메뉴 건너뛰기




Volumn 86, Issue 7, 2008, Pages 747-759

NF-κB signaling in skeletal muscle: Prospects for intervention in muscle diseases

Author keywords

Genetic and pharmacological models; Muscle diseases; NF B transcription factor

Indexed keywords

CALPAIN 3; CREATINE KINASE MM; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIN D1; ESTROGEN RECEPTOR ALPHA; I KAPPA B ALPHA; I KAPPA B BETA; I KAPPA B KINASE BETA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1BETA; INTERLEUKIN 6; LYMPHOTOXIN; MITOGEN ACTIVATED PROTEIN KINASE P38; MUSCLE RING FINGER 1 PROTEIN; MYOD PROTEIN; PROTEIN BAX; PROTEIN BCL 3; PROTEIN P100; PROTEIN P50; PROTEIN P52; PROTEIN P75; SYNAPTOTAGMIN I; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR REL; TRANSCRIPTION FACTOR RELA; TUMOR NECROSIS FACTOR ALPHA; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; UBIQUITIN PROTEIN LIGASE E3; UNINDEXED DRUG;

EID: 46149126918     PISSN: 09462716     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00109-008-0308-4     Document Type: Review
Times cited : (106)

References (104)
  • 1
    • 0036781052 scopus 로고    scopus 로고
    • NF-kappaB regulation in the immune system
    • 10
    • Li Q, Verma IM (2002) NF-kappaB regulation in the immune system. Nat Rev Immunol 2(10):725-734
    • (2002) Nat Rev Immunol , vol.2 , pp. 725-734
    • Li, Q.1    Verma, I.M.2
  • 2
    • 0442323562 scopus 로고    scopus 로고
    • NF-kappaB: Tumor promoter or suppressor
    • 2
    • Perkins ND (2004) NF-kappaB: tumor promoter or suppressor. Trends Cell Biol 14(2):64-69
    • (2004) Trends Cell Biol , vol.14 , pp. 64-69
    • Perkins, N.D.1
  • 3
    • 0032941594 scopus 로고    scopus 로고
    • Calpain 3 deficiency is associated with myonuclear apoptosis and profound perturbation of the IkappaB alpha/NF-kappaB pathway in limb-girdle muscular dystrophy type 2A
    • 5
    • Baghdiguian S et al (1999) Calpain 3 deficiency is associated with myonuclear apoptosis and profound perturbation of the IkappaB alpha/NF-kappaB pathway in limb-girdle muscular dystrophy type 2A. Nat Med 5(5):503-511
    • (1999) Nat Med , vol.5 , pp. 503-511
    • Baghdiguian, S.1
  • 4
    • 5444262078 scopus 로고    scopus 로고
    • IKKbeta/NF-kappaB activation causes severe muscle wasting in mice
    • 2
    • Cai D et al (2004) IKKbeta/NF-kappaB activation causes severe muscle wasting in mice. Cell 119(2):285-298
    • (2004) Cell , vol.119 , pp. 285-298
    • Cai, D.1
  • 5
    • 33750595325 scopus 로고    scopus 로고
    • Targeted ablation of IKK2 improves skeletal muscle strength, maintains mass, and promotes regeneration
    • 11
    • Mourkioti F et al (2006) Targeted ablation of IKK2 improves skeletal muscle strength, maintains mass, and promotes regeneration. J Clin Invest 116(11):2945-2954
    • (2006) J Clin Invest , vol.116 , pp. 2945-2954
    • Mourkioti, F.1
  • 6
    • 32144450234 scopus 로고    scopus 로고
    • Skin lesion development in a mouse model of incontinentia pigmenti is triggered by NEMO deficiency in epidermal keratinocytes and requires TNF signaling
    • 4
    • Nenci A et al (2006) Skin lesion development in a mouse model of incontinentia pigmenti is triggered by NEMO deficiency in epidermal keratinocytes and requires TNF signaling. Hum Mol Genet 15(4):531-542
    • (2006) Hum Mol Genet , vol.15 , pp. 531-542
    • Nenci, A.1
  • 7
    • 33747609345 scopus 로고    scopus 로고
    • Inhibition of transcription factor NF-kappaB in the central nervous system ameliorates autoimmune encephalomyelitis in mice
    • 9
    • van Loo G et al (2006) Inhibition of transcription factor NF-kappaB in the central nervous system ameliorates autoimmune encephalomyelitis in mice. Nat Immunol 7(9):954-961
    • (2006) Nat Immunol , vol.7 , pp. 954-961
    • Van Loo, G.1
  • 8
    • 34047189274 scopus 로고    scopus 로고
    • Normal epidermal differentiation but impaired skin-barrier formation upon keratinocyte-restricted IKK1 ablation
    • 4
    • Gareus R et al (2007) Normal epidermal differentiation but impaired skin-barrier formation upon keratinocyte-restricted IKK1 ablation. Nat Cell Biol 9(4):461-469
    • (2007) Nat Cell Biol , vol.9 , pp. 461-469
    • Gareus, R.1
  • 9
    • 34249807348 scopus 로고    scopus 로고
    • P38alpha MAP kinase is essential in lung stem and progenitor cell proliferation and differentiation
    • 6
    • Ventura JJ et al (2007) p38alpha MAP kinase is essential in lung stem and progenitor cell proliferation and differentiation. Nat Genet 39(6):750-758
    • (2007) Nat Genet , vol.39 , pp. 750-758
    • Ventura, J.J.1
  • 10
    • 0031897632 scopus 로고    scopus 로고
    • NF-kappa B and Rel proteins: Evolutionarily conserved mediators of immune responses
    • Ghosh S, May MJ, Kopp EB (1998) NF-kappa B and Rel proteins: evolutionarily conserved mediators of immune responses. Annu Rev Immunol 16:225-260
    • (1998) Annu Rev Immunol , vol.16 , pp. 225-260
    • Ghosh, S.1    May, M.J.2    Kopp, E.B.3
  • 11
    • 4444376712 scopus 로고    scopus 로고
