The TWEAK–Fn14 system is a critical regulator of denervation-induced skeletal muscle atrophy in mice

Ashwani Mittal; Shephali Bhatnagar; Akhilesh Kumar; Estelle Lach-Trifilieff; Sandrine Wauters; Hong Li; Denys Y. Makonchuk; David J. Glass; Ashok Kumar

doi:10.1083/jcb.200909117

The TNF-related cytokine TWEAK promotes skeletal muscle atrophy that is associated with classical disuse syndromes.

Loading next page...

References (112)

R. Hunter, S. Kandarian (2004)
Disruption of either the Nfkb1 or the Bcl3 gene inhibits skeletal muscle atrophy.
The Journal of clinical investigation, 114 10
Masafumi Nakayama, N. Harada, K. Okumura, H. Yagita (2003)
Characterization of murine TWEAK and its receptor (Fn14) by monoclonal antibodies.
Biochemical and biophysical research communications, 306 4
S. Bodine, T. Stitt, Michael Gonzalez, W. Kline, Gretchen Stover, Roy Bauerlein, Elizabeth Zlotchenko, A. Scrimgeour, J. Lawrence, D. Glass, G. Yancopoulos (2001)
Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo
Nature Cell Biology, 3
R. Jackman, S. Kandarian (2004)
The molecular basis of skeletal muscle atrophy.
American journal of physiology. Cell physiology, 287 4
Yvonne Kobayashi, Erik Rader, R. Crawford, Nikhil Iyengar, D. Thedens, J. Faulkner, Swapnesh Parikh, R. Weiss, J. Chamberlain, S. Moore, K. Campbell (2008)
Sarcolemma-localized nNOS is required to maintain activity after mild exercise
Nature, 456
C. Dogra, Harish Changoua, Nia Wedhas, X. Qin, J. Wergedal, Ashok Kumar (2007)
TNF‐related weak inducer of apoptosis (TWEAK) is a potent skeletal muscle‐wasting cytokine
The FASEB Journal, 21
C. Mammucari, G. Milan, V. Romanello, E. Masiero, Ruediger Rudolf, P. Piccolo, S. Burden, R. Lisi, C. Sandri, Jinghui Zhao, A. Goldberg, S. Schiaffino, M. Sandri (2007)
FoxO3 controls autophagy in skeletal muscle in vivo.
Cell metabolism, 6 6
J. Percival, Kendra Anderson, P. Gregorevic, J. Chamberlain, S. Froehner (2008)
Functional Deficits in nNOSμ-Deficient Skeletal Muscle: Myopathy in nNOS Knockout Mice
PLoS ONE, 3
M. Sandri (2008)
Signaling in muscle atrophy and hypertrophy.
Physiology, 23
D. Glass (2005)
Skeletal muscle hypertrophy and atrophy signaling pathways.
The international journal of biochemistry & cell biology, 37 10
(DograC.HallS.L.WedhasN.LinkhartT.A.KumarA. 2007b Fibroblast growth factor inducible 14 (Fn14) is required for the expression of myogenic regulatory factors and differentiation of myoblasts into myotubes. Evidence for TWEAK-independent functions of Fn14 during myogenesis. J. Biol. Chem. 282:15000–15010 10.1074/jbc.M60866820017383968)
DograC.HallS.L.WedhasN.LinkhartT.A.KumarA. 2007b Fibroblast growth factor inducible 14 (Fn14) is required for the expression of myogenic regulatory factors and differentiation of myoblasts into myotubes. Evidence for TWEAK-independent functions of Fn14 during myogenesis. J. Biol. Chem. 282:15000–15010 10.1074/jbc.M60866820017383968
DograC.HallS.L.WedhasN.LinkhartT.A.KumarA. 2007b Fibroblast growth factor inducible 14 (Fn14) is required for the expression of myogenic regulatory factors and differentiation of myoblasts into myotubes. Evidence for TWEAK-independent functions of Fn14 during myogenesis. J. Biol. Chem. 282:15000–15010 10.1074/jbc.M60866820017383968, DograC.HallS.L.WedhasN.LinkhartT.A.KumarA. 2007b Fibroblast growth factor inducible 14 (Fn14) is required for the expression of myogenic regulatory factors and differentiation of myoblasts into myotubes. Evidence for TWEAK-independent functions of Fn14 during myogenesis. J. Biol. Chem. 282:15000–15010 10.1074/jbc.M60866820017383968
K. Tanabe, Iris Bonilla, J. Winkles, S. Strittmatter (2003)
Development / Plasticity / Repair Fibroblast Growth Factor-Inducible-14 Is Induced in Axotomized Neurons and Promotes Neurite Outgrowth
Hong Li, S. Malhotra, Ashok Kumar (2008)
Nuclear factor-kappa B signaling in skeletal muscle atrophy
Journal of Molecular Medicine, 86
(PercivalJ.M.AndersonK.N.GregorevicP.ChamberlainJ.S.FroehnerS.C. 2008 Functional deficits in nNOSmu-deficient skeletal muscle: myopathy in nNOS knockout mice. PLoS One. 3:e3387 10.1371/journal.pone.000338718852886)
PercivalJ.M.AndersonK.N.GregorevicP.ChamberlainJ.S.FroehnerS.C. 2008 Functional deficits in nNOSmu-deficient skeletal muscle: myopathy in nNOS knockout mice. PLoS One. 3:e3387 10.1371/journal.pone.000338718852886
PercivalJ.M.AndersonK.N.GregorevicP.ChamberlainJ.S.FroehnerS.C. 2008 Functional deficits in nNOSmu-deficient skeletal muscle: myopathy in nNOS knockout mice. PLoS One. 3:e3387 10.1371/journal.pone.000338718852886, PercivalJ.M.AndersonK.N.GregorevicP.ChamberlainJ.S.FroehnerS.C. 2008 Functional deficits in nNOSmu-deficient skeletal muscle: myopathy in nNOS knockout mice. PLoS One. 3:e3387 10.1371/journal.pone.000338718852886
D. Glass (2003)
Signalling pathways that mediate skeletal muscle hypertrophy and atrophy
Nature Cell Biology, 5
W. Kline, Frank Panaro, Hayung Yang, S. Bodine (2007)
Rapamycin inhibits the growth and muscle-sparing effects of clenbuterol.
Journal of applied physiology, 102 2
R. Hinkle, K. Hodge, D. Cody, R. Sheldon, B. Kobilka, R. Isfort (2002)
Skeletal muscle hypertrophy and anti‐atrophy effects of clenbuterol are mediated by the β2‐adrenergic receptor
Muscle & Nerve, 25
Shenhav Cohen, J. Brault, S. Gygi, D. Glass, D. Valenzuela, C. Gartner, E. Latres, A. Goldberg (2009)
During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation
The Journal of Cell Biology, 185
(IrizarryR.A.WuZ.JaffeeH.A. 2006 Comparison of Affymetrix GeneChip expression measures. Bioinformatics. 22:789–794 10.1093/bioinformatics/btk04616410320)
IrizarryR.A.WuZ.JaffeeH.A. 2006 Comparison of Affymetrix GeneChip expression measures. Bioinformatics. 22:789–794 10.1093/bioinformatics/btk04616410320
IrizarryR.A.WuZ.JaffeeH.A. 2006 Comparison of Affymetrix GeneChip expression measures. Bioinformatics. 22:789–794 10.1093/bioinformatics/btk04616410320, IrizarryR.A.WuZ.JaffeeH.A. 2006 Comparison of Affymetrix GeneChip expression measures. Bioinformatics. 22:789–794 10.1093/bioinformatics/btk04616410320
(PetteD.StaronR.S. 2001 Transitions of muscle fiber phenotypic profiles. Histochem. Cell Biol. 115:359–37211449884)
PetteD.StaronR.S. 2001 Transitions of muscle fiber phenotypic profiles. Histochem. Cell Biol. 115:359–37211449884
PetteD.StaronR.S. 2001 Transitions of muscle fiber phenotypic profiles. Histochem. Cell Biol. 115:359–37211449884, PetteD.StaronR.S. 2001 Transitions of muscle fiber phenotypic profiles. Histochem. Cell Biol. 115:359–37211449884
B. Blaauw, C. Mammucari, L. Toniolo, L. Agatea, Reimar Abraham, M. Sandri, C. Reggiani, S. Schiaffino (2008)
Akt activation prevents the force drop induced by eccentric contractions in dystrophin-deficient skeletal muscle.
Human molecular genetics, 17 23
(JackmanR.W.KandarianS.C. 2004 The molecular basis of skeletal muscle atrophy. Am. J. Physiol. Cell Physiol. 287:C834–C843 10.1152/ajpcell.00579.200315355854)
JackmanR.W.KandarianS.C. 2004 The molecular basis of skeletal muscle atrophy. Am. J. Physiol. Cell Physiol. 287:C834–C843 10.1152/ajpcell.00579.200315355854
JackmanR.W.KandarianS.C. 2004 The molecular basis of skeletal muscle atrophy. Am. J. Physiol. Cell Physiol. 287:C834–C843 10.1152/ajpcell.00579.200315355854, JackmanR.W.KandarianS.C. 2004 The molecular basis of skeletal muscle atrophy. Am. J. Physiol. Cell Physiol. 287:C834–C843 10.1152/ajpcell.00579.200315355854
(AttaixD.BechetD. 2007 FoxO3 controls dangerous proteolytic liaisons. Cell Metab. 6:425–427 10.1016/j.cmet.2007.11.00518054311)
AttaixD.BechetD. 2007 FoxO3 controls dangerous proteolytic liaisons. Cell Metab. 6:425–427 10.1016/j.cmet.2007.11.00518054311
AttaixD.BechetD. 2007 FoxO3 controls dangerous proteolytic liaisons. Cell Metab. 6:425–427 10.1016/j.cmet.2007.11.00518054311, AttaixD.BechetD. 2007 FoxO3 controls dangerous proteolytic liaisons. Cell Metab. 6:425–427 10.1016/j.cmet.2007.11.00518054311
(KumarA.BoriekA.M. 2003 Mechanical stress activates the nuclear factor-kappaB pathway in skeletal muscle fibers: a possible role in Duchenne muscular dystrophy. FASEB J. 17:386–396 10.1096/fj.02-0542com12631578)
KumarA.BoriekA.M. 2003 Mechanical stress activates the nuclear factor-kappaB pathway in skeletal muscle fibers: a possible role in Duchenne muscular dystrophy. FASEB J. 17:386–396 10.1096/fj.02-0542com12631578
KumarA.BoriekA.M. 2003 Mechanical stress activates the nuclear factor-kappaB pathway in skeletal muscle fibers: a possible role in Duchenne muscular dystrophy. FASEB J. 17:386–396 10.1096/fj.02-0542com12631578, KumarA.BoriekA.M. 2003 Mechanical stress activates the nuclear factor-kappaB pathway in skeletal muscle fibers: a possible role in Duchenne muscular dystrophy. FASEB J. 17:386–396 10.1096/fj.02-0542com12631578
Kronqvist (2002)
ADAM12 alleviates the skeletal muscle pathology in mdx dystrophic mice
Am. J. Pathol., 161
Yi-Ping Li, Yuling Chen, J. John, J. Moylan, Bingwen Jin, Douglas Mann, Michael Reid (2005)
TNF- acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle
(DrexlerH.RiedeU.MünzelT.KönigH.FunkeE.JustH. 1992 Alterations of skeletal muscle in chronic heart failure. Circulation. 85:1751–17591315220)
DrexlerH.RiedeU.MünzelT.KönigH.FunkeE.JustH. 1992 Alterations of skeletal muscle in chronic heart failure. Circulation. 85:1751–17591315220
DrexlerH.RiedeU.MünzelT.KönigH.FunkeE.JustH. 1992 Alterations of skeletal muscle in chronic heart failure. Circulation. 85:1751–17591315220, DrexlerH.RiedeU.MünzelT.KönigH.FunkeE.JustH. 1992 Alterations of skeletal muscle in chronic heart failure. Circulation. 85:1751–17591315220
(LiH.MittalA.MakonchukD.Y.BhatnagarS.KumarA. 2009a Matrix metalloproteinase-9 inhibition ameliorates pathogenesis and improves skeletal muscle regeneration in muscular dystrophy. Hum. Mol. Genet. 18:2584–2598 10.1093/hmg/ddp19119401296)
LiH.MittalA.MakonchukD.Y.BhatnagarS.KumarA. 2009a Matrix metalloproteinase-9 inhibition ameliorates pathogenesis and improves skeletal muscle regeneration in muscular dystrophy. Hum. Mol. Genet. 18:2584–2598 10.1093/hmg/ddp19119401296
LiH.MittalA.MakonchukD.Y.BhatnagarS.KumarA. 2009a Matrix metalloproteinase-9 inhibition ameliorates pathogenesis and improves skeletal muscle regeneration in muscular dystrophy. Hum. Mol. Genet. 18:2584–2598 10.1093/hmg/ddp19119401296, LiH.MittalA.MakonchukD.Y.BhatnagarS.KumarA. 2009a Matrix metalloproteinase-9 inhibition ameliorates pathogenesis and improves skeletal muscle regeneration in muscular dystrophy. Hum. Mol. Genet. 18:2584–2598 10.1093/hmg/ddp19119401296
(HinkleR.T.HodgeK.M.CodyD.B.SheldonR.J.KobilkaB.K.IsfortR.J. 2002 Skeletal muscle hypertrophy and anti-atrophy effects of clenbuterol are mediated by the beta2-adrenergic receptor. Muscle Nerve. 25:729–734 10.1002/mus.1009211994968)
HinkleR.T.HodgeK.M.CodyD.B.SheldonR.J.KobilkaB.K.IsfortR.J. 2002 Skeletal muscle hypertrophy and anti-atrophy effects of clenbuterol are mediated by the beta2-adrenergic receptor. Muscle Nerve. 25:729–734 10.1002/mus.1009211994968
HinkleR.T.HodgeK.M.CodyD.B.SheldonR.J.KobilkaB.K.IsfortR.J. 2002 Skeletal muscle hypertrophy and anti-atrophy effects of clenbuterol are mediated by the beta2-adrenergic receptor. Muscle Nerve. 25:729–734 10.1002/mus.1009211994968, HinkleR.T.HodgeK.M.CodyD.B.SheldonR.J.KobilkaB.K.IsfortR.J. 2002 Skeletal muscle hypertrophy and anti-atrophy effects of clenbuterol are mediated by the beta2-adrenergic receptor. Muscle Nerve. 25:729–734 10.1002/mus.1009211994968
D. Pette, R. Staron (2001)
Transitions of muscle fiber phenotypic profiles
Histochemistry and Cell Biology, 115
(JainM.JakubowskiA.CuiL.ShiJ.SuL.BauerM.GuanJ.LimC.C.NaitoY.ThompsonJ.S. 2009 A novel role for tumor necrosis factor-like weak inducer of apoptosis (TWEAK) in the development of cardiac dysfunction and failure. Circulation. 119:2058–2068 10.1161/CIRCULATIONAHA.108.83728619349318)
JainM.JakubowskiA.CuiL.ShiJ.SuL.BauerM.GuanJ.LimC.C.NaitoY.ThompsonJ.S. 2009 A novel role for tumor necrosis factor-like weak inducer of apoptosis (TWEAK) in the development of cardiac dysfunction and failure. Circulation. 119:2058–2068 10.1161/CIRCULATIONAHA.108.83728619349318
JainM.JakubowskiA.CuiL.ShiJ.SuL.BauerM.GuanJ.LimC.C.NaitoY.ThompsonJ.S. 2009 A novel role for tumor necrosis factor-like weak inducer of apoptosis (TWEAK) in the development of cardiac dysfunction and failure. Circulation. 119:2058–2068 10.1161/CIRCULATIONAHA.108.83728619349318, JainM.JakubowskiA.CuiL.ShiJ.SuL.BauerM.GuanJ.LimC.C.NaitoY.ThompsonJ.S. 2009 A novel role for tumor necrosis factor-like weak inducer of apoptosis (TWEAK) in the development of cardiac dysfunction and failure. Circulation. 119:2058–2068 10.1161/CIRCULATIONAHA.108.83728619349318
D. Attaix, D. Béchet (2007)
FoxO3 controls dangerous proteolytic liaisons.
Cell metabolism, 6 6
H. Drexler, U. Riede, Thomas Miinzel, H. Kdnig, E. Funke, H. Just (1992)
Alterations of Skeletal Muscle in Chronic Heart Failure
Circulation, 85
(LahouteC.SotiropoulosA.FavierM.Guillet-DeniauI.CharvetC.FerryA.Butler-BrowneG.MetzgerD.TuilD.DaegelenD. 2008 Premature aging in skeletal muscle lacking serum response factor. PLoS One. 3:e3910 10.1371/journal.pone.000391019079548)
LahouteC.SotiropoulosA.FavierM.Guillet-DeniauI.CharvetC.FerryA.Butler-BrowneG.MetzgerD.TuilD.DaegelenD. 2008 Premature aging in skeletal muscle lacking serum response factor. PLoS One. 3:e3910 10.1371/journal.pone.000391019079548
LahouteC.SotiropoulosA.FavierM.Guillet-DeniauI.CharvetC.FerryA.Butler-BrowneG.MetzgerD.TuilD.DaegelenD. 2008 Premature aging in skeletal muscle lacking serum response factor. PLoS One. 3:e3910 10.1371/journal.pone.000391019079548, LahouteC.SotiropoulosA.FavierM.Guillet-DeniauI.CharvetC.FerryA.Butler-BrowneG.MetzgerD.TuilD.DaegelenD. 2008 Premature aging in skeletal muscle lacking serum response factor. PLoS One. 3:e3910 10.1371/journal.pone.000391019079548
(ArgilésJ.M.BusquetsS.López-SorianoF.J. 2005 The pivotal role of cytokines in muscle wasting during cancer. Int. J. Biochem. Cell Biol. 37:2036–2046 10.1016/j.biocel.2005.03.01416105746)
ArgilésJ.M.BusquetsS.López-SorianoF.J. 2005 The pivotal role of cytokines in muscle wasting during cancer. Int. J. Biochem. Cell Biol. 37:2036–2046 10.1016/j.biocel.2005.03.01416105746
ArgilésJ.M.BusquetsS.López-SorianoF.J. 2005 The pivotal role of cytokines in muscle wasting during cancer. Int. J. Biochem. Cell Biol. 37:2036–2046 10.1016/j.biocel.2005.03.01416105746, ArgilésJ.M.BusquetsS.López-SorianoF.J. 2005 The pivotal role of cytokines in muscle wasting during cancer. Int. J. Biochem. Cell Biol. 37:2036–2046 10.1016/j.biocel.2005.03.01416105746
(ZhaoJ.BraultJ.J.SchildA.GoldbergA.L. 2008 Coordinate activation of autophagy and the proteasome pathway by FoxO transcription factor. Autophagy. 4:378–38018227643)
ZhaoJ.BraultJ.J.SchildA.GoldbergA.L. 2008 Coordinate activation of autophagy and the proteasome pathway by FoxO transcription factor. Autophagy. 4:378–38018227643
ZhaoJ.BraultJ.J.SchildA.GoldbergA.L. 2008 Coordinate activation of autophagy and the proteasome pathway by FoxO transcription factor. Autophagy. 4:378–38018227643, ZhaoJ.BraultJ.J.SchildA.GoldbergA.L. 2008 Coordinate activation of autophagy and the proteasome pathway by FoxO transcription factor. Autophagy. 4:378–38018227643
A. Macaluso, G. Vito (2004)
Muscle strength, power and adaptations to resistance training in older people
European Journal of Applied Physiology, 91
(CaiD.FrantzJ.D.TawaN.E.Jr.MelendezP.A.OhB.C.LidovH.G.HasselgrenP.O.FronteraW.R.LeeJ.GlassD.J.ShoelsonS.E. 2004 IKKbeta/NF-kappaB activation causes severe muscle wasting in mice. Cell. 119:285–298 10.1016/j.cell.2004.09.02715479644)
CaiD.FrantzJ.D.TawaN.E.Jr.MelendezP.A.OhB.C.LidovH.G.HasselgrenP.O.FronteraW.R.LeeJ.GlassD.J.ShoelsonS.E. 2004 IKKbeta/NF-kappaB activation causes severe muscle wasting in mice. Cell. 119:285–298 10.1016/j.cell.2004.09.02715479644
CaiD.FrantzJ.D.TawaN.E.Jr.MelendezP.A.OhB.C.LidovH.G.HasselgrenP.O.FronteraW.R.LeeJ.GlassD.J.ShoelsonS.E. 2004 IKKbeta/NF-kappaB activation causes severe muscle wasting in mice. Cell. 119:285–298 10.1016/j.cell.2004.09.02715479644, CaiD.FrantzJ.D.TawaN.E.Jr.MelendezP.A.OhB.C.LidovH.G.HasselgrenP.O.FronteraW.R.LeeJ.GlassD.J.ShoelsonS.E. 2004 IKKbeta/NF-kappaB activation causes severe muscle wasting in mice. Cell. 119:285–298 10.1016/j.cell.2004.09.02715479644
(LiY.-P.ChenY.JohnJ.MoylanJ.JinB.MannD.L.ReidM.B. 2005 TNF-alpha acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle. FASEB J. 19:362–370 10.1096/fj.04-2364com15746179)
LiY.-P.ChenY.JohnJ.MoylanJ.JinB.MannD.L.ReidM.B. 2005 TNF-alpha acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle. FASEB J. 19:362–370 10.1096/fj.04-2364com15746179
LiY.-P.ChenY.JohnJ.MoylanJ.JinB.MannD.L.ReidM.B. 2005 TNF-alpha acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle. FASEB J. 19:362–370 10.1096/fj.04-2364com15746179, LiY.-P.ChenY.JohnJ.MoylanJ.JinB.MannD.L.ReidM.B. 2005 TNF-alpha acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle. FASEB J. 19:362–370 10.1096/fj.04-2364com15746179
C. Dogra, S. Hall, Nia Wedhas, T. Linkhart, Ashok Kumar (2007)
Fibroblast Growth Factor Inducible 14 (Fn14) Is Required for the Expression of Myogenic Regulatory Factors and Differentiation of Myoblasts into Myotubes
Journal of Biological Chemistry, 282
(WinklesJ.A. 2008 The TWEAK-Fn14 cytokine-receptor axis: discovery, biology and therapeutic targeting. Nat. Rev. Drug Discov. 7:411–425 10.1038/nrd248818404150)
WinklesJ.A. 2008 The TWEAK-Fn14 cytokine-receptor axis: discovery, biology and therapeutic targeting. Nat. Rev. Drug Discov. 7:411–425 10.1038/nrd248818404150
WinklesJ.A. 2008 The TWEAK-Fn14 cytokine-receptor axis: discovery, biology and therapeutic targeting. Nat. Rev. Drug Discov. 7:411–425 10.1038/nrd248818404150, WinklesJ.A. 2008 The TWEAK-Fn14 cytokine-receptor axis: discovery, biology and therapeutic targeting. Nat. Rev. Drug Discov. 7:411–425 10.1038/nrd248818404150
(DograC.ChangotraH.MohanS.KumarA. 2006 Tumor necrosis factor-like weak inducer of apoptosis inhibits skeletal myogenesis through sustained activation of nuclear factor-kappaB and degradation of MyoD protein. J. Biol. Chem. 281:10327–10336 10.1074/jbc.M51113120016461349)
DograC.ChangotraH.MohanS.KumarA. 2006 Tumor necrosis factor-like weak inducer of apoptosis inhibits skeletal myogenesis through sustained activation of nuclear factor-kappaB and degradation of MyoD protein. J. Biol. Chem. 281:10327–10336 10.1074/jbc.M51113120016461349
DograC.ChangotraH.MohanS.KumarA. 2006 Tumor necrosis factor-like weak inducer of apoptosis inhibits skeletal myogenesis through sustained activation of nuclear factor-kappaB and degradation of MyoD protein. J. Biol. Chem. 281:10327–10336 10.1074/jbc.M51113120016461349, DograC.ChangotraH.MohanS.KumarA. 2006 Tumor necrosis factor-like weak inducer of apoptosis inhibits skeletal myogenesis through sustained activation of nuclear factor-kappaB and degradation of MyoD protein. J. Biol. Chem. 281:10327–10336 10.1074/jbc.M51113120016461349
Jinghui Zhao, J. Brault, A. Schild, Pei-rang Cao, M. Sandri, S. Schiaffino, S. Lecker, A. Goldberg (2007)
FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells.
Cell metabolism, 6 6
J. Winkles (2008)
The TWEAK–Fn14 cytokine–receptor axis: discovery, biology and therapeutic targeting
Nature Reviews Drug Discovery, 7
(SuzukiN.MotohashiN.UezumiA.FukadaS.YoshimuraT.ItoyamaY.AokiM.Miyagoe-SuzukiY.TakedaS. 2007 NO production results in suspension-induced muscle atrophy through dislocation of neuronal NOS. J. Clin. Invest. 117:2468–2476 10.1172/JCI3065417786240)
SuzukiN.MotohashiN.UezumiA.FukadaS.YoshimuraT.ItoyamaY.AokiM.Miyagoe-SuzukiY.TakedaS. 2007 NO production results in suspension-induced muscle atrophy through dislocation of neuronal NOS. J. Clin. Invest. 117:2468–2476 10.1172/JCI3065417786240
SuzukiN.MotohashiN.UezumiA.FukadaS.YoshimuraT.ItoyamaY.AokiM.Miyagoe-SuzukiY.TakedaS. 2007 NO production results in suspension-induced muscle atrophy through dislocation of neuronal NOS. J. Clin. Invest. 117:2468–2476 10.1172/JCI3065417786240, SuzukiN.MotohashiN.UezumiA.FukadaS.YoshimuraT.ItoyamaY.AokiM.Miyagoe-SuzukiY.TakedaS. 2007 NO production results in suspension-induced muscle atrophy through dislocation of neuronal NOS. J. Clin. Invest. 117:2468–2476 10.1172/JCI3065417786240
(TanabeK.BonillaI.WinklesJ.A.StrittmatterS.M. 2003 Fibroblast growth factor-inducible-14 is induced in axotomized neurons and promotes neurite outgrowth. J. Neurosci. 23:9675–968614573547)
TanabeK.BonillaI.WinklesJ.A.StrittmatterS.M. 2003 Fibroblast growth factor-inducible-14 is induced in axotomized neurons and promotes neurite outgrowth. J. Neurosci. 23:9675–968614573547
TanabeK.BonillaI.WinklesJ.A.StrittmatterS.M. 2003 Fibroblast growth factor-inducible-14 is induced in axotomized neurons and promotes neurite outgrowth. J. Neurosci. 23:9675–968614573547, TanabeK.BonillaI.WinklesJ.A.StrittmatterS.M. 2003 Fibroblast growth factor-inducible-14 is induced in axotomized neurons and promotes neurite outgrowth. J. Neurosci. 23:9675–968614573547
(MourkiotiF.KratsiosP.LueddeT.SongY.H.DelafontaineP.AdamiR.ParenteV.BottinelliR.PasparakisM.RosenthalN. 2006 Targeted ablation of IKK2 improves skeletal muscle strength, maintains mass, and promotes regeneration. J. Clin. Invest. 116:2945–2954 10.1172/JCI2872117080195)
MourkiotiF.KratsiosP.LueddeT.SongY.H.DelafontaineP.AdamiR.ParenteV.BottinelliR.PasparakisM.RosenthalN. 2006 Targeted ablation of IKK2 improves skeletal muscle strength, maintains mass, and promotes regeneration. J. Clin. Invest. 116:2945–2954 10.1172/JCI2872117080195
MourkiotiF.KratsiosP.LueddeT.SongY.H.DelafontaineP.AdamiR.ParenteV.BottinelliR.PasparakisM.RosenthalN. 2006 Targeted ablation of IKK2 improves skeletal muscle strength, maintains mass, and promotes regeneration. J. Clin. Invest. 116:2945–2954 10.1172/JCI2872117080195, MourkiotiF.KratsiosP.LueddeT.SongY.H.DelafontaineP.AdamiR.ParenteV.BottinelliR.PasparakisM.RosenthalN. 2006 Targeted ablation of IKK2 improves skeletal muscle strength, maintains mass, and promotes regeneration. J. Clin. Invest. 116:2945–2954 10.1172/JCI2872117080195
(StittT.N.DrujanD.ClarkeB.A.PanaroF.J.TimofeyvaY.KlineW.O.GonzalezM.YancopoulosG.D.GlassD.J. 2004 The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. Mol. Cell. 14:395–403 10.1016/S1097-2765(04)00211-415125842)
StittT.N.DrujanD.ClarkeB.A.PanaroF.J.TimofeyvaY.KlineW.O.GonzalezM.YancopoulosG.D.GlassD.J. 2004 The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. Mol. Cell. 14:395–403 10.1016/S1097-2765(04)00211-415125842
StittT.N.DrujanD.ClarkeB.A.PanaroF.J.TimofeyvaY.KlineW.O.GonzalezM.YancopoulosG.D.GlassD.J. 2004 The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. Mol. Cell. 14:395–403 10.1016/S1097-2765(04)00211-415125842, StittT.N.DrujanD.ClarkeB.A.PanaroF.J.TimofeyvaY.KlineW.O.GonzalezM.YancopoulosG.D.GlassD.J. 2004 The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. Mol. Cell. 14:395–403 10.1016/S1097-2765(04)00211-415125842
J. Argiles, S. Busquets, F. López‐Soriano (2005)
The pivotal role of cytokines in muscle wasting during cancer.
The international journal of biochemistry & cell biology, 37 8
J. Fielitz, Mi-Sung Kim, J. Shelton, Shuaib Latif, J. Spencer, D. Glass, J. Richardson, R. Bassel-Duby, E. Olson (2007)
Myosin accumulation and striated muscle myopathy result from the loss of muscle RING finger 1 and 3.
The Journal of clinical investigation, 117 9
R. Irizarry, Zhijin Wu, Harris Jaffee (2006)
Comparison of Affymetrix GeneChip expression measures
Bioinformatics, 22 7
(SpäteU.SchulzeP.C. 2004 Proinflammatory cytokines and skeletal muscle. Curr. Opin. Clin. Nutr. Metab. Care. 7:265–269 10.1097/00075197-200405000-0000515075917)
SpäteU.SchulzeP.C. 2004 Proinflammatory cytokines and skeletal muscle. Curr. Opin. Clin. Nutr. Metab. Care. 7:265–269 10.1097/00075197-200405000-0000515075917
SpäteU.SchulzeP.C. 2004 Proinflammatory cytokines and skeletal muscle. Curr. Opin. Clin. Nutr. Metab. Care. 7:265–269 10.1097/00075197-200405000-0000515075917, SpäteU.SchulzeP.C. 2004 Proinflammatory cytokines and skeletal muscle. Curr. Opin. Clin. Nutr. Metab. Care. 7:265–269 10.1097/00075197-200405000-0000515075917
(AcharyyaS.LadnerK.J.NelsenL.L.DamrauerJ.ReiserP.J.SwoapS.GuttridgeD.C. 2004 Cancer cachexia is regulated by selective targeting of skeletal muscle gene products. J. Clin. Invest. 114:370–37815286803)
AcharyyaS.LadnerK.J.NelsenL.L.DamrauerJ.ReiserP.J.SwoapS.GuttridgeD.C. 2004 Cancer cachexia is regulated by selective targeting of skeletal muscle gene products. J. Clin. Invest. 114:370–37815286803
AcharyyaS.LadnerK.J.NelsenL.L.DamrauerJ.ReiserP.J.SwoapS.GuttridgeD.C. 2004 Cancer cachexia is regulated by selective targeting of skeletal muscle gene products. J. Clin. Invest. 114:370–37815286803, AcharyyaS.LadnerK.J.NelsenL.L.DamrauerJ.ReiserP.J.SwoapS.GuttridgeD.C. 2004 Cancer cachexia is regulated by selective targeting of skeletal muscle gene products. J. Clin. Invest. 114:370–37815286803
(KlineW.O.PanaroF.J.YangH.BodineS.C. 2007 Rapamycin inhibits the growth and muscle-sparing effects of clenbuterol. J. Appl. Physiol. 102:740–747 10.1152/japplphysiol.00873.200617068216)
KlineW.O.PanaroF.J.YangH.BodineS.C. 2007 Rapamycin inhibits the growth and muscle-sparing effects of clenbuterol. J. Appl. Physiol. 102:740–747 10.1152/japplphysiol.00873.200617068216
KlineW.O.PanaroF.J.YangH.BodineS.C. 2007 Rapamycin inhibits the growth and muscle-sparing effects of clenbuterol. J. Appl. Physiol. 102:740–747 10.1152/japplphysiol.00873.200617068216, KlineW.O.PanaroF.J.YangH.BodineS.C. 2007 Rapamycin inhibits the growth and muscle-sparing effects of clenbuterol. J. Appl. Physiol. 102:740–747 10.1152/japplphysiol.00873.200617068216
P. Kronqvist, N. Kawaguchi, R. Albrechtsen, Xiufeng Xu, H. Schrøder, B. Moghadaszadeh, Finn Cilius, Nielsen, Camilla, E. Engvall, U. Wewer (2002)
Short Communication ADAM12 Alleviates the Skeletal Muscle Pathology in mdx Dystrophic Mice
(DograC.ChangotraH.WedhasN.QinX.WergedalJ.E.KumarA. 2007a TNF-related weak inducer of apoptosis (TWEAK) is a potent skeletal muscle-wasting cytokine. FASEB J. 21:1857–1869 10.1096/fj.06-7537com17314137)
DograC.ChangotraH.WedhasN.QinX.WergedalJ.E.KumarA. 2007a TNF-related weak inducer of apoptosis (TWEAK) is a potent skeletal muscle-wasting cytokine. FASEB J. 21:1857–1869 10.1096/fj.06-7537com17314137
DograC.ChangotraH.WedhasN.QinX.WergedalJ.E.KumarA. 2007a TNF-related weak inducer of apoptosis (TWEAK) is a potent skeletal muscle-wasting cytokine. FASEB J. 21:1857–1869 10.1096/fj.06-7537com17314137, DograC.ChangotraH.WedhasN.QinX.WergedalJ.E.KumarA. 2007a TNF-related weak inducer of apoptosis (TWEAK) is a potent skeletal muscle-wasting cytokine. FASEB J. 21:1857–1869 10.1096/fj.06-7537com17314137
(BlaauwB.MammucariC.TonioloL.AgateaL.AbrahamR.SandriM.ReggianiC.SchiaffinoS. 2008 Akt activation prevents the force drop induced by eccentric contractions in dystrophin-deficient skeletal muscle. Hum. Mol. Genet. 17:3686–3696 10.1093/hmg/ddn26418753145)
BlaauwB.MammucariC.TonioloL.AgateaL.AbrahamR.SandriM.ReggianiC.SchiaffinoS. 2008 Akt activation prevents the force drop induced by eccentric contractions in dystrophin-deficient skeletal muscle. Hum. Mol. Genet. 17:3686–3696 10.1093/hmg/ddn26418753145
BlaauwB.MammucariC.TonioloL.AgateaL.AbrahamR.SandriM.ReggianiC.SchiaffinoS. 2008 Akt activation prevents the force drop induced by eccentric contractions in dystrophin-deficient skeletal muscle. Hum. Mol. Genet. 17:3686–3696 10.1093/hmg/ddn26418753145, BlaauwB.MammucariC.TonioloL.AgateaL.AbrahamR.SandriM.ReggianiC.SchiaffinoS. 2008 Akt activation prevents the force drop induced by eccentric contractions in dystrophin-deficient skeletal muscle. Hum. Mol. Genet. 17:3686–3696 10.1093/hmg/ddn26418753145
(KobayashiY.M.RaderE.P.CrawfordR.W.IyengarN.K.ThedensD.R.FaulknerJ.A.ParikhS.V.WeissR.M.ChamberlainJ.S.MooreS.A.CampbellK.P. 2008 Sarcolemma-localized nNOS is required to maintain activity after mild exercise. Nature. 456:511–515 10.1038/nature0741418953332)
KobayashiY.M.RaderE.P.CrawfordR.W.IyengarN.K.ThedensD.R.FaulknerJ.A.ParikhS.V.WeissR.M.ChamberlainJ.S.MooreS.A.CampbellK.P. 2008 Sarcolemma-localized nNOS is required to maintain activity after mild exercise. Nature. 456:511–515 10.1038/nature0741418953332
KobayashiY.M.RaderE.P.CrawfordR.W.IyengarN.K.ThedensD.R.FaulknerJ.A.ParikhS.V.WeissR.M.ChamberlainJ.S.MooreS.A.CampbellK.P. 2008 Sarcolemma-localized nNOS is required to maintain activity after mild exercise. Nature. 456:511–515 10.1038/nature0741418953332, KobayashiY.M.RaderE.P.CrawfordR.W.IyengarN.K.ThedensD.R.FaulknerJ.A.ParikhS.V.WeissR.M.ChamberlainJ.S.MooreS.A.CampbellK.P. 2008 Sarcolemma-localized nNOS is required to maintain activity after mild exercise. Nature. 456:511–515 10.1038/nature0741418953332
D. Cai, J. Frantz, N. Tawa, P. Meléndez, Byung-Chul Oh, H. Lidov, P. Hasselgren, W. Frontera, Jongsoon Lee, D. Glass, S. Shoelson (2004)
IKKβ/NF-κB Activation Causes Severe Muscle Wasting in Mice
Cell, 119
(FielitzJ.KimM.S.SheltonJ.M.LatifS.SpencerJ.A.GlassD.J.RichardsonJ.A.Bassel-DubyR.OlsonE.N. 2007 Myosin accumulation and striated muscle myopathy result from the loss of muscle RING finger 1 and 3. J. Clin. Invest. 117:2486–2495 10.1172/JCI3282717786241)
FielitzJ.KimM.S.SheltonJ.M.LatifS.SpencerJ.A.GlassD.J.RichardsonJ.A.Bassel-DubyR.OlsonE.N. 2007 Myosin accumulation and striated muscle myopathy result from the loss of muscle RING finger 1 and 3. J. Clin. Invest. 117:2486–2495 10.1172/JCI3282717786241
FielitzJ.KimM.S.SheltonJ.M.LatifS.SpencerJ.A.GlassD.J.RichardsonJ.A.Bassel-DubyR.OlsonE.N. 2007 Myosin accumulation and striated muscle myopathy result from the loss of muscle RING finger 1 and 3. J. Clin. Invest. 117:2486–2495 10.1172/JCI3282717786241, FielitzJ.KimM.S.SheltonJ.M.LatifS.SpencerJ.A.GlassD.J.RichardsonJ.A.Bassel-DubyR.OlsonE.N. 2007 Myosin accumulation and striated muscle myopathy result from the loss of muscle RING finger 1 and 3. J. Clin. Invest. 117:2486–2495 10.1172/JCI3282717786241
(MaeckerH.VarfolomeevE.KischkelF.LawrenceD.LeBlancH.LeeW.HurstS.DanilenkoD.LiJ.FilvaroffE. 2005 TWEAK attenuates the transition from innate to adaptive immunity. Cell. 123:931–944 10.1016/j.cell.2005.09.02216325585)
MaeckerH.VarfolomeevE.KischkelF.LawrenceD.LeBlancH.LeeW.HurstS.DanilenkoD.LiJ.FilvaroffE. 2005 TWEAK attenuates the transition from innate to adaptive immunity. Cell. 123:931–944 10.1016/j.cell.2005.09.02216325585
MaeckerH.VarfolomeevE.KischkelF.LawrenceD.LeBlancH.LeeW.HurstS.DanilenkoD.LiJ.FilvaroffE. 2005 TWEAK attenuates the transition from innate to adaptive immunity. Cell. 123:931–944 10.1016/j.cell.2005.09.02216325585, MaeckerH.VarfolomeevE.KischkelF.LawrenceD.LeBlancH.LeeW.HurstS.DanilenkoD.LiJ.FilvaroffE. 2005 TWEAK attenuates the transition from innate to adaptive immunity. Cell. 123:931–944 10.1016/j.cell.2005.09.02216325585
(SandriM. 2008 Signaling in muscle atrophy and hypertrophy. Physiology (Bethesda). 23:160–17018556469)
SandriM. 2008 Signaling in muscle atrophy and hypertrophy. Physiology (Bethesda). 23:160–17018556469
SandriM. 2008 Signaling in muscle atrophy and hypertrophy. Physiology (Bethesda). 23:160–17018556469, SandriM. 2008 Signaling in muscle atrophy and hypertrophy. Physiology (Bethesda). 23:160–17018556469
(MacalusoA.De VitoG. 2004 Muscle strength, power and adaptations to resistance training in older people. Eur. J. Appl. Physiol. 91:450–472 10.1007/s00421-003-0991-314639481)
MacalusoA.De VitoG. 2004 Muscle strength, power and adaptations to resistance training in older people. Eur. J. Appl. Physiol. 91:450–472 10.1007/s00421-003-0991-314639481
MacalusoA.De VitoG. 2004 Muscle strength, power and adaptations to resistance training in older people. Eur. J. Appl. Physiol. 91:450–472 10.1007/s00421-003-0991-314639481, MacalusoA.De VitoG. 2004 Muscle strength, power and adaptations to resistance training in older people. Eur. J. Appl. Physiol. 91:450–472 10.1007/s00421-003-0991-314639481
Hong Li, A. Mittal, Denys Makonchuk, Shephali Bhatnagar, Ashok Kumar (2009)
Matrix metalloproteinase-9 inhibition ameliorates pathogenesis and improves skeletal muscle regeneration in muscular dystrophy.
Human molecular genetics, 18 14
Hong Li, A. Mittal, P. Paul, Mukesh Kumar, D. Srivastava, S. Tyagi, Ashok Kumar (2009)
Tumor Necrosis Factor-related Weak Inducer of Apoptosis Augments Matrix Metalloproteinase 9 (MMP-9) Production in Skeletal Muscle through the Activation of Nuclear Factor-κB-inducing Kinase and p38 Mitogen-activated Protein Kinase
Journal of Biological Chemistry, 284
Ashok Kumar, A. Boriek (2003)
Mechanical stress activates the nuclear factor‐kappaB pathway in skeletal muscle fibers: a possible role in Duchenne muscular dystrophy
The FASEB Journal, 17
Jinghui Zhao, J. Brault, A. Schild, A. Goldberg (2008)
Coordinate activation of autophagy and the proteasome pathway by FoxO transcription factor
Autophagy, 4
Ulrike Späte, P. Schulze (2004)
Proinflammatory cytokines and skeletal muscle
Current Opinion in Clinical Nutrition and Metabolic Care, 7
H. Maecker, E. Varfolomeev, F. Kischkel, D. Lawrence, Heidi Leblanc, Wyne Lee, Stephen Hurst, D. Danilenko, Jun Li, E. Filvaroff, Becky Yang, D. Daniel, A. Ashkenazi (2005)
TWEAK Attenuates the Transition from Innate to Adaptive Immunity
Cell, 123
(HunterR.B.KandarianS.C. 2004 Disruption of either the Nfkb1 or the Bcl3 gene inhibits skeletal muscle atrophy. J. Clin. Invest. 114:1504–151115546001)
HunterR.B.KandarianS.C. 2004 Disruption of either the Nfkb1 or the Bcl3 gene inhibits skeletal muscle atrophy. J. Clin. Invest. 114:1504–151115546001
HunterR.B.KandarianS.C. 2004 Disruption of either the Nfkb1 or the Bcl3 gene inhibits skeletal muscle atrophy. J. Clin. Invest. 114:1504–151115546001, HunterR.B.KandarianS.C. 2004 Disruption of either the Nfkb1 or the Bcl3 gene inhibits skeletal muscle atrophy. J. Clin. Invest. 114:1504–151115546001
(LiH.MittalA.PaulP.K.KumarM.SrivastavaD.S.TyagiS.C.KumarA. 2009b Tumor necrosis factor-related weak inducer of apoptosis augments matrix metalloproteinase 9 (MMP-9) production in skeletal muscle through the activation of nuclear factor-kappaB-inducing kinase and p38 mitogen-activated protein kinase: a potential role of MMP-9 in myopathy. J. Biol. Chem. 284:4439–4450 10.1074/jbc.M80554620019074147)
LiH.MittalA.PaulP.K.KumarM.SrivastavaD.S.TyagiS.C.KumarA. 2009b Tumor necrosis factor-related weak inducer of apoptosis augments matrix metalloproteinase 9 (MMP-9) production in skeletal muscle through the activation of nuclear factor-kappaB-inducing kinase and p38 mitogen-activated protein kinase: a potential role of MMP-9 in myopathy. J. Biol. Chem. 284:4439–4450 10.1074/jbc.M80554620019074147
LiH.MittalA.PaulP.K.KumarM.SrivastavaD.S.TyagiS.C.KumarA. 2009b Tumor necrosis factor-related weak inducer of apoptosis augments matrix metalloproteinase 9 (MMP-9) production in skeletal muscle through the activation of nuclear factor-kappaB-inducing kinase and p38 mitogen-activated protein kinase: a potential role of MMP-9 in myopathy. J. Biol. Chem. 284:4439–4450 10.1074/jbc.M80554620019074147, LiH.MittalA.PaulP.K.KumarM.SrivastavaD.S.TyagiS.C.KumarA. 2009b Tumor necrosis factor-related weak inducer of apoptosis augments matrix metalloproteinase 9 (MMP-9) production in skeletal muscle through the activation of nuclear factor-kappaB-inducing kinase and p38 mitogen-activated protein kinase: a potential role of MMP-9 in myopathy. J. Biol. Chem. 284:4439–4450 10.1074/jbc.M80554620019074147
Hunter (2004)
Disruption of either the Nfkb1 or the Bcl3 gene inhibits skeletal muscle atrophy
J. Clin. Invest., 114
Tanabe (2003)
Fibroblast growth factor-inducible-14 is induced in axotomized neurons and promotes neurite outgrowth
J. Neurosci., 23
F. Mourkioti, P. Kratsios, T. Luedde, Yao‐Hua Song, P. Delafontaine, R. Adami, V. Parente, R. Bottinelli, M. Pasparakis, N. Rosenthal (2006)
Targeted ablation of IKK2 improves skeletal muscle strength, maintains mass, and promotes regeneration.
The Journal of clinical investigation, 116 11
(AcharyyaS.GuttridgeD.C. 2007 Cancer cachexia signaling pathways continue to emerge yet much still points to the proteasome. Clin. Cancer Res. 13:1356–1361 10.1158/1078-0432.CCR-06-230717332276)
AcharyyaS.GuttridgeD.C. 2007 Cancer cachexia signaling pathways continue to emerge yet much still points to the proteasome. Clin. Cancer Res. 13:1356–1361 10.1158/1078-0432.CCR-06-230717332276
AcharyyaS.GuttridgeD.C. 2007 Cancer cachexia signaling pathways continue to emerge yet much still points to the proteasome. Clin. Cancer Res. 13:1356–1361 10.1158/1078-0432.CCR-06-230717332276, AcharyyaS.GuttridgeD.C. 2007 Cancer cachexia signaling pathways continue to emerge yet much still points to the proteasome. Clin. Cancer Res. 13:1356–1361 10.1158/1078-0432.CCR-06-230717332276
(CohenS.BraultJ.J.GygiS.P.GlassD.J.ValenzuelaD.M.GartnerC.LatresE.GoldbergA.L. 2009 During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation. J. Cell Biol. 185:1083–1095 10.1083/jcb.20090105219506036)
CohenS.BraultJ.J.GygiS.P.GlassD.J.ValenzuelaD.M.GartnerC.LatresE.GoldbergA.L. 2009 During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation. J. Cell Biol. 185:1083–1095 10.1083/jcb.20090105219506036
CohenS.BraultJ.J.GygiS.P.GlassD.J.ValenzuelaD.M.GartnerC.LatresE.GoldbergA.L. 2009 During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation. J. Cell Biol. 185:1083–1095 10.1083/jcb.20090105219506036, CohenS.BraultJ.J.GygiS.P.GlassD.J.ValenzuelaD.M.GartnerC.LatresE.GoldbergA.L. 2009 During muscle atrophy, thick, but not thin, filament components are degraded by MuRF1-dependent ubiquitylation. J. Cell Biol. 185:1083–1095 10.1083/jcb.20090105219506036
(GlassD.J. 2005 Skeletal muscle hypertrophy and atrophy signaling pathways. Int. J. Biochem. Cell Biol. 37:1974–198416087388)
GlassD.J. 2005 Skeletal muscle hypertrophy and atrophy signaling pathways. Int. J. Biochem. Cell Biol. 37:1974–198416087388
GlassD.J. 2005 Skeletal muscle hypertrophy and atrophy signaling pathways. Int. J. Biochem. Cell Biol. 37:1974–198416087388, GlassD.J. 2005 Skeletal muscle hypertrophy and atrophy signaling pathways. Int. J. Biochem. Cell Biol. 37:1974–198416087388
D. Cai, J. Frantz, N. Tawa, P. Meléndez, Byung-Chul Oh, H. Lidov, P. Hasselgren, W. Frontera, Jongsoon Lee, D. Glass, S. Shoelson (2004)
IKKbeta/NF-kappaB activation causes severe muscle wasting in mice.
Cell, 119 2
K. Kamata, S. Kamijo, A. Nakajima, Akemi Koyanagi, H. Kurosawa, H. Yagita, K. Okumura (2006)
Involvement of TNF-Like Weak Inducer of Apoptosis in the Pathogenesis of Collagen-Induced Arthritis1
The Journal of Immunology, 177
(CaoP.R.KimH.J.LeckerS.H. 2005 Ubiquitin-protein ligases in muscle wasting. Int. J. Biochem. Cell Biol. 37:2088–2097 10.1016/j.biocel.2004.11.01016125112)
CaoP.R.KimH.J.LeckerS.H. 2005 Ubiquitin-protein ligases in muscle wasting. Int. J. Biochem. Cell Biol. 37:2088–2097 10.1016/j.biocel.2004.11.01016125112
CaoP.R.KimH.J.LeckerS.H. 2005 Ubiquitin-protein ligases in muscle wasting. Int. J. Biochem. Cell Biol. 37:2088–2097 10.1016/j.biocel.2004.11.01016125112, CaoP.R.KimH.J.LeckerS.H. 2005 Ubiquitin-protein ligases in muscle wasting. Int. J. Biochem. Cell Biol. 37:2088–2097 10.1016/j.biocel.2004.11.01016125112
Ka-man Lai, Michael Gonzalez, W. Poueymirou, W. Kline, Erqian Na, Elizabeth Zlotchenko, T. Stitt, A. Economides, G. Yancopoulos, D. Glass (2004)
Conditional Activation of Akt in Adult Skeletal Muscle Induces Rapid Hypertrophy
Molecular and Cellular Biology, 24
(MordierS.DevalC.BéchetD.TassaA.FerraraM. 2000 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 10.1074/jbc.M00363320010893413)
MordierS.DevalC.BéchetD.TassaA.FerraraM. 2000 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 10.1074/jbc.M00363320010893413
MordierS.DevalC.BéchetD.TassaA.FerraraM. 2000 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 10.1074/jbc.M00363320010893413, MordierS.DevalC.BéchetD.TassaA.FerraraM. 2000 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 10.1074/jbc.M00363320010893413
J. Schertzer, D. Plant, G. Lynch (2006)
Optimizing plasmid-based gene transfer for investigating skeletal muscle structure and function.
Molecular therapy : the journal of the American Society of Gene Therapy, 13 4
Swarnali Acharyya, Matthew Butchbach, Z. Sahenk, Huating Wang, M. Saji, Micheal Carathers, M. Ringel, R. Skipworth, K. Fearon, M. Hollingsworth, P. Muscarella, A. Burghes, Jill Rafael-Fortney, D. Guttridge (2005)
Dystrophin glycoprotein complex dysfunction: a regulatory link between muscular dystrophy and cancer cachexia.
Cancer cell, 8 5
(ClarkeB.A.DrujanD.WillisM.S.MurphyL.O.CorpinaR.A.BurovaE.RakhilinS.V.StittT.N.PattersonC.LatresE.GlassD.J. 2007 The E3 Ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle. Cell Metab. 6:376–385 10.1016/j.cmet.2007.09.00917983583)
ClarkeB.A.DrujanD.WillisM.S.MurphyL.O.CorpinaR.A.BurovaE.RakhilinS.V.StittT.N.PattersonC.LatresE.GlassD.J. 2007 The E3 Ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle. Cell Metab. 6:376–385 10.1016/j.cmet.2007.09.00917983583
ClarkeB.A.DrujanD.WillisM.S.MurphyL.O.CorpinaR.A.BurovaE.RakhilinS.V.StittT.N.PattersonC.LatresE.GlassD.J. 2007 The E3 Ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle. Cell Metab. 6:376–385 10.1016/j.cmet.2007.09.00917983583, ClarkeB.A.DrujanD.WillisM.S.MurphyL.O.CorpinaR.A.BurovaE.RakhilinS.V.StittT.N.PattersonC.LatresE.GlassD.J. 2007 The E3 Ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle. Cell Metab. 6:376–385 10.1016/j.cmet.2007.09.00917983583
(GomesM.D.LeckerS.H.JagoeR.T.NavonA.GoldbergA.L. 2001 Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proc. Natl. Acad. Sci. USA. 98:14440–14445 10.1073/pnas.25154119811717410)
GomesM.D.LeckerS.H.JagoeR.T.NavonA.GoldbergA.L. 2001 Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proc. Natl. Acad. Sci. USA. 98:14440–14445 10.1073/pnas.25154119811717410
GomesM.D.LeckerS.H.JagoeR.T.NavonA.GoldbergA.L. 2001 Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proc. Natl. Acad. Sci. USA. 98:14440–14445 10.1073/pnas.25154119811717410, GomesM.D.LeckerS.H.JagoeR.T.NavonA.GoldbergA.L. 2001 Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proc. Natl. Acad. Sci. USA. 98:14440–14445 10.1073/pnas.25154119811717410
(BodineS.C.StittT.N.GonzalezM.KlineW.O.StoverG.L.BauerleinR.ZlotchenkoE.ScrimgeourA.LawrenceJ.C.GlassD.J.YancopoulosG.D. 2001b Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo. Nat. Cell Biol. 3:1014–1019 10.1038/ncb1101-101411715023)
BodineS.C.StittT.N.GonzalezM.KlineW.O.StoverG.L.BauerleinR.ZlotchenkoE.ScrimgeourA.LawrenceJ.C.GlassD.J.YancopoulosG.D. 2001b Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo. Nat. Cell Biol. 3:1014–1019 10.1038/ncb1101-101411715023
BodineS.C.StittT.N.GonzalezM.KlineW.O.StoverG.L.BauerleinR.ZlotchenkoE.ScrimgeourA.LawrenceJ.C.GlassD.J.YancopoulosG.D. 2001b Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo. Nat. Cell Biol. 3:1014–1019 10.1038/ncb1101-101411715023, BodineS.C.StittT.N.GonzalezM.KlineW.O.StoverG.L.BauerleinR.ZlotchenkoE.ScrimgeourA.LawrenceJ.C.GlassD.J.YancopoulosG.D. 2001b Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo. Nat. Cell Biol. 3:1014–1019 10.1038/ncb1101-101411715023
(BodineS.C.LatresE.BaumhueterS.LaiV.K.NunezL.ClarkeB.A.PoueymirouW.T.PanaroF.J.NaE.DharmarajanK. 2001a Identification of ubiquitin ligases required for skeletal muscle atrophy. Science. 294:1704–1708 10.1126/science.106587411679633)
BodineS.C.LatresE.BaumhueterS.LaiV.K.NunezL.ClarkeB.A.PoueymirouW.T.PanaroF.J.NaE.DharmarajanK. 2001a Identification of ubiquitin ligases required for skeletal muscle atrophy. Science. 294:1704–1708 10.1126/science.106587411679633
BodineS.C.LatresE.BaumhueterS.LaiV.K.NunezL.ClarkeB.A.PoueymirouW.T.PanaroF.J.NaE.DharmarajanK. 2001a Identification of ubiquitin ligases required for skeletal muscle atrophy. Science. 294:1704–1708 10.1126/science.106587411679633, BodineS.C.LatresE.BaumhueterS.LaiV.K.NunezL.ClarkeB.A.PoueymirouW.T.PanaroF.J.NaE.DharmarajanK. 2001a Identification of ubiquitin ligases required for skeletal muscle atrophy. Science. 294:1704–1708 10.1126/science.106587411679633
Marcelo Gomes, S. Lecker, R. Jagoe, A. Navon, A. Goldberg (2001)
Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
Proceedings of the National Academy of Sciences of the United States of America, 98
(ZhaoJ.BraultJ.J.SchildA.CaoP.SandriM.SchiaffinoS.LeckerS.H.GoldbergA.L. 2007 FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab. 6:472–483 10.1016/j.cmet.2007.11.00418054316)
ZhaoJ.BraultJ.J.SchildA.CaoP.SandriM.SchiaffinoS.LeckerS.H.GoldbergA.L. 2007 FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab. 6:472–483 10.1016/j.cmet.2007.11.00418054316
ZhaoJ.BraultJ.J.SchildA.CaoP.SandriM.SchiaffinoS.LeckerS.H.GoldbergA.L. 2007 FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab. 6:472–483 10.1016/j.cmet.2007.11.00418054316, ZhaoJ.BraultJ.J.SchildA.CaoP.SandriM.SchiaffinoS.LeckerS.H.GoldbergA.L. 2007 FoxO3 coordinately activates protein degradation by the autophagic/lysosomal and proteasomal pathways in atrophying muscle cells. Cell Metab. 6:472–483 10.1016/j.cmet.2007.11.00418054316
C. Dogra, H. Changotra, S. Mohan, Ashok Kumar (2006)
Tumor Necrosis Factor-like Weak Inducer of Apoptosis Inhibits Skeletal Myogenesis through Sustained Activation of Nuclear Factor-κB and Degradation of MyoD Protein*
Journal of Biological Chemistry, 281
(NakayamaM.HaradaN.OkumuraK.YagitaH. 2003 Characterization of murine TWEAK and its receptor (Fn14) by monoclonal antibodies. Biochem. Biophys. Res. Commun. 306:819–825 10.1016/S0006-291X(03)01051-912821115)
NakayamaM.HaradaN.OkumuraK.YagitaH. 2003 Characterization of murine TWEAK and its receptor (Fn14) by monoclonal antibodies. Biochem. Biophys. Res. Commun. 306:819–825 10.1016/S0006-291X(03)01051-912821115
NakayamaM.HaradaN.OkumuraK.YagitaH. 2003 Characterization of murine TWEAK and its receptor (Fn14) by monoclonal antibodies. Biochem. Biophys. Res. Commun. 306:819–825 10.1016/S0006-291X(03)01051-912821115, NakayamaM.HaradaN.OkumuraK.YagitaH. 2003 Characterization of murine TWEAK and its receptor (Fn14) by monoclonal antibodies. Biochem. Biophys. Res. Commun. 306:819–825 10.1016/S0006-291X(03)01051-912821115
T. Stitt, D. Drujan, B. Clarke, Frank Panaro, Yekatarina Timofeyva, W. Kline, Michael Gonzalez, G. Yancopoulos, D. Glass (2004)
The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors.
Molecular cell, 14 3
(AcharyyaS.ButchbachM.E.SahenkZ.WangH.SajiM.CarathersM.RingelM.D.SkipworthR.J.FearonK.C.HollingsworthM.A. 2005 Dystrophin glycoprotein complex dysfunction: a regulatory link between muscular dystrophy and cancer cachexia. Cancer Cell. 8:421–432 10.1016/j.ccr.2005.10.00416286249)
AcharyyaS.ButchbachM.E.SahenkZ.WangH.SajiM.CarathersM.RingelM.D.SkipworthR.J.FearonK.C.HollingsworthM.A. 2005 Dystrophin glycoprotein complex dysfunction: a regulatory link between muscular dystrophy and cancer cachexia. Cancer Cell. 8:421–432 10.1016/j.ccr.2005.10.00416286249
AcharyyaS.ButchbachM.E.SahenkZ.WangH.SajiM.CarathersM.RingelM.D.SkipworthR.J.FearonK.C.HollingsworthM.A. 2005 Dystrophin glycoprotein complex dysfunction: a regulatory link between muscular dystrophy and cancer cachexia. Cancer Cell. 8:421–432 10.1016/j.ccr.2005.10.00416286249, AcharyyaS.ButchbachM.E.SahenkZ.WangH.SajiM.CarathersM.RingelM.D.SkipworthR.J.FearonK.C.HollingsworthM.A. 2005 Dystrophin glycoprotein complex dysfunction: a regulatory link between muscular dystrophy and cancer cachexia. Cancer Cell. 8:421–432 10.1016/j.ccr.2005.10.00416286249
M. Girgenrath, Shawn Weng, C. Kostek, B. Browning, Monica Wang, S. Brown, J. Winkles, J. Michaelson, N. Allaire, P. Schneider, M. Scott, Y. Hsu, H. Yagita, R. Flavell, J. Miller, L. Burkly, T. Zheng (2006)
TWEAK, via its receptor Fn14, is a novel regulator of mesenchymal progenitor cells and skeletal muscle regeneration
The EMBO Journal, 25
Swarnali Acharyya, K. Ladner, Lori Nelsen, Jeffrey Damrauer, P. Reiser, S. Swoap, D. Guttridge (2004)
Cancer cachexia is regulated by selective targeting of skeletal muscle gene products.
The Journal of clinical investigation, 114 3
Acharyya (2004)
Cancer cachexia is regulated by selective targeting of skeletal muscle gene products
J. Clin. Invest., 114
N. Suzuki, N. Motohashi, A. Uezumi, S. Fukada, T. Yoshimura, Y. Itoyama, M. Aoki, Y. Miyagoe‐Suzuki, S. Takeda (2007)
NO production results in suspension-induced muscle atrophy through dislocation of neuronal NOS.
The Journal of clinical investigation, 117 9
(KamataK.KamijoS.NakajimaA.KoyanagiA.KurosawaH.YagitaH.OkumuraK. 2006 Involvement of TNF-like weak inducer of apoptosis in the pathogenesis of collagen-induced arthritis. J. Immunol. 177:6433–643917056575)
KamataK.KamijoS.NakajimaA.KoyanagiA.KurosawaH.YagitaH.OkumuraK. 2006 Involvement of TNF-like weak inducer of apoptosis in the pathogenesis of collagen-induced arthritis. J. Immunol. 177:6433–643917056575
KamataK.KamijoS.NakajimaA.KoyanagiA.KurosawaH.YagitaH.OkumuraK. 2006 Involvement of TNF-like weak inducer of apoptosis in the pathogenesis of collagen-induced arthritis. J. Immunol. 177:6433–643917056575, KamataK.KamijoS.NakajimaA.KoyanagiA.KurosawaH.YagitaH.OkumuraK. 2006 Involvement of TNF-like weak inducer of apoptosis in the pathogenesis of collagen-induced arthritis. J. Immunol. 177:6433–643917056575
(LaiK.-M.V.GonzalezM.PoueymirouW.T.KlineW.O.NaE.ZlotchenkoE.StittT.N.EconomidesA.N.YancopoulosG.D.GlassD.J. 2004 Conditional activation of akt in adult skeletal muscle induces rapid hypertrophy. Mol. Cell. Biol. 24:9295–9304 10.1128/MCB.24.21.9295-9304.200415485899)
LaiK.-M.V.GonzalezM.PoueymirouW.T.KlineW.O.NaE.ZlotchenkoE.StittT.N.EconomidesA.N.YancopoulosG.D.GlassD.J. 2004 Conditional activation of akt in adult skeletal muscle induces rapid hypertrophy. Mol. Cell. Biol. 24:9295–9304 10.1128/MCB.24.21.9295-9304.200415485899
LaiK.-M.V.GonzalezM.PoueymirouW.T.KlineW.O.NaE.ZlotchenkoE.StittT.N.EconomidesA.N.YancopoulosG.D.GlassD.J. 2004 Conditional activation of akt in adult skeletal muscle induces rapid hypertrophy. Mol. Cell. Biol. 24:9295–9304 10.1128/MCB.24.21.9295-9304.200415485899, LaiK.-M.V.GonzalezM.PoueymirouW.T.KlineW.O.NaE.ZlotchenkoE.StittT.N.EconomidesA.N.YancopoulosG.D.GlassD.J. 2004 Conditional activation of akt in adult skeletal muscle induces rapid hypertrophy. Mol. Cell. Biol. 24:9295–9304 10.1128/MCB.24.21.9295-9304.200415485899
Pei-rang Cao, Hannah Kim, S. Lecker (2005)
Ubiquitin-protein ligases in muscle wasting.
The international journal of biochemistry & cell biology, 37 10
S. Bodine, E. Latres, S. Baumhueter, V. Lai, L. Nuñez, B. Clarke, W. Poueymirou, Frank Panaro, Erqian Na, Kumar Dharmarajan, Z. Pan, D. Valenzuela, T. Dechiara, T. Stitt, G. Yancopoulos, D. Glass (2001)
Identification of Ubiquitin Ligases Required for Skeletal Muscle Atrophy
Science, 294
B. Clarke, D. Drujan, M. Willis, Leon Murphy, R. Corpina, E. Burova, S. Rakhilin, T. Stitt, C. Patterson, E. Latres, D. Glass (2007)
The E3 Ligase MuRF1 degrades myosin heavy chain protein in dexamethasone-treated skeletal muscle.
Cell metabolism, 6 5
(SchertzerJ.D.PlantD.R.LynchG.S. 2006 Optimizing plasmid-based gene transfer for investigating skeletal muscle structure and function. Mol. Ther. 13:795–803 10.1016/j.ymthe.2005.09.01916309967)
SchertzerJ.D.PlantD.R.LynchG.S. 2006 Optimizing plasmid-based gene transfer for investigating skeletal muscle structure and function. Mol. Ther. 13:795–803 10.1016/j.ymthe.2005.09.01916309967
SchertzerJ.D.PlantD.R.LynchG.S. 2006 Optimizing plasmid-based gene transfer for investigating skeletal muscle structure and function. Mol. Ther. 13:795–803 10.1016/j.ymthe.2005.09.01916309967, SchertzerJ.D.PlantD.R.LynchG.S. 2006 Optimizing plasmid-based gene transfer for investigating skeletal muscle structure and function. Mol. Ther. 13:795–803 10.1016/j.ymthe.2005.09.01916309967
S. Mordier, C. Deval, D. Béchet, Amina Tassa, M. Ferrara (2000)
Leucine Limitation Induces Autophagy and Activation of Lysosome-dependent Proteolysis in C2C12 Myotubes through a Mammalian Target of Rapamycin-independent Signaling Pathway*
The Journal of Biological Chemistry, 275
(MammucariC.MilanG.RomanelloV.MasieroE.RudolfR.Del PiccoloP.BurdenS.J.Di LisiR.SandriC.ZhaoJ. 2007 FoxO3 controls autophagy in skeletal muscle in vivo. Cell Metab. 6:458–471 10.1016/j.cmet.2007.11.00118054315)
MammucariC.MilanG.RomanelloV.MasieroE.RudolfR.Del PiccoloP.BurdenS.J.Di LisiR.SandriC.ZhaoJ. 2007 FoxO3 controls autophagy in skeletal muscle in vivo. Cell Metab. 6:458–471 10.1016/j.cmet.2007.11.00118054315
MammucariC.MilanG.RomanelloV.MasieroE.RudolfR.Del PiccoloP.BurdenS.J.Di LisiR.SandriC.ZhaoJ. 2007 FoxO3 controls autophagy in skeletal muscle in vivo. Cell Metab. 6:458–471 10.1016/j.cmet.2007.11.00118054315, MammucariC.MilanG.RomanelloV.MasieroE.RudolfR.Del PiccoloP.BurdenS.J.Di LisiR.SandriC.ZhaoJ. 2007 FoxO3 controls autophagy in skeletal muscle in vivo. Cell Metab. 6:458–471 10.1016/j.cmet.2007.11.00118054315
(LiH.MalhotraS.KumarA. 2008 Nuclear factor-kappa B signaling in skeletal muscle atrophy. J. Mol. Med. 86:1113–1126 10.1007/s00109-008-0373-818574572)
LiH.MalhotraS.KumarA. 2008 Nuclear factor-kappa B signaling in skeletal muscle atrophy. J. Mol. Med. 86:1113–1126 10.1007/s00109-008-0373-818574572
LiH.MalhotraS.KumarA. 2008 Nuclear factor-kappa B signaling in skeletal muscle atrophy. J. Mol. Med. 86:1113–1126 10.1007/s00109-008-0373-818574572, LiH.MalhotraS.KumarA. 2008 Nuclear factor-kappa B signaling in skeletal muscle atrophy. J. Mol. Med. 86:1113–1126 10.1007/s00109-008-0373-818574572
(KronqvistP.KawaguchiN.AlbrechtsenR.XuX.SchrøderH.D.MoghadaszadehB.NielsenF.C.FröhlichC.EngvallE.WewerU.M. 2002 ADAM12 alleviates the skeletal muscle pathology in mdx dystrophic mice. Am. J. Pathol. 161:1535–154012414501)
KronqvistP.KawaguchiN.AlbrechtsenR.XuX.SchrøderH.D.MoghadaszadehB.NielsenF.C.FröhlichC.EngvallE.WewerU.M. 2002 ADAM12 alleviates the skeletal muscle pathology in mdx dystrophic mice. Am. J. Pathol. 161:1535–154012414501
KronqvistP.KawaguchiN.AlbrechtsenR.XuX.SchrøderH.D.MoghadaszadehB.NielsenF.C.FröhlichC.EngvallE.WewerU.M. 2002 ADAM12 alleviates the skeletal muscle pathology in mdx dystrophic mice. Am. J. Pathol. 161:1535–154012414501, KronqvistP.KawaguchiN.AlbrechtsenR.XuX.SchrøderH.D.MoghadaszadehB.NielsenF.C.FröhlichC.EngvallE.WewerU.M. 2002 ADAM12 alleviates the skeletal muscle pathology in mdx dystrophic mice. Am. J. Pathol. 161:1535–154012414501
C. Lahoute, A. Sotiropoulos, M. Favier, I. Guillet-Deniau, C. Charvet, A. Ferry, G. Butler-Browne, D. Metzger, D. Tuil, D. Daegelen (2008)
Premature Aging in Skeletal Muscle Lacking Serum Response Factor
PLoS ONE, 3
Swarnali Acharyya, D. Guttridge (2007)
Cancer Cachexia Signaling Pathways Continue to Emerge Yet Much Still Points to the Proteasome
Clinical Cancer Research, 13
(GirgenrathM.WengS.KostekC.A.BrowningB.WangM.BrownS.A.WinklesJ.A.MichaelsonJ.S.AllaireN.SchneiderP. 2006 TWEAK, via its receptor Fn14, is a novel regulator of mesenchymal progenitor cells and skeletal muscle regeneration. EMBO J. 25:5826–5839 10.1038/sj.emboj.760144117124496)
GirgenrathM.WengS.KostekC.A.BrowningB.WangM.BrownS.A.WinklesJ.A.MichaelsonJ.S.AllaireN.SchneiderP. 2006 TWEAK, via its receptor Fn14, is a novel regulator of mesenchymal progenitor cells and skeletal muscle regeneration. EMBO J. 25:5826–5839 10.1038/sj.emboj.760144117124496
GirgenrathM.WengS.KostekC.A.BrowningB.WangM.BrownS.A.WinklesJ.A.MichaelsonJ.S.AllaireN.SchneiderP. 2006 TWEAK, via its receptor Fn14, is a novel regulator of mesenchymal progenitor cells and skeletal muscle regeneration. EMBO J. 25:5826–5839 10.1038/sj.emboj.760144117124496, GirgenrathM.WengS.KostekC.A.BrowningB.WangM.BrownS.A.WinklesJ.A.MichaelsonJ.S.AllaireN.SchneiderP. 2006 TWEAK, via its receptor Fn14, is a novel regulator of mesenchymal progenitor cells and skeletal muscle regeneration. EMBO J. 25:5826–5839 10.1038/sj.emboj.760144117124496
Mohit Jain, Aniela Jakubowski, Lei Cui, Jianru Shi, Lihe Su, M. Bauer, J. Guan, C. Lim, Y. Naito, J. Thompson, F. Sam, C. Ambrose, M. Parr, T. Crowell, J. Lincecum, Monica Wang, Y. Hsu, T. Zheng, J. Michaelson, R. Liao, L. Burkly (2009)
A Novel Role for Tumor Necrosis Factor–Like Weak Inducer of Apoptosis (TWEAK) in the Development of Cardiac Dysfunction and Failure
Circulation, 119

Publisher: Pubmed Central
ISSN: 0021-9525
eISSN: 1540-8140
DOI: 10.1083/jcb.200909117
Publisher site: See Article on Publisher Site

Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 7-Day Trial for You or Your Team.

Learn More →

The TWEAK–Fn14 system is a critical regulator of denervation-induced skeletal muscle atrophy in mice

The TWEAK–Fn14 system is a critical regulator of denervation-induced skeletal muscle atrophy in mice

Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 7-Day Trial for You or Your Team.

Learn More →

The TWEAK–Fn14 system is a critical regulator of denervation-induced skeletal muscle atrophy in mice

The TWEAK–Fn14 system is a critical regulator of denervation-induced skeletal muscle atrophy in mice

References (112)

Abstract

Journal

Recommended Articles

There are no references for this article.

Our policy towards the use of cookies