aging, stem cells and tissue regeneration: Lessons from muscle
    • Conboy IM, Rando TA. Aging, stem cells and tissue regeneration: lessons from muscle. Cell Cycle 2005; 4:407-410.
    • (2005) Cell Cycle , vol.4 , pp. 407-410
    • Conboy, I.M.1    Rando, T.A.2
  • 69
    • 0344827208 scopus 로고    scopus 로고
    • Notch-mediated restoration of regenerative potential to aged muscle
    • Conboy IM, Conboy MJ, Smythe GM, Rando TA. Notch-mediated restoration of regenerative potential to aged muscle. Science 2003; 302:1575-1577.
    • (2003) Science , vol.302 , pp. 1575-1577
    • Conboy, I.M.1    Conboy, M.J.2    Smythe, G.M.3    Rando, T.A.4
  • 70
    • 0036744815 scopus 로고    scopus 로고
    • The regulation of Notch signaling controls satellite cell activation and cell fate determination in postnatal myogenesis
    • Conboy IM, Rando TA. The regulation of Notch signaling controls satellite cell activation and cell fate determination in postnatal myogenesis. Dev Cell 2002; 3:397-409.
    • (2002) Dev Cell , vol.3 , pp. 397-409
    • Conboy, I.M.1    Rando, T.A.2
  • 71
    • 13944261231 scopus 로고    scopus 로고
    • Rejuvenation of aged progenitor cells by exposure to a young systemic environment
    • Conboy IM, Conboy MJ, Wagers AJ, et al. Rejuvenation of aged progenitor cells by exposure to a young systemic environment. Nature 2005; 433:760-764.
    • (2005) Nature , vol.433 , pp. 760-764
    • Conboy, I.M.1    Conboy, M.J.2    Wagers, A.J.3
  • 72
    • 0023856536 scopus 로고
    • What is the cause of the ageing atrophy? Total number, size and proportion of different fiber types studied in whole vastus lateralis muscle from 15- to 83-year-old men
    • Lexell J, Taylor CC, Sjöström M. What is the cause of the ageing atrophy? Total number, size and proportion of different fiber types studied in whole vastus lateralis muscle from 15- to 83-year-old men. J Neurol Sci 1988; 84:275-294.
    • (1988) J Neurol Sci , vol.84 , pp. 275-294
    • Lexell, J.1    Taylor, C.C.2    Sjöström, M.3
  • 73
    • 0034996561 scopus 로고    scopus 로고
    • Age effect on transcript levels and synthesis rate of muscle MHC and response to resistance exercise
    • Balagopal P, Schimke JC, Ades P, et al. Age effect on transcript levels and synthesis rate of muscle MHC and response to resistance exercise. Am J Physiol Endocrinol Metab 2001; 280:E203-E208.
    • (2001) Am J Physiol Endocrinol Metab , vol.280
    • Balagopal, P.1    Schimke, J.C.2    Ades, P.3
  • 74
    • 14844328611 scopus 로고    scopus 로고
    • Tissue-specific regulation of metabolic pathways through the transcriptional coactivator PGC1-alpha
    • Puigserver P. Tissue-specific regulation of metabolic pathways through the transcriptional coactivator PGC1-alpha. Int J Obes (Lond) 2005; 29 (Suppl 1):S5-S9.
    • (2005) Int J Obes (Lond) , vol.29 , Issue.SUPPL. 1
    • Puigserver, P.1
  • 75
    • 0037102256 scopus 로고    scopus 로고
    • Transcriptional co-activator PGC-1 alpha drives the formation of slow-twitch muscle fibres
    • Lin J, Wu H, Tarr PT, et al. Transcriptional co-activator PGC-1 alpha drives the formation of slow-twitch muscle fibres. Nature 2002; 418:797-801.
    • (2002) Nature , vol.418 , pp. 797-801
    • Lin, J.1    Wu, H.2    Tarr, P.T.3
  • 76
    • 33750825245 scopus 로고    scopus 로고
    • PGC-1alpha protects skeletal muscle from atrophy by suppressing FoxO3 action and atrophy-specific gene transcription
    • Sandri M, Lin J, Handschin C, et al. PGC-1alpha protects skeletal muscle from atrophy by suppressing FoxO3 action and atrophy-specific gene transcription. Proc Natl Acad Sci USA 2006; 103:16260-16265.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 16260-16265
    • Sandri, M.1    Lin, J.2    Handschin, C.3
  • 77
    • 0036165434 scopus 로고    scopus 로고
    • MEF2: A calcium-dependent regulator of cell division, differentiation and death
    • McKinsey TA, Zhang CL, Olson EN. MEF2: a calcium-dependent regulator of cell division, differentiation and death. Trends Biochem Sci 2002; 27:40-47.
    • (2002) Trends Biochem Sci , vol.27 , pp. 40-47
    • McKinsey, T.A.1    Zhang, C.L.2    Olson, E.N.3
  • 78
    • 33646871787 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations, energy metabolism and apoptosis in aging muscle
    • Dirks AJ, Hofer T, Marzetti E, et al. Mitochondrial DNA mutations, energy metabolism and apoptosis in aging muscle. Ageing Res Rev 2006; 5:179-195.
    • (2006) Ageing Res Rev , vol.5 , pp. 179-195
    • Dirks, A.J.1    Hofer, T.2    Marzetti, E.3
  • 80
    • 35448962512 scopus 로고    scopus 로고
    • Involvement of the calcium-dependent proteolytic system in skeletal muscle aging
    • This paper presents evidence of the implication of calpains in sarcopenia
    • Dargelos E, Brulé C, Combaret L, et al. Involvement of the calcium-dependent proteolytic system in skeletal muscle aging. Exp Gerontol 2007; 42:1088-1098. This paper presents evidence of the implication of calpains in sarcopenia.
    • (2007) Exp Gerontol , vol.42 , pp. 1088-1098
    • Dargelos, E.1    Brulé, C.2    Combaret, L.3
  • 81
    • 0036830917 scopus 로고    scopus 로고
    • Cachexia in cancer patients
    • Tisdale MJ. Cachexia in cancer patients. Nat Rev Cancer 2002; 2:862-871.
    • (2002) Nat Rev Cancer , vol.2 , pp. 862-871
    • Tisdale, M.J.1
  • 82
    • 17844393368 scopus 로고    scopus 로고
    • Skeletal muscle cytokines: Regulation by pathogen-associated molecules and catabolic hormones
    • Frost RA, Lang CH. Skeletal muscle cytokines: regulation by pathogen-associated molecules and catabolic hormones. Curr Opin Clin Nutr Metab Care 2005; 8:255-263.
    • (2005) Curr Opin Clin Nutr Metab Care , vol.8 , pp. 255-263
    • Frost, R.A.1    Lang, C.H.2
  • 83
    • 0035161185 scopus 로고    scopus 로고
    • Effect of tumor necrosis factor-alpha on skeletal muscle metabolism
    • Li YP, Reid MB. Effect of tumor necrosis factor-alpha on skeletal muscle metabolism. Curr Opin Rheumatol 2001; 13:483-487.
    • (2001) Curr Opin Rheumatol , vol.13 , pp. 483-487
    • Li, Y.P.1    Reid, M.B.2
  • 84
    • 0036295676 scopus 로고    scopus 로고
    • Molecular regulation of muscle cachexia: It may be more than the proteasome
    • Hasselgren PO, Wray C, Mammen J. Molecular regulation of muscle cachexia: it may be more than the proteasome. Biochem Biophys Res Commun 2002; 290:1-10.
    • (2002) Biochem Biophys Res Commun , vol.290 , pp. 1-10
    • Hasselgren, P.O.1    Wray, C.2    Mammen, J.3
  • 85
    • 0037083867 scopus 로고    scopus 로고
    • TNFalpha inhibits skeletal myogenesis through a PW1-dependent pathway by recruitment of caspase pathways
    • Coletti D, Yang E, Marazzi G, Sassoon D. TNFalpha inhibits skeletal myogenesis through a PW1-dependent pathway by recruitment of caspase pathways. EMBO J 2002; 21:631-642.
    • (2002) EMBO J , vol.21 , pp. 631-642
    • Coletti, D.1    Yang, E.2    Marazzi, G.3    Sassoon, D.4
  • 86
    • 33845697226 scopus 로고    scopus 로고
    • Muscle cachexia is regulated by a p53-PW1/Peg3-dependent pathway
    • Schwarzkopf M, Coletti D, Sassoon D, Marazzi G. Muscle cachexia is regulated by a p53-PW1/Peg3-dependent pathway. Genes Dev 2006; 20:3440-3452.
    • (2006) Genes Dev , vol.20 , pp. 3440-3452
    • Schwarzkopf, M.1    Coletti, D.2    Sassoon, D.3    Marazzi, G.4
  • 87
    • 9244254305 scopus 로고    scopus 로고
    • Skeletal muscle atrophy is associated with an increased expression of myostatin and impaired satellite cell function in the portacaval anastamosis rat
    • Dasarathy S, Dodig M, Muc SM, et al. Skeletal muscle atrophy is associated with an increased expression of myostatin and impaired satellite cell function in the portacaval anastamosis rat. Am J Physiol Gastrointest Liver Physiol 2004; 287:G1124-G1130.
    • (2004) Am J Physiol Gastrointest Liver Physiol , vol.287
    • Dasarathy, S.1    Dodig, M.2    Muc, S.M.3
  • 88
    • 28844451913 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha gene transfer induces cachexia and inhibits muscle regeneration
    • Coletti D, Moresi V, Adamo S, et al. Tumor necrosis factor-alpha gene transfer induces cachexia and inhibits muscle regeneration. Genesis 2005; 43:120-128.
    • (2005) Genesis , vol.43 , pp. 120-128
    • Coletti, D.1    Moresi, V.2    Adamo, S.3
  • 89
    • 27644471080 scopus 로고    scopus 로고
    • Dystrophin glycoprotein complex dysfunction: A regulatory link between muscular dystrophy and cancer cachexia
    • Acharyya S, Butchbach ME, Sahenk Z, et al. Dystrophin glycoprotein complex dysfunction: a regulatory link between muscular dystrophy and cancer cachexia. Cancer Cell 2005; 8:421-432.
    • (2005) Cancer Cell , vol.8 , pp. 421-432
    • Acharyya, S.1    Butchbach, M.E.2    Sahenk, Z.3
  • 90
    • 0036591684 scopus 로고    scopus 로고
    • Muscular dystrophies involving the dystrophin-glycoprotein complex: An overview of current mouse models
    • Durbeej M, Campbell KP. Muscular dystrophies involving the dystrophin-glycoprotein complex: an overview of current mouse models. Curr Opin Genet Dev 2002; 12:349-361.
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 349-361
    • Durbeej, M.1    Campbell, K.P.2
  • 91
    • 0036842214 scopus 로고    scopus 로고
    • Inhibition of dystroglycan binding to laminin disrupts the PI3K/AKT pathway and survival signaling in muscle cells
    • Langenbach KJ, Rando TA. Inhibition of dystroglycan binding to laminin disrupts the PI3K/AKT pathway and survival signaling in muscle cells. Muscle Nerve 2002; 26:644-653.
    • (2002) Muscle Nerve , vol.26 , pp. 644-653
    • Langenbach, K.J.1    Rando, T.A.2
  • 92
    • 33745894322 scopus 로고    scopus 로고
    • rAAV6-microdystrophin preserves muscle function and extends lifespan in severely dystrophic mice
    • Gregorevic P, Allen JM, Minami E, et al. rAAV6-microdystrophin preserves muscle function and extends lifespan in severely dystrophic mice. Nat Med 2006; 12:787-789.
    • (2006) Nat Med , vol.12 , pp. 787-789
    • Gregorevic, P.1    Allen, J.M.2    Minami, E.3
  • 93
    • 0030070765 scopus 로고    scopus 로고
    • Nitric oxide synthase I (NOS-I) is deficient in the sarcolemma of striated muscle fibers in patients with Duchenne muscular dystrophy, suggesting an association with dystrophin
    • Grozdanovic Z, Gosztonyi G, Gossrau R. Nitric oxide synthase I (NOS-I) is deficient in the sarcolemma of striated muscle fibers in patients with Duchenne muscular dystrophy, suggesting an association with dystrophin. Acta Histochem 1996; 98:61-69.
    • (1996) Acta Histochem , vol.98 , pp. 61-69
    • Grozdanovic, Z.1    Gosztonyi, G.2    Gossrau, R.3
  • 94
    • 0036845662 scopus 로고    scopus 로고
    • Loss of sarcolemma nNOS in sarcoglycan-deficient muscle
    • Crosbie RH, Barresi R, Campbell KP. Loss of sarcolemma nNOS in sarcoglycan-deficient muscle. FASEB J 2002; 16:1786-1791.
    • (2002) FASEB J , vol.16 , pp. 1786-1791
    • Crosbie, R.H.1    Barresi, R.2    Campbell, K.P.3
  • 95
    • 36249025723 scopus 로고    scopus 로고
    • Autophagy: Process and function
    • Review describing the process of autophagy and its role in cell metabolism
    • Mizushima N. Autophagy: process and function. Genes Dev 2007; 21:2861-2873. Review describing the process of autophagy and its role in cell metabolism.
    • (2007) Genes Dev , vol.21 , pp. 2861-2873
    • Mizushima, N.1
  • 96
    • 27644493346 scopus 로고    scopus 로고
    • The pleiotropic role of autophagy: From protein metabolism to bactericide
    • Mizushima N. The pleiotropic role of autophagy: from protein metabolism to bactericide. Cell Death Differ 2005; 12 (Suppl 2):1535-1541.
    • (2005) Cell Death Differ , vol.12 , Issue.SUPPL. 2 , pp. 1535-1541
    • Mizushima, N.1
  • 98
    • 0347579841 scopus 로고    scopus 로고
    • Lysosomal dysfunction in muscle with special reference to glycogen storage disease type II
    • Hesselink RP, Wagenmakers AJ, Drost MR, et al. Lysosomal dysfunction in muscle with special reference to glycogen storage disease type II. Biochim Biophys Acta 2003; 1637:164-170.
    • (2003) Biochim Biophys Acta , vol.1637 , pp. 164-170
    • Hesselink, R.P.1    Wagenmakers, A.J.2    Drost, M.R.3
  • 99
    • 17044440789 scopus 로고    scopus 로고
    • Primary LAMP-2 deficiency causes X-linked vacuolar cardiomyopathy and myopathy (Danon disease)
    • Nishino I, Fu J, Tanji K, et al. Primary LAMP-2 deficiency causes X-linked vacuolar cardiomyopathy and myopathy (Danon disease). Nature 2000; 406:906-910.
    • (2000) Nature , vol.406 , pp. 906-910
    • Nishino, I.1    Fu, J.2    Tanji, K.3
  • 100
    • 33749261091 scopus 로고    scopus 로고
    • Autophagic vacuolar myopathy
    • Nishino I. Autophagic vacuolar myopathy. Semin Pediatr Neurol 2006; 13:90-95.
    • (2006) Semin Pediatr Neurol , vol.13 , pp. 90-95
    • Nishino, I.1
  • 102
    • 33846015010 scopus 로고    scopus 로고
    • Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases
    • This paper shows that the atrophy associated with systemic catabolic states and following disuse involves the induction of similar transcription patterns
    • Sacheck JM, Hyatt JP, Raffaello A, et al. Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases. FASEB J 2007; 21:140-155. This paper shows that the atrophy associated with systemic catabolic states and following disuse involves the induction of similar transcription patterns.
    • (2007) FASEB J , vol.21 , pp. 140-155
    • Sacheck, J.M.1    Hyatt, J.P.2    Raffaello, A.3
  • 103
    • 34249096247 scopus 로고    scopus 로고
    • Gene expression profiling identifies FKBP39 as an inhibitor of autophagy in larval Drosophila fat body
    • Evidence of the role of FOXO in modulating autophagy in Drosophila
    • Juhász G, Puskás LG, Komonyi O, et al. Gene expression profiling identifies FKBP39 as an inhibitor of autophagy in larval Drosophila fat body. Cell Death Differ 2007; 14:1181-1190. Evidence of the role of FOXO in modulating autophagy in Drosophila.
    • (2007) Cell Death Differ , vol.14 , pp. 1181-1190
    • Juhász, G.1    Puskás, L.G.2    Komonyi, O.3
  • 104
    • 36448940798 scopus 로고    scopus 로고
    • FoxO3 controls autophagy in skeletal muscle in vivo
    • Mammucari C, Milan G, Romanello V, et al. FoxO3 controls autophagy in skeletal muscle in vivo. Cell Metab 2007; 6:458-471.
    • (2007) Cell Metab , vol.6 , pp. 458-471
    • Mammucari, C.1    Milan, G.2    Romanello, V.3
  • 105
    • 36448968532 scopus 로고    scopus 로고
    • FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells
    • These two papers demonstrate the involvement of autophagy in muscle atrophy, and most importantly, define FOXO as a key mediator of both proteolysis and autophagy
    • Zhao J, Brault JJ, Schild A, et al. FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab 2007; 6:472-483. These two papers demonstrate the involvement of autophagy in muscle atrophy, and most importantly, define FOXO as a key mediator of both proteolysis and autophagy.
    • (2007) Cell Metab , vol.6 , pp. 472-483
    • Zhao, J.1    Brault, J.J.2    Schild, A.3
  • 106
    • 0037470501 scopus 로고    scopus 로고
    • The endocrine regulation of aging by insulin-like signals
    • Tatar M, Bartke A, Antebi A. The endocrine regulation of aging by insulin-like signals. Science 2003; 299:1346-1351.
    • (2003) Science , vol.299 , pp. 1346-1351
    • Tatar, M.1    Bartke, A.2    Antebi, A.3
  • 107
    • 0042092531 scopus 로고    scopus 로고
    • Genes that act downstream of DAF-16 to influence the lifespan of caenorhabditis elegans
    • Murphy CT, McCarroll SA, Bargmann CI, et al. Genes that act downstream of DAF-16 to influence the lifespan of caenorhabditis elegans. Nature 2003; 424:277-283.
    • (2003) Nature , vol.424 , pp. 277-283
    • Murphy, C.T.1    McCarroll, S.A.2    Bargmann, C.I.3
  • 108
    • 33744976074 scopus 로고    scopus 로고
    • Berdichevsky A, Viswanathan M, Horvitz HR, Guarente L. C. elegans SIR-2.1 interacts with 14-3-3 proteins to activate DAF-16 and extend life span. Cell 2006; 125:1165-1177.
    • Berdichevsky A, Viswanathan M, Horvitz HR, Guarente L. C. elegans SIR-2.1 interacts with 14-3-3 proteins to activate DAF-16 and extend life span. Cell 2006; 125:1165-1177.
  • 109
    • 0042691506 scopus 로고    scopus 로고
    • Autophagy genes are essential for dauer development and life-span extension in C. elegans
    • Meléndez A, Tallóczy Z, Seaman M, et al. Autophagy genes are essential for dauer development and life-span extension in C. elegans. Science 2003; 301:1387-1391.
    • (2003) Science , vol.301 , pp. 1387-1391
    • Meléndez, A.1    Tallóczy, Z.2    Seaman, M.3
  • 110
    • 30344477367 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer
    • Minucci S, Pelicci PG. Histone deacetylase inhibitors and the promise of epigenetic (and more) treatments for cancer. Nat Rev Cancer 2006; 1:38-45.
    • (2006) Nat Rev Cancer , vol.1 , pp. 38-45
    • Minucci, S.1    Pelicci, P.G.2
  • 111
    • 0035909330 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in drosophila
    • Steffan JS, Bodai L, Pallos J, et al. Histone deacetylase inhibitors arrest polyglutamine-dependent neurodegeneration in drosophila. Nature 2001; 413:739-744.
    • (2001) Nature , vol.413 , pp. 739-744
    • Steffan, J.S.1    Bodai, L.2    Pallos, J.3
  • 112
    • 2942733520 scopus 로고    scopus 로고
    • Sodium butyrate ameliorates phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy
    • Minamiyama M, Katsuno M, Adachi H, et al. Sodium butyrate ameliorates phenotypic expression in a transgenic mouse model of spinal and bulbar muscular atrophy. Hum Mol Genet 2004; 11:1183-1192.
    • (2004) Hum Mol Genet , vol.11 , pp. 1183-1192
    • Minamiyama, M.1    Katsuno, M.2    Adachi, H.3
  • 113
    • 34548748173 scopus 로고    scopus 로고
    • The pharmaceutical potential of histone deacetylase inhibitors
    • Review on the pharmacological relevance of the use of histone deacetylase inhibitors in the treatment of human disorders
    • Elaut G, Rogiers V, Vanhaecke T. The pharmaceutical potential of histone deacetylase inhibitors. Curr Pharm Des 2007; 13:2584-2662. Review on the pharmacological relevance of the use of histone deacetylase inhibitors in the treatment of human disorders.
    • (2007) Curr Pharm Des , vol.13 , pp. 2584-2662
    • Elaut, G.1    Rogiers, V.2    Vanhaecke, T.3
  • 114
    • 33749507982 scopus 로고    scopus 로고
    • Functional and morphological recovery of dystrophic muscles in mice treated with deacetylase inhibitors
    • Minetti GC, Colussi C, Adami R, et al. Functional and morphological recovery of dystrophic muscles in mice treated with deacetylase inhibitors. Nat Med 2006; 10:1147-1155.
    • (2006) Nat Med , vol.10 , pp. 1147-1155
    • Minetti, G.C.1    Colussi, C.2    Adami, R.3
  • 115
    • 0037188532 scopus 로고    scopus 로고
    • Stage-specific modulation of skeletal myogenesis by inhibitors of nuclear deacetylases
    • Iezzi S, Cossu G, Nervi C, et al. Stage-specific modulation of skeletal myogenesis by inhibitors of nuclear deacetylases. Proc Natl Acad Sci USA 2002; 11:7757-7766.
    • (2002) Proc Natl Acad Sci USA , vol.11 , pp. 7757-7766
    • Iezzi, S.1    Cossu, G.2    Nervi, C.3
  • 116
    • 2342627231 scopus 로고    scopus 로고
    • Deacetylase inhibitors increase muscle cell size by promoting myoblast recruitment and fusion through induction of follistatin
    • Iezzi S, Di Padova M, Serra C, et al. Deacetylase inhibitors increase muscle cell size by promoting myoblast recruitment and fusion through induction of follistatin. Dev Cell 2004; 5:673-684.
    • (2004) Dev Cell , vol.5 , pp. 673-684
    • Iezzi, S.1    Di Padova, M.2    Serra, C.3
  • 117
    • 33845997798 scopus 로고    scopus 로고
    • Suberoylanilide hydroxamic acid induces Akt-mediated phosphorylation of p300, which promotes acetylation and transcriptional activation of RelA/p65
    • Liu Y, Denlinger CE, Rundall BK, et al. Suberoylanilide hydroxamic acid induces Akt-mediated phosphorylation of p300, which promotes acetylation and transcriptional activation of RelA/p65. J Biol Chem 2006; 281:31359-31368.
    • (2006) J Biol Chem , vol.281 , pp. 31359-31368
    • Liu, Y.1    Denlinger, C.E.2    Rundall, B.K.3


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