    • Signaling to NF-kappaB
    • 18
    • Hayden MS, Ghosh S (2004) Signaling to NF-kappaB. Genes Dev 18(18):2195-2224
    • (2004) Genes Dev , vol.18 , pp. 2195-2224
    • Hayden, M.S.1    Ghosh, S.2
  • 12
    • 39049183044 scopus 로고    scopus 로고
    • Regulation and function of IKK and IKK-related kinases
    • 357
    • Hacker H, Karin M (2006) Regulation and function of IKK and IKK-related kinases. Sci STKE 2006(357):re13
    • (2006) Sci STKE , vol.2006 , pp. 13
    • Hacker, H.1    Karin, M.2
  • 13
    • 0025943986 scopus 로고
    • The p65 subunit is responsible for the strong transcription activating potential of NF-kappa B
    • 12
    • Schmitz ML, Baeuerle PA (1991) The p65 subunit is responsible for the strong transcription activating potential of NF-kappa B. EMBO J 10(12):3805-3817
    • (1991) EMBO J , vol.10 , pp. 3805-3817
    • Schmitz, M.L.1    Baeuerle, P.A.2
  • 14
    • 0029843343 scopus 로고    scopus 로고
    • Differential regulation of NF-kappaB2(p100) processing and control by amino-terminal sequences
    • 11
    • Betts JC, Nabel GJ (1996) Differential regulation of NF-kappaB2(p100) processing and control by amino-terminal sequences. Mol Cell Biol 16(11):6363-6371
    • (1996) Mol Cell Biol , vol.16 , pp. 6363-6371
    • Betts, J.C.1    Nabel, G.J.2
  • 15
    • 0026066613 scopus 로고
    • Generation of p50 subunit of NF-kappa B by processing of p105 through an ATP-dependent pathway
    • 6352
    • Fan CM, Maniatis T (1991) Generation of p50 subunit of NF-kappa B by processing of p105 through an ATP-dependent pathway. Nature 354(6352):395-398
    • (1991) Nature , vol.354 , pp. 395-398
    • Fan, C.M.1    Maniatis, T.2
  • 16
    • 33845768987 scopus 로고    scopus 로고
    • Integrating cell-signalling pathways with NF-kappaB and IKK function
    • 1
    • Perkins ND (2007) Integrating cell-signalling pathways with NF-kappaB and IKK function. Nat Rev Mol Cell Biol 8(1):49-62
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 49-62
    • Perkins, N.D.1
  • 17
    • 0037192823 scopus 로고    scopus 로고
    • Signaling molecules of the NF-kappa B pathway shuttle constitutively between cytoplasm and nucleus
    • 13
    • Birbach A et al (2002) Signaling molecules of the NF-kappa B pathway shuttle constitutively between cytoplasm and nucleus. J Biol Chem 277(13):10842-10851
    • (2002) J Biol Chem , vol.277 , pp. 10842-10851
    • Birbach, A.1
  • 18
    • 0033519690 scopus 로고    scopus 로고
    • The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators
    • 22
    • Dechend R et al (1999) The Bcl-3 oncoprotein acts as a bridging factor between NF-kappaB/Rel and nuclear co-regulators. Oncogene 18(22):3316-3323
    • (1999) Oncogene , vol.18 , pp. 3316-3323
    • Dechend, R.1
  • 19
    • 0036234459 scopus 로고    scopus 로고
    • Missing pieces in the NF-kappaB puzzle
    • Suppl
    • Ghosh S, Karin M (2002) Missing pieces in the NF-kappaB puzzle. Cell 109(Suppl):S81-S96
    • (2002) Cell , vol.109
    • Ghosh, S.1    Karin, M.2
  • 20
    • 0030613551 scopus 로고    scopus 로고
    • The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation
    • 2
    • Zandi E et al (1997) The IkappaB kinase complex (IKK) contains two kinase subunits, IKKalpha and IKKbeta, necessary for IkappaB phosphorylation and NF-kappaB activation. Cell 91(2):243-252
    • (1997) Cell , vol.91 , pp. 243-252
    • Zandi, E.1
  • 21
    • 0032568792 scopus 로고    scopus 로고
    • Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation
    • 7
    • Yamaoka S et al (1998) Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation. Cell 93(7):1231-1240
    • (1998) Cell , vol.93 , pp. 1231-1240
    • Yamaoka, S.1
  • 22
    • 23144449789 scopus 로고    scopus 로고
    • Ubiquitin signalling in the NF-kappaB pathway
    • 8
    • Chen ZJ (2005) Ubiquitin signalling in the NF-kappaB pathway. Nat Cell Biol 7(8):758-765
    • (2005) Nat Cell Biol , vol.7 , pp. 758-765
    • Chen, Z.J.1
  • 23
    • 2342464085 scopus 로고    scopus 로고
    • The two NF-kappaB activation pathways and their role in innate and adaptive immunity
    • 6
    • Bonizzi G, Karin M (2004) The two NF-kappaB activation pathways and their role in innate and adaptive immunity. Trends Immunol 25(6):280-288
    • (2004) Trends Immunol , vol.25 , pp. 280-288
    • Bonizzi, G.1    Karin, M.2
  • 24
    • 0037497184 scopus 로고    scopus 로고
    • A nucleosomal function for IkappaB kinase-alpha in NF-kappaB-dependent gene expression
    • 6940
    • Anest V et al (2003) A nucleosomal function for IkappaB kinase-alpha in NF-kappaB-dependent gene expression. Nature 423(6940):659-663
    • (2003) Nature , vol.423 , pp. 659-663
    • Anest, V.1
  • 25
    • 0038511129 scopus 로고    scopus 로고
    • Histone H3 phosphorylation by IKK-alpha is critical for cytokine-induced gene expression
    • 6940
    • Yamamoto Y et al (2003) Histone H3 phosphorylation by IKK-alpha is critical for cytokine-induced gene expression. Nature 423(6940):655-659
    • (2003) Nature , vol.423 , pp. 655-659
    • Yamamoto, Y.1
  • 26
    • 15944379896 scopus 로고    scopus 로고
    • Formation of an IKKalpha-dependent transcription complex is required for estrogen receptor-mediated gene activation
    • 1
    • Park KJ et al (2005) Formation of an IKKalpha-dependent transcription complex is required for estrogen receptor-mediated gene activation. Mol Cell 18(1):71-82
    • (2005) Mol Cell , vol.18 , pp. 71-82
    • Park, K.J.1
  • 27
    • 0037329233 scopus 로고    scopus 로고
    • IKKalpha regulates mitogenic signaling through transcriptional induction of cyclin D1 via Tcf
    • 2
    • Albanese C et al (2003) IKKalpha regulates mitogenic signaling through transcriptional induction of cyclin D1 via Tcf. Mol Biol Cell 14(2):585-599
    • (2003) Mol Biol Cell , vol.14 , pp. 585-599
    • Albanese, C.1
  • 28
    • 26644457201 scopus 로고    scopus 로고
    • IkappaB kinase alpha regulates subcellular distribution and turnover of cyclin D1 by phosphorylation
    • 40
    • Kwak YT et al (2005) IkappaB kinase alpha regulates subcellular distribution and turnover of cyclin D1 by phosphorylation. J Biol Chem 280(40):33945-33952
    • (2005) J Biol Chem , vol.280 , pp. 33945-33952
    • Kwak, Y.T.1
  • 29
    • 0035809983 scopus 로고    scopus 로고
    • IKKalpha controls formation of the epidermis independently of NF-kappaB
    • 6829
    • Hu Y et al (2001) IKKalpha controls formation of the epidermis independently of NF-kappaB. Nature 410(6829):710-714
    • (2001) Nature , vol.410 , pp. 710-714
    • Hu, Y.1
  • 30
    • 0442309823 scopus 로고    scopus 로고
    • A dual role for Ikk alpha in tooth development
    • 2
    • Ohazama A et al (2004) A dual role for Ikk alpha in tooth development. Dev Cell 6(2):219-227
    • (2004) Dev Cell , vol.6 , pp. 219-227
    • Ohazama, A.1
  • 31
    • 11144357466 scopus 로고    scopus 로고
    • IkappaB kinase promotes tumorigenesis through inhibition of forkhead FOXO3a
    • 2
    • Hu MC et al (2004) IkappaB kinase promotes tumorigenesis through inhibition of forkhead FOXO3a. Cell 117(2):225-237
    • (2004) Cell , vol.117 , pp. 225-237
    • Hu, M.C.1
  • 32
    • 22544461297 scopus 로고    scopus 로고
    • Convergent actions of I kappa B kinase beta and protein kinase C delta modulate mRNA stability through phosphorylation of 14-3-3 beta complexed with tristetraprolin
    • 15
    • Gringhuis SI et al (2005) Convergent actions of I kappa B kinase beta and protein kinase C delta modulate mRNA stability through phosphorylation of 14-3-3 beta complexed with tristetraprolin. Mol Cell Biol 25(15):6454-6463
    • (2005) Mol Cell Biol , vol.25 , pp. 6454-6463
    • Gringhuis, S.I.1
  • 33
    • 33644538632 scopus 로고    scopus 로고
    • Molecular linkage between the kinase ATM and NF-kappaB signaling in response to genotoxic stimuli
    • 5764
    • Wu ZH et al (2006) Molecular linkage between the kinase ATM and NF-kappaB signaling in response to genotoxic stimuli. Science 311(5764):1141-1146
    • (2006) Science , vol.311 , pp. 1141-1146
    • Wu, Z.H.1
  • 34
    • 34247566510 scopus 로고    scopus 로고
    • The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling
    • 5
    • O'Neill LA, Bowie AG (2007) The family of five: TIR-domain-containing adaptors in Toll-like receptor signalling. Nat Rev Immunol 7(5):353-364
    • (2007) Nat Rev Immunol , vol.7 , pp. 353-364
    • O'Neill, L.A.1    Bowie, A.G.2
  • 35
    • 0033119952 scopus 로고    scopus 로고
    • Embryonic lethality, liver degeneration, and impaired NF-kappa B activation in IKK-beta-deficient mice
    • 4
    • Tanaka M et al (1999) Embryonic lethality, liver degeneration, and impaired NF-kappa B activation in IKK-beta-deficient mice. Immunity 10(4):421-429
    • (1999) Immunity , vol.10 , pp. 421-429
    • Tanaka, M.1
  • 36
    • 33846839443 scopus 로고    scopus 로고
    • Deletion of NEMO/IKKgamma in liver parenchymal cells causes steatohepatitis and hepatocellular carcinoma
    • 2
    • Luedde T et al (2007) Deletion of NEMO/IKKgamma in liver parenchymal cells causes steatohepatitis and hepatocellular carcinoma. Cancer Cell 11(2):119-132
    • (2007) Cancer Cell , vol.11 , pp. 119-132
    • Luedde, T.1
  • 37
    • 0028176666 scopus 로고
    • Constitutive NF-kappa B activity in neurons
    • 6
    • Kaltschmidt C et al (1994) Constitutive NF-kappa B activity in neurons. Mol Cell Biol 14(6):3981-3992
    • (1994) Mol Cell Biol , vol.14 , pp. 3981-3992
    • Kaltschmidt, C.1
  • 38
    • 0034746288 scopus 로고    scopus 로고
    • NF-kappaB in neuronal plasticity and neurodegenerative disorders
    • 3
    • Mattson MP, Camandola S (2001) NF-kappaB in neuronal plasticity and neurodegenerative disorders. J Clin Invest 107(3):247-254
    • (2001) J Clin Invest , vol.107 , pp. 247-254
    • Mattson, M.P.1    Camandola, S.2
  • 39
    • 0034729346 scopus 로고    scopus 로고
    • It's got you covered. NF-kappaB in the epidermis
    • 5
    • Kaufman CK, Fuchs E (2000) It's got you covered. NF-kappaB in the epidermis. J Cell Biol 149(5):999-1004
    • (2000) J Cell Biol , vol.149 , pp. 999-1004
    • Kaufman, C.K.1    Fuchs, E.2
  • 40
    • 0037142027 scopus 로고    scopus 로고
    • TNF-mediated inflammatory skin disease in mice with epidermis-specific deletion of IKK2
    • 6891
    • Pasparakis M et al (2002) TNF-mediated inflammatory skin disease in mice with epidermis-specific deletion of IKK2. Nature 417(6891):861-866
    • (2002) Nature , vol.417 , pp. 861-866
    • Pasparakis, M.1
  • 41
    • 34047173496 scopus 로고    scopus 로고
    • Epithelial NEMO links innate immunity to chronic intestinal inflammation
    • 7135
    • Nenci A et al (2007) Epithelial NEMO links innate immunity to chronic intestinal inflammation. Nature 446(7135):557-561
    • (2007) Nature , vol.446 , pp. 557-561
    • Nenci, A.1
  • 42
    • 0034733634 scopus 로고    scopus 로고
    • Glucocorticoids induce proteasome C3 subunit expression in L6 muscle cells by opposing the suppression of its transcription by NF-kappa B
    • 26
    • Du J et al (2000) Glucocorticoids induce proteasome C3 subunit expression in L6 muscle cells by opposing the suppression of its transcription by NF-kappa B. J Biol Chem 275(26):19661-19666
    • (2000) J Biol Chem , vol.275 , pp. 19661-19666
    • Du, J.1
  • 43
    • 0032588186 scopus 로고    scopus 로고
    • NF-kappaB controls cell growth and differentiation through transcriptional regulation of cyclin D1
    • 8
    • Guttridge DC et al (1999) NF-kappaB controls cell growth and differentiation through transcriptional regulation of cyclin D1. Mol Cell Biol 19(8):5785-5799
    • (1999) Mol Cell Biol , vol.19 , pp. 5785-5799
    • Guttridge, D.C.1
  • 44
    • 33846269970 scopus 로고    scopus 로고
    • Role for IkappaBalpha, but not c-Rel, in skeletal muscle atrophy
    • 1
    • Judge AR et al (2007) Role for IkappaBalpha, but not c-Rel, in skeletal muscle atrophy. Am J Physiol Cell Physiol 292(1):C372-C382
    • (2007) Am J Physiol Cell Physiol , vol.292
    • Judge, A.R.1
  • 45
    • 11144317940 scopus 로고    scopus 로고
    • Disruption of either the Nfkb1 or the Bcl3 gene inhibits skeletal muscle atrophy
    • 10
    • Hunter RB, Kandarian SC (2004) Disruption of either the Nfkb1 or the Bcl3 gene inhibits skeletal muscle atrophy. J Clin Invest 114(10):1504-1511
    • (2004) J Clin Invest , vol.114 , pp. 1504-1511
    • Hunter, R.B.1    Kandarian, S.C.2
  • 46
    • 34250218193 scopus 로고    scopus 로고
    • NF-kappaB regulation of YY1 inhibits skeletal myogenesis through transcriptional silencing of myofibrillar genes
    • 12
    • Wang H et al (2007) NF-kappaB regulation of YY1 inhibits skeletal myogenesis through transcriptional silencing of myofibrillar genes. Mol Cell Biol 27(12):4374-4387
    • (2007) Mol Cell Biol , vol.27 , pp. 4374-4387
    • Wang, H.1
  • 47
    • 0035941020 scopus 로고    scopus 로고
    • Identification of ubiquitin ligases required for skeletal muscle atrophy
    • 5547
    • Bodine SC et al (2001) Identification of ubiquitin ligases required for skeletal muscle atrophy. Science 294(5547):1704-1708
    • (2001) Science , vol.294 , pp. 1704-1708
    • Bodine, S.C.1
  • 48
    • 34250669605 scopus 로고    scopus 로고
    • TNF-alpha regulates myogenesis and muscle regeneration by activating p38 MAPK
    • 5
    • Chen SE, Jin B, Li YP (2007) TNF-alpha regulates myogenesis and muscle regeneration by activating p38 MAPK. Am J Physiol Cell Physiol 292(5):C1660-C1671
    • (2007) Am J Physiol Cell Physiol , vol.292
    • Chen, S.E.1    Jin, B.2    Li, Y.P.3
  • 49
    • 33744542153 scopus 로고    scopus 로고
    • Tumor necrosis factor-like weak inducer of apoptosis inhibits skeletal myogenesis through sustained activation of nuclear factor-kappaB and degradation of MyoD protein
    • 15
    • Dogra C et al (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(15):10327-10336
    • (2006) J Biol Chem , vol.281 , pp. 10327-10336
    • Dogra, C.1
  • 50
    • 26844499819 scopus 로고    scopus 로고
    • Role of TNF-{alpha} signaling in regeneration of cardiotoxin-injured muscle
    • 5
    • Chen SE et al (2005) Role of TNF-{alpha} signaling in regeneration of cardiotoxin-injured muscle. Am J Physiol Cell Physiol 289(5):C1179-C1187
    • (2005) Am J Physiol Cell Physiol , vol.289
    • Chen, S.E.1
  • 51
    • 0442324933 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha inhibits myogenic differentiation through MyoD protein destabilization
    • 2
    • Langen RC et al (2004) Tumor necrosis factor-alpha inhibits myogenic differentiation through MyoD protein destabilization. FASEB J 18(2):227-237
    • (2004) FASEB J , vol.18 , pp. 227-237
    • Langen, R.C.1
  • 52
    • 0037462802 scopus 로고    scopus 로고
    • Tumor necrosis factor-regulated biphasic activation of NF-kappa B is required for cytokine-induced loss of skeletal muscle gene products
    • 4
    • Ladner KJ, Caligiuri MA, Guttridge DC (2003) Tumor necrosis factor-regulated biphasic activation of NF-kappa B is required for cytokine-induced loss of skeletal muscle gene products. J Biol Chem 278(4):2294-2303
    • (2003) J Biol Chem , vol.278 , pp. 2294-2303
    • Ladner, K.J.1    Caligiuri, M.A.2    Guttridge, D.C.3
  • 53
    • 0036720492 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha inhibits myogenesis through redox-dependent and -independent pathways
    • 3
    • Langen RC et al (2002) Tumor necrosis factor-alpha inhibits myogenesis through redox-dependent and -independent pathways. Am J Physiol Cell Physiol 283(3):C714-C721
    • (2002) Am J Physiol Cell Physiol , vol.283
    • Langen, R.C.1
  • 54
    • 0037083867 scopus 로고    scopus 로고
    • TNFalpha inhibits skeletal myogenesis through a PW1-dependent pathway by recruitment of caspase pathways
    • 4
    • Coletti D et al (2002) TNFalpha inhibits skeletal myogenesis through a PW1-dependent pathway by recruitment of caspase pathways. EMBO J 21(4):631-642
    • (2002) EMBO J , vol.21 , pp. 631-642
    • Coletti, D.1
  • 55
    • 0034923715 scopus 로고    scopus 로고
    • The role of tumor necrosis factor-alpha (TNF-alpha) in skeletal muscle regeneration. Studies in TNF-alpha(-/-) and TNF-alpha(-/-)/LT-alpha(-/-) mice
    • 8
    • Collins RA, Grounds MD (2001) The role of tumor necrosis factor-alpha (TNF-alpha) in skeletal muscle regeneration. Studies in TNF-alpha(-/-) and TNF-alpha(-/-)/LT-alpha(-/-) mice. J Histochem Cytochem 49(8):989-1001
    • (2001) J Histochem Cytochem , vol.49 , pp. 989-1001
    • Collins, R.A.1    Grounds, M.D.2
  • 56
    • 0033602762 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha and basic fibroblast growth factor differentially inhibit the insulin-like growth factor-I induced expression of myogenin in C2C12 myoblasts
    • 1
    • Layne MD, Farmer SR (1999) Tumor necrosis factor-alpha and basic fibroblast growth factor differentially inhibit the insulin-like growth factor-I induced expression of myogenin in C2C12 myoblasts. Exp Cell Res 249(1):177-187
    • (1999) Exp Cell Res , vol.249 , pp. 177-187
    • Layne, M.D.1    Farmer, S.R.2
  • 57
    • 0042242879 scopus 로고    scopus 로고
    • TNF-alpha is a mitogen in skeletal muscle
    • 2
    • Li YP (2003) TNF-alpha is a mitogen in skeletal muscle. Am J Physiol Cell Physiol 285(2):C370-C376
    • (2003) Am J Physiol Cell Physiol , vol.285
    • Li, Y.P.1
  • 58
    • 0023924058 scopus 로고
    • Tumor necrosis factor inhibits human myogenesis in vitro
    • 6
    • Miller SC et al (1988) Tumor necrosis factor inhibits human myogenesis in vitro. Mol Cell Biol 8(6):2295-2301
    • (1988) Mol Cell Biol , vol.8 , pp. 2295-2301
    • Miller, S.C.1
  • 59
    • 0025639022 scopus 로고
    • Metabolic effects of cachectin/tumor necrosis factor are modified by site of production. Cachectin/tumor necrosis factor-secreting tumor in skeletal muscle induces chronic cachexia, while implantation in brain induces predominantly acute anorexia
    • 6
    • Tracey KJ et al (1990) Metabolic effects of cachectin/tumor necrosis factor are modified by site of production. Cachectin/tumor necrosis factor-secreting tumor in skeletal muscle induces chronic cachexia, while implantation in brain induces predominantly acute anorexia. J Clin Invest 86(6):2014-2024
    • (1990) J Clin Invest , vol.86 , pp. 2014-2024
    • Tracey, K.J.1
  • 60
    • 0034730251 scopus 로고    scopus 로고
    • NF-kappaB-induced loss of MyoD messenger RNA: Possible role in muscle decay and cachexia
    • 5488
    • Guttridge DC et al (2000) NF-kappaB-induced loss of MyoD messenger RNA: possible role in muscle decay and cachexia. Science 289(5488):2363-2366
    • (2000) Science , vol.289 , pp. 2363-2366
    • Guttridge, D.C.1
  • 61
    • 0036311526 scopus 로고    scopus 로고
    • RIP2, a checkpoint in myogenic differentiation
    • 16
    • Munz B et al (2002) RIP2, a checkpoint in myogenic differentiation. Mol Cell Biol 22(16):5879-5886
    • (2002) Mol Cell Biol , vol.22 , pp. 5879-5886
    • Munz, B.1
  • 62
    • 0031463025 scopus 로고    scopus 로고
    • Early lethality, functional NF-kappaB activation, and increased sensitivity to TNF-induced cell death in TRAF2-deficient mice
    • 5
    • Yeh WC et al (1997) Early lethality, functional NF-kappaB activation, and increased sensitivity to TNF-induced cell death in TRAF2-deficient mice. Immunity 7(5):715-725
    • (1997) Immunity , vol.7 , pp. 715-725
    • Yeh, W.C.1
  • 63
    • 0032534588 scopus 로고    scopus 로고
    • TRAF2 expression in differentiated muscle
    • 4
    • MacLachlan TK, Giordano A (1998) TRAF2 expression in differentiated muscle. J Cell Biochem 71(4):461-466
    • (1998) J Cell Biochem , vol.71 , pp. 461-466
    • MacLachlan, T.K.1    Giordano, A.2
  • 64
    • 9044253328 scopus 로고    scopus 로고
    • Peg3 imprinted gene on proximal chromosome 7 encodes for a zinc finger protein
    • 2
    • Kuroiwa Y et al (1996) Peg3 imprinted gene on proximal chromosome 7 encodes for a zinc finger protein. Nat Genet 12(2):186-190
    • (1996) Nat Genet , vol.12 , pp. 186-190
    • Kuroiwa, Y.1
  • 65
    • 0031906851 scopus 로고    scopus 로고
    • Peg3/Pw1 is an imprinted gene involved in the TNF-NFkappaB signal transduction pathway
    • 3
    • Relaix F et al (1998) Peg3/Pw1 is an imprinted gene involved in the TNF-NFkappaB signal transduction pathway. Nat Genet 18(3):287-291
    • (1998) Nat Genet , vol.18 , pp. 287-291
    • Relaix, F.1
  • 66
    • 0030220274 scopus 로고    scopus 로고
    • Pw1, a novel zinc finger gene implicated in the myogenic and neuronal lineages
    • 2
    • Relaix F et al (1996) Pw1, a novel zinc finger gene implicated in the myogenic and neuronal lineages. Dev Biol 177(2):383-396
    • (1996) Dev Biol , vol.177 , pp. 383-396
    • Relaix, F.1
  • 67
    • 30444440735 scopus 로고    scopus 로고
    • Regulation of skeletal muscle gene expression by p38 MAP kinases
    • 1
    • Lluis F et al (2006) Regulation of skeletal muscle gene expression by p38 MAP kinases. Trends Cell Biol 16(1):36-44
    • (2006) Trends Cell Biol , vol.16 , pp. 36-44
    • Lluis, F.1
  • 68
    • 0037711091 scopus 로고    scopus 로고
    • TNF-alpha increases ubiquitin-conjugating activity in skeletal muscle by up-regulating UbcH2/E220k
    • 9
    • Li YP et al (2003) TNF-alpha increases ubiquitin-conjugating activity in skeletal muscle by up-regulating UbcH2/E220k. FASEB J 17(9):1048-1057
    • (2003) FASEB J , vol.17 , pp. 1048-1057
    • Li, Y.P.1
  • 69
    • 0034967925 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and proteasome inhibitors
    • 4
    • Myung J, Kim KB, Crews CM (2001) The ubiquitin-proteasome pathway and proteasome inhibitors. Med Res Rev 21(4):245-273
    • (2001) Med Res Rev , vol.21 , pp. 245-273
    • Myung, J.1    Kim, K.B.2    Crews, C.M.3
  • 70
    • 1642423481 scopus 로고    scopus 로고
    • P38 MAPK-induced nuclear factor-kappaB activity is required for skeletal muscle differentiation: Role of interleukin-6
    • 4
    • Baeza-Raja B, Munoz-Canoves P (2004) p38 MAPK-induced nuclear factor-kappaB activity is required for skeletal muscle differentiation: role of interleukin-6. Mol Biol Cell 15(4):2013-2026
    • (2004) Mol Biol Cell , vol.15 , pp. 2013-2026
    • Baeza-Raja, B.1    Munoz-Canoves, P.2
  • 71
    • 0023620504 scopus 로고
    • Interleukin 1 and tumor necrosis factor do not regulate protein balance in skeletal muscle
    • 6 Pt 1
    • Moldawer LL et al (1987) Interleukin 1 and tumor necrosis factor do not regulate protein balance in skeletal muscle. Am J Physiol 253(6 Pt 1):C766-C773
    • (1987) Am J Physiol , vol.253
    • Moldawer, L.L.1
  • 72
    • 0037400609 scopus 로고    scopus 로고
    • Calcineurin activates NF-kappaB in skeletal muscle C2C12 cells
    • 5
    • Alzuherri H, Chang KC (2003) Calcineurin activates NF-kappaB in skeletal muscle C2C12 cells. Cell Signal 15(5):471-478
    • (2003) Cell Signal , vol.15 , pp. 471-478
    • Alzuherri, H.1    Chang, K.C.2
  • 74
    • 11144324372 scopus 로고    scopus 로고
    • Molecular mechanisms of muscle atrophy
    • 7
    • McKinnell IW, Rudnicki MA (2004) Molecular mechanisms of muscle atrophy. Cell 119(7):907-910
    • (2004) Cell , vol.119 , pp. 907-910
    • McKinnell, I.W.1    Rudnicki, M.A.2
  • 75
    • 0036208356 scopus 로고    scopus 로고
    • Activation of an alternative NF-kappaB pathway in skeletal muscle during disuse atrophy
    • 6
    • Hunter RB et al (2002) Activation of an alternative NF-kappaB pathway in skeletal muscle during disuse atrophy. FASEB J 16(6):529-538
    • (2002) FASEB J , vol.16 , pp. 529-538
    • Hunter, R.B.1
  • 76
    • 14644444464 scopus 로고    scopus 로고
    • Anabolic signaling deficits underlie amino acid resistance of wasting, aging muscle
    • 3
    • Cuthbertson D et al (2005) Anabolic signaling deficits underlie amino acid resistance of wasting, aging muscle. FASEB J 19(3):422-424
    • (2005) FASEB J , vol.19 , pp. 422-424
    • Cuthbertson, D.1
  • 77
    • 0037160782 scopus 로고    scopus 로고
    • The muscular dystrophies
    • 9307
    • Emery AE (2002) The muscular dystrophies. Lancet 359(9307):687-695
    • (2002) Lancet , vol.359 , pp. 687-695
    • Emery, A.E.1
  • 78
    • 0345731966 scopus 로고
    • X chromosome-linked muscular dystrophy (mdx) in the mouse
    • 4
    • Bulfield G et al (1984) X chromosome-linked muscular dystrophy (mdx) in the mouse. Proc Natl Acad Sci U S A 81(4):1189-1192
    • (1984) Proc Natl Acad Sci U S a , vol.81 , pp. 1189-1192
    • Bulfield, G.1
  • 79
    • 24744449943 scopus 로고    scopus 로고
    • IGF-1, inflammation and stem cells: Interactions during muscle regeneration
    • 10
    • Mourkioti F, Rosenthal N (2005) IGF-1, inflammation and stem cells: interactions during muscle regeneration. Trends Immunol 26(10):535-542
    • (2005) Trends Immunol , vol.26 , pp. 535-542
    • Mourkioti, F.1    Rosenthal, N.2
  • 80
    • 0036471858 scopus 로고    scopus 로고
    • A chronic inflammatory response dominates the skeletal muscle molecular signature in dystrophin-deficient mdx mice
    • 3
    • Porter JD et al (2002) A chronic inflammatory response dominates the skeletal muscle molecular signature in dystrophin-deficient mdx mice. Hum Mol Genet 11(3):263-272
    • (2002) Hum Mol Genet , vol.11 , pp. 263-272
    • Porter, J.D.1
  • 81
    • 0037465720 scopus 로고    scopus 로고
    • Activation of nuclear factor-kappaB in inflammatory myopathies and Duchenne muscular dystrophy
    • 6
    • Monici MC et al (2003) Activation of nuclear factor-kappaB in inflammatory myopathies and Duchenne muscular dystrophy. Neurology 60(6):993-997
    • (2003) Neurology , vol.60 , pp. 993-997
    • Monici, M.C.1
  • 82
    • 0037373615 scopus 로고    scopus 로고
    • Persistent over-expression of specific CC class chemokines correlates with macrophage and T-cell recruitment in mdx skeletal muscle
    • 3
    • Porter JD et al (2003) Persistent over-expression of specific CC class chemokines correlates with macrophage and T-cell recruitment in mdx skeletal muscle. Neuromuscul Disord 13(3):223-235
    • (2003) Neuromuscul Disord , vol.13 , pp. 223-235
    • Porter, J.D.1
  • 83
    • 34147122660 scopus 로고    scopus 로고
    • Interplay of IKK/NF-kappaB signaling in macrophages and myofibers promotes muscle degeneration in Duchenne muscular dystrophy
    • 4
    • Acharyya S et al (2007) Interplay of IKK/NF-kappaB signaling in macrophages and myofibers promotes muscle degeneration in Duchenne muscular dystrophy. J Clin Invest 117(4):889-901
    • (2007) J Clin Invest , vol.117 , pp. 889-901
    • Acharyya, S.1
  • 84
    • 0034937370 scopus 로고    scopus 로고
    • Pathophysiology of limb girdle muscular dystrophy type 2A: Hypothesis and new insights into the IkappaBalpha/NF-kappaB survival pathway in skeletal muscle
    • 5-6
    • Baghdiguian S et al (2001) Pathophysiology of limb girdle muscular dystrophy type 2A: hypothesis and new insights into the IkappaBalpha/NF-kappaB survival pathway in skeletal muscle. J Mol Med 79(5-6):254-261
    • (2001) J Mol Med , vol.79 , pp. 254-261
    • Baghdiguian, S.1
  • 85
    • 0344875464 scopus 로고    scopus 로고
    • Cytokines, chemokines, and cell adhesion molecules in inflammatory myopathies
    • 6
    • Figarella-Branger D et al (2003) Cytokines, chemokines, and cell adhesion molecules in inflammatory myopathies. Muscle Nerve 28(6):659-682
    • (2003) Muscle Nerve , vol.28 , pp. 659-682
    • Figarella-Branger, D.1
  • 86
    • 0032566756 scopus 로고    scopus 로고
    • Immunolocalization of transcription factor NF-kappaB in inclusion-body myositis muscle and at normal human neuromuscular junctions
    • 2
    • Yang CC et al (1998) Immunolocalization of transcription factor NF-kappaB in inclusion-body myositis muscle and at normal human neuromuscular junctions. Neurosci Lett 254(2):77-80
    • (1998) Neurosci Lett , vol.254 , pp. 77-80
    • Yang, C.C.1
  • 87
    • 0033787688 scopus 로고    scopus 로고
    • Altered pathological progression of diaphragm and quadriceps muscle in TNF-deficient, dystrophin-deficient mice
    • 8
    • Spencer MJ, Marino MW, Winckler WM (2000) Altered pathological progression of diaphragm and quadriceps muscle in TNF-deficient, dystrophin-deficient mice. Neuromuscul Disord 10(8):612-619
    • (2000) Neuromuscul Disord , vol.10 , pp. 612-619
    • Spencer, M.J.1    Marino, M.W.2    Winckler, W.M.3
  • 88
    • 11144356766 scopus 로고    scopus 로고
    • Conditional disruption of IkappaB kinase 2 fails to prevent obesity-induced insulin resistance
    • 3
    • Rohl M et al (2004) Conditional disruption of IkappaB kinase 2 fails to prevent obesity-induced insulin resistance. J Clin Invest 113(3):474-481
    • (2004) J Clin Invest , vol.113 , pp. 474-481
    • Rohl, M.1
  • 89
    • 33750446341 scopus 로고    scopus 로고
    • Inhibitors of NF-kappaB signaling: 785 and counting
    • 51
    • Gilmore TD, Herscovitch M (2006) Inhibitors of NF-kappaB signaling: 785 and counting. Oncogene 25(51):6887-6899
    • (2006) Oncogene , vol.25 , pp. 6887-6899
    • Gilmore, T.D.1    Herscovitch, M.2
  • 90
    • 1842454966 scopus 로고    scopus 로고
    • Anti-TNFalpha (Remicade) therapy protects dystrophic skeletal muscle from necrosis
    • 6
    • Grounds MD, Torrisi J (2004) Anti-TNFalpha (Remicade) therapy protects dystrophic skeletal muscle from necrosis. FASEB J 18(6):676-682
    • (2004) FASEB J , vol.18 , pp. 676-682
    • Grounds, M.D.1    Torrisi, J.2
  • 91
    • 21244438311 scopus 로고    scopus 로고
    • Silencing TNFalpha activity by using Remicade or Enbrel blocks inflammation in whole muscle grafts: An in vivo bioassay to assess the efficacy of anti-cytokine drugs in mice
    • 3
    • Grounds MD et al (2005) Silencing TNFalpha activity by using Remicade or Enbrel blocks inflammation in whole muscle grafts: an in vivo bioassay to assess the efficacy of anti-cytokine drugs in mice. Cell Tissue Res 320(3):509-515
    • (2005) Cell Tissue Res , vol.320 , pp. 509-515
    • Grounds, M.D.1
  • 92
    • 28844451913 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha gene transfer induces cachexia and inhibits muscle regeneration
    • 3
    • Coletti D et al (2005) Tumor necrosis factor-alpha gene transfer induces cachexia and inhibits muscle regeneration. Genesis 43(3):120-128
    • (2005) Genesis , vol.43 , pp. 120-128
    • Coletti, D.1
  • 93
    • 32644442731 scopus 로고    scopus 로고
    • Nuclear factor kappa-B blockade reduces skeletal muscle degeneration and enhances muscle function in Mdx mice
    • 1
    • Messina S et al (2006) Nuclear factor kappa-B blockade reduces skeletal muscle degeneration and enhances muscle function in Mdx mice. Exp Neurol 198(1):234-241
    • (2006) Exp Neurol , vol.198 , pp. 234-241
    • Messina, S.1
  • 94
    • 34250370973 scopus 로고    scopus 로고
    • Curcumin suppresses AP1 transcription factor-dependent differentiation and activates apoptosis in human epidermal keratinocytes
    • 9
    • Balasubramanian S, Eckert RL (2007) Curcumin suppresses AP1 transcription factor-dependent differentiation and activates apoptosis in human epidermal keratinocytes. J Biol Chem 282(9):6707-6715
    • (2007) J Biol Chem , vol.282 , pp. 6707-6715
    • Balasubramanian, S.1    Eckert, R.L.2
  • 95
    • 34447328075 scopus 로고    scopus 로고
    • Up-regulation of aldose reductase expression mediated by phosphatidylinositol 3-kinase/Akt and Nrf2 is involved in the protective effect of curcumin against oxidative damage
    • 4
    • Kang ES et al (2007) Up-regulation of aldose reductase expression mediated by phosphatidylinositol 3-kinase/Akt and Nrf2 is involved in the protective effect of curcumin against oxidative damage. Free Radic Biol Med 43(4):535-545
    • (2007) Free Radic Biol Med , vol.43 , pp. 535-545
    • Kang, E.S.1
  • 96
    • 0038663090 scopus 로고    scopus 로고
    • Erk activation is required for Nrf2 nuclear localization during pyrrolidine dithiocarbamate induction of glutamate cysteine ligase modulatory gene expression in HepG2 cells
    • 1
    • Zipper LM, Mulcahy RT (2003) Erk activation is required for Nrf2 nuclear localization during pyrrolidine dithiocarbamate induction of glutamate cysteine ligase modulatory gene expression in HepG2 cells. Toxicol Sci 73(1):124-134
    • (2003) Toxicol Sci , vol.73 , pp. 124-134
    • Zipper, L.M.1    Mulcahy, R.T.2
  • 97
    • 0028167846 scopus 로고
    • Inhibition of NF-kappa B by sodium salicylate and aspirin
    • 5174
    • Kopp E, Ghosh S (1994) Inhibition of NF-kappa B by sodium salicylate and aspirin. Science 265(5174):956-959
    • (1994) Science , vol.265 , pp. 956-959
    • Kopp, E.1    Ghosh, S.2
  • 98
    • 0037188750 scopus 로고    scopus 로고
    • Anti-inflammatory effects of aspirin and sodium salicylate
    • 1
    • Amann R, Peskar BA (2002) Anti-inflammatory effects of aspirin and sodium salicylate. Eur J Pharmacol 447(1):1-9
    • (2002) Eur J Pharmacol , vol.447 , pp. 1-9
    • Amann, R.1    Peskar, B.A.2
  • 99
    • 0028787659 scopus 로고
    • Pentoxifylline for treatment of cancer anorexia and cachexia? a randomized, double-blind, placebo-controlled trial
    • 11
    • Goldberg RM et al (1995) Pentoxifylline for treatment of cancer anorexia and cachexia? A randomized, double-blind, placebo-controlled trial. J Clin Oncol 13(11):2856-2859
    • (1995) J Clin Oncol , vol.13 , pp. 2856-2859
    • Goldberg, R.M.1
  • 100
    • 15444379633 scopus 로고    scopus 로고
    • Thalidomide in the treatment of cancer cachexia: A randomised placebo controlled trial
    • 4
    • Gordon JN et al (2005) Thalidomide in the treatment of cancer cachexia: a randomised placebo controlled trial. Gut 54(4):540-545
    • (2005) Gut , vol.54 , pp. 540-545
    • Gordon, J.N.1
  • 101
    • 33845689427 scopus 로고    scopus 로고
    • TWEAK, via its receptor Fn14, is a novel regulator of mesenchymal progenitor cells and skeletal muscle regeneration
    • 24
    • Girgenrath M et al (2006) TWEAK, via its receptor Fn14, is a novel regulator of mesenchymal progenitor cells and skeletal muscle regeneration. EMBO J 25(24):5826-5839
    • (2006) EMBO J , vol.25 , pp. 5826-5839
    • Girgenrath, M.1
  • 102
    • 0032833681 scopus 로고    scopus 로고
    • Systemic administration of the NF-kappaB inhibitor curcumin stimulates muscle regeneration after traumatic injury
    • 2 Pt 1
    • Thaloor D et al (1999) Systemic administration of the NF-kappaB inhibitor curcumin stimulates muscle regeneration after traumatic injury. Am J Physiol 277(2 Pt 1):C320-C329
    • (1999) Am J Physiol , vol.277
    • Thaloor, D.1
  • 103
    • 0036778388 scopus 로고    scopus 로고
    • Physiological role of tumor necrosis factor alpha in traumatic muscle injury
    • 12
    • Warren GL et al (2002) Physiological role of tumor necrosis factor alpha in traumatic muscle injury. FASEB J 16(12):1630-1632
    • (2002) FASEB J , vol.16 , pp. 1630-1632
    • Warren, G.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.