메뉴 건너뛰기




Volumn 33, Issue 2, 2006, Pages 155-165

Intracellular signaling during skeletal muscle atrophy

Author keywords

FOXO; Inactivity; Muscle wasting; NF kappaB; PI3K Akt; Ubiquitin ligases

Indexed keywords

CASPASE 3; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; SOMATOMEDIN; TRANSCRIPTION FACTOR FOXO; UBIQUITIN PROTEIN LIGASE;

EID: 32144457727     PISSN: 0148639X     EISSN: 10974598     Source Type: Journal    
DOI: 10.1002/mus.20442     Document Type: Review
Times cited : (301)

References (94)
  • 1
    • 0033558684 scopus 로고    scopus 로고
    • Apoptosis in skeletal myocytes of patients with chronic heart failure is associated with exercise intolerance
    • Adams V, Jiang H, Yu J, Mobius-Winkler S, Fiehn E, Linke A, et al. Apoptosis in skeletal myocytes of patients with chronic heart failure is associated with exercise intolerance. J Am Coll Cardiol 1999;33:959-965.
    • (1999) J Am Coll Cardiol , vol.33 , pp. 959-965
    • Adams, V.1    Jiang, H.2    Yu, J.3    Mobius-Winkler, S.4    Fiehn, E.5    Linke, A.6
  • 2
    • 13944269898 scopus 로고    scopus 로고
    • The AKT/I kappa B kinase pathway promotes angiogenic/metastatic gene expression in colorectal cancer by activating nuclear factor-kappa B and beta-catenin
    • Agarwal A, Das K, Lerner N, Sathe S, Cicek M, Casey G, et al. The AKT/I kappa B kinase pathway promotes angiogenic/metastatic gene expression in colorectal cancer by activating nuclear factor-kappa B and beta-catenin. Oncogene 2005;24:1021-1031.
    • (2005) Oncogene , vol.24 , pp. 1021-1031
    • Agarwal, A.1    Das, K.2    Lerner, N.3    Sathe, S.4    Cicek, M.5    Casey, G.6
  • 3
    • 0030782993 scopus 로고    scopus 로고
    • Apoptosis: A mechanism contributing to remodeling of skeletal muscle in response to hindlimb unweighting
    • Allen DL, Linderman JK, Roy RR, Bigbee AJ, Grindeland RE, Mukku V, et al. Apoptosis: a mechanism contributing to remodeling of skeletal muscle in response to hindlimb unweighting. Am J Physiol 1997;273:C579-C587.
    • (1997) Am J Physiol , vol.273
    • Allen, D.L.1    Linderman, J.K.2    Roy, R.R.3    Bigbee, A.J.4    Grindeland, R.E.5    Mukku, V.6
  • 4
    • 0032833852 scopus 로고    scopus 로고
    • Myonuclear domains in muscle adaptation and disease
    • Allen DL, Roy RR, Edgerton VR. Myonuclear domains in muscle adaptation and disease. Muscle Nerve 1999;22:1350-1360.
    • (1999) Muscle Nerve , vol.22 , pp. 1350-1360
    • Allen, D.L.1    Roy, R.R.2    Edgerton, V.R.3
  • 5
    • 0033119212 scopus 로고    scopus 로고
    • Adaptation of the ubiquitin-proteasome proteolytic pathway in cancer cachexia
    • Attaix D, Combaret L, Tilignac T, Taillandier D. Adaptation of the ubiquitin-proteasome proteolytic pathway in cancer cachexia. Mol Biol Rep 1999;26:77-82.
    • (1999) Mol Biol Rep , vol.26 , pp. 77-82
    • Attaix, D.1    Combaret, L.2    Tilignac, T.3    Taillandier, D.4
  • 6
    • 0029874138 scopus 로고    scopus 로고
    • The NF-kappaB and IkappaB proteins: New discoveries and insights
    • Baldwin AS Jr. The NF-kappaB and IkappaB proteins: new discoveries and insights. Annu Rev Immunol 1996;14:649-683.
    • (1996) Annu Rev Immunol , vol.14 , pp. 649-683
    • Baldwin Jr., A.S.1
  • 7
    • 0035883480 scopus 로고    scopus 로고
    • Management of muscle wasting in cancer-associated cachexia: Understanding gained from experimental studies
    • Baracos VE. Management of muscle wasting in cancer-associated cachexia: understanding gained from experimental studies. Cancer 2001;92:1669-1677.
    • (2001) Cancer , vol.92 , pp. 1669-1677
    • Baracos, V.E.1
  • 8
    • 16544374323 scopus 로고    scopus 로고
    • Expanded nuclear roles for IkappaBs
    • Bates PW, Miyamoto S. Expanded nuclear roles for IkappaBs. Sci STKE 2004;2004:pe48.
    • (2004) Sci STKE , vol.2004
    • Bates, P.W.1    Miyamoto, S.2
  • 9
    • 0035941020 scopus 로고    scopus 로고
    • Identification of ubiquitin ligases required for skeletal muscle atrophy
    • Bodine SC, Latres E, Baumhueter S, Lai VK, Nunez L, Clarke BA, et al. Identification of ubiquitin ligases required for skeletal muscle atrophy. Science 2001;294:1704-1708.
    • (2001) Science , vol.294 , pp. 1704-1708
    • Bodine, S.C.1    Latres, E.2    Baumhueter, S.3    Lai, V.K.4    Nunez, L.5    Clarke, B.A.6
  • 10
    • 0035736260 scopus 로고    scopus 로고
    • Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo
    • Bodine SC, Stitt TN, Gonzalez M, Kline WO, Stover GL, Bauerlein R, et al. Akt/mTOR pathway is a crucial regulator of skeletal muscle hypertrophy and can prevent muscle atrophy in vivo. Nat Cell Biol 2001;3:1014-1019.
    • (2001) Nat Cell Biol , vol.3 , pp. 1014-1019
    • Bodine, S.C.1    Stitt, T.N.2    Gonzalez, M.3    Kline, W.O.4    Stover, G.L.5    Bauerlein, R.6
  • 12
    • 0035793703 scopus 로고    scopus 로고
    • Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain
    • Centner T, Yano J, Kimura E, McElhinny AS, Pelin K, Witt CC, et al. Identification of muscle specific ring finger proteins as potential regulators of the titin kinase domain. J Mol Biol 2001;306:717-726.
    • (2001) J Mol Biol , vol.306 , pp. 717-726
    • Centner, T.1    Yano, J.2    Kimura, E.3    McElhinny, A.S.4    Pelin, K.5    Witt, C.C.6
  • 13
    • 2342522110 scopus 로고    scopus 로고
    • Shaping the nuclear action of NF-kappaB
    • Chen LF, Greene WC. Shaping the nuclear action of NF-kappaB. Nat Rev Mol Cell Biol 2004;5:392-401.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 392-401
    • Chen, L.F.1    Greene, W.C.2
  • 14
    • 0035448879 scopus 로고    scopus 로고
    • Growth retardation and increased apoptosis in mice with homozygous disruption of the Akt1 gene
    • Chen WS, Xu PZ, Gottlob K, Chen ML, Sokol K, Shiyanova T, et al. Growth retardation and increased apoptosis in mice with homozygous disruption of the Akt1 gene. Genes Dev 2001;15:2203-2208.
    • (2001) Genes Dev , vol.15 , pp. 2203-2208
    • Chen, W.S.1    Xu, P.Z.2    Gottlob, K.3    Chen, M.L.4    Sokol, K.5    Shiyanova, T.6
  • 15
    • 0033913119 scopus 로고    scopus 로고
    • Cancer cachexia: From experimental models to patient management
    • Costelli P, Baccino FM. Cancer cachexia: from experimental models to patient management. Curr Opin Clin Nutr Metab Care 2000;3:177-181.
    • (2000) Curr Opin Clin Nutr Metab Care , vol.3 , pp. 177-181
    • Costelli, P.1    Baccino, F.M.2
  • 16
    • 0035968313 scopus 로고    scopus 로고
    • A novel human striated muscle RING zinc finger protein, SMRZ, interacts with SMT3b via its RING domain
    • Dai KS, Liew CC. A novel human striated muscle RING zinc finger protein, SMRZ, interacts with SMT3b via its RING domain. J Biol Chem 2001;276:23992- 23999.
    • (2001) J Biol Chem , vol.276 , pp. 23992-23999
    • Dai, K.S.1    Liew, C.C.2
  • 17
    • 85047693596 scopus 로고    scopus 로고
    • Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions
    • Du J, Wang X, Miereies C, Bailey JL, Debigare R, Zheng B, et al. Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions. J Clin Invest 2004;113:115-123.
    • (2004) J Clin Invest , vol.113 , pp. 115-123
    • Du, J.1    Wang, X.2    Miereies, C.3    Bailey, J.L.4    Debigare, R.5    Zheng, B.6
  • 18
    • 0033883216 scopus 로고    scopus 로고
    • Physiology of a microgravity environment invited review: Microgravity and skeletal muscle
    • Fitts RH, Riley DR, Widrick JJ. Physiology of a microgravity environment invited review: microgravity and skeletal muscle. J Appl Physiol 2000;89:823-839.
    • (2000) J Appl Physiol , vol.89 , pp. 823-839
    • Fitts, R.H.1    Riley, D.R.2    Widrick, J.J.3
  • 19
    • 0033899769 scopus 로고    scopus 로고
    • Complement activation promotes muscle inflammation during modified muscle use
    • Frenette J, Cai B, Tidball JG. Complement activation promotes muscle inflammation during modified muscle use. Am J Pathol 2000;156:2103-2110.
    • (2000) Am J Pathol , vol.156 , pp. 2103-2110
    • Frenette, J.1    Cai, B.2    Tidball, J.G.3
  • 20
    • 0027184023 scopus 로고
    • The candidate proto-oncogene bcl-3 encodes a transcriptional co-activator that activates through NF-kappa B p50 homodimers
    • Fujita T, Nolan GP, Liou HC, Scott ML, Baltimore D. The candidate proto-oncogene bcl-3 encodes a transcriptional co-activator that activates through NF-kappa B p50 homodimers. Genes Dev 1993;7:1354-1363.
    • (1993) Genes Dev , vol.7 , pp. 1354-1363
    • Fujita, T.1    Nolan, G.P.2    Liou, H.C.3    Scott, M.L.4    Baltimore, D.5
  • 21
    • 0031897632 scopus 로고    scopus 로고
    • NF-kappaB and Rel proteins: Evolutionarily conserved mediators of immune responses
    • Ghosh S, May MJ, Kopp EB. NF-kappaB and Rel proteins: evolutionarily conserved mediators of immune responses. Annu Rev Immunol 1998;16:225-260.
    • (1998) Annu Rev Immunol , vol.16 , pp. 225-260
    • Ghosh, S.1    May, M.J.2    Kopp, E.B.3
  • 23
    • 0041424822 scopus 로고    scopus 로고
    • Molecular mechanisms modulating muscle mass
    • Glass DJ. Molecular mechanisms modulating muscle mass. Trends Mol Med 2003;9:344-350.
    • (2003) Trends Mol Med , vol.9 , pp. 344-350
    • Glass, D.J.1
  • 25
    • 0037458739 scopus 로고    scopus 로고
    • Conditional expression of mutant M-line titins results in cardiomyopathy with altered sarcomere structure
    • Gotthardt M, Hammer RE, Hubner N, Monti J, Witt CC, McNabb M, et al. Conditional expression of mutant M-line titins results in cardiomyopathy with altered sarcomere structure. J Biol Chem 2003;278:6059-6065.
    • (2003) J Biol Chem , vol.278 , pp. 6059-6065
    • Gotthardt, M.1    Hammer, R.E.2    Hubner, N.3    Monti, J.4    Witt, C.C.5    McNabb, M.6
  • 26
    • 18844398202 scopus 로고    scopus 로고
    • Mechanically induced titin kinase activation studied by force-probe molecular dynamics simulations
    • Grater F, Shen J, Jiang H, Gautel M, Grubmuller H. Mechanically induced titin kinase activation studied by force-probe molecular dynamics simulations. Biophys J 2005;88:790-804.
    • (2005) Biophys J , vol.88 , pp. 790-804
    • Grater, F.1    Shen, J.2    Jiang, H.3    Gautel, M.4    Grubmuller, H.5
  • 27
    • 0034730251 scopus 로고    scopus 로고
    • NF-kappaB-induced loss of MyoD messenger RNA: Possible role in muscle decay and cachexia
    • Guttridge DC, Mayo MW, Madrid LV, Wang CY, Baldwin AS Jr. NF-kappaB-induced loss of MyoD messenger RNA: possible role in muscle decay and cachexia. Science 2000;289:2363-2366.
    • (2000) Science , vol.289 , pp. 2363-2366
    • Guttridge, D.C.1    Mayo, M.W.2    Madrid, L.V.3    Wang, C.Y.4    Baldwin Jr., A.S.5
  • 28
    • 0041530203 scopus 로고    scopus 로고
    • Atrophy responses to muscle inactivity. II. Molecular markers of protein deficits
    • Haddad F, Roy RR, Zhong H, Edgerton VR, Baldwin KM. Atrophy responses to muscle inactivity. II. Molecular markers of protein deficits. J Appl Physiol 2003;95:791-802.
    • (2003) J Appl Physiol , vol.95 , pp. 791-802
    • Haddad, F.1    Roy, R.R.2    Zhong, H.3    Edgerton, V.R.4    Baldwin, K.M.5
  • 29
    • 0026948255 scopus 로고
    • Regulation by insulin of muscle protein metabolism during sepsis and other catabolic conditions
    • Hasselgren PO, Fischer JE. Regulation by insulin of muscle protein metabolism during sepsis and other catabolic conditions. Nutrition 1992;8:434-439.
    • (1992) Nutrition , vol.8 , pp. 434-439
    • Hasselgren, P.O.1    Fischer, J.E.2
  • 30
    • 0035164533 scopus 로고    scopus 로고
    • Muscle cachexia: Current concepts of intracellular mechanisms and molecular regulation
    • Hasselgren PO, Fischer JE. Muscle cachexia: current concepts of intracellular mechanisms and molecular regulation. Ann Surg 2001;233:9-17.
    • (2001) Ann Surg , vol.233 , pp. 9-17
    • Hasselgren, P.O.1    Fischer, J.E.2
  • 31
    • 0033199348 scopus 로고    scopus 로고
    • NF-kappaB p105 is a target of IkappaB kinases and controls signal induction of Bcl-3-p50 complexes
    • Heissmeyer V, Krappmann D, Wulczyn FG, Scheidereit C. NF-kappaB p105 is a target of IkappaB kinases and controls signal induction of Bcl-3-p50 complexes. EMBO J 1999;18:4766-4778.
    • (1999) EMBO J , vol.18 , pp. 4766-4778
    • Heissmeyer, V.1    Krappmann, D.2    Wulczyn, F.G.3    Scheidereit, C.4
  • 32
    • 0034814951 scopus 로고    scopus 로고
    • Regulation of translation factors during hindlimb unloading and denervation of skeletal muscle in rats
    • Hornberger TA, Hunter RB, Kandarian SC, Esser KA. Regulation of translation factors during hindlimb unloading and denervation of skeletal muscle in rats. Am J Physiol Cell Physiol 2001;281:C179-C187.
    • (2001) Am J Physiol Cell Physiol , vol.281
    • Hornberger, T.A.1    Hunter, R.B.2    Kandarian, S.C.3    Esser, K.A.4
  • 33
    • 11144317940 scopus 로고    scopus 로고
    • Disruption of either the Nfkb1 or the Bcl3 gene inhibits skeletal muscle atrophy
    • Hunter RB, Kandarian SC. Disruption of either the Nfkb1 or the Bcl3 gene inhibits skeletal muscle atrophy. J Clin Invest 2004;114:1504-1511.
    • (2004) J Clin Invest , vol.114 , pp. 1504-1511
    • Hunter, R.B.1    Kandarian, S.C.2
  • 36
    • 0035350530 scopus 로고    scopus 로고
    • What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?
    • Jagoe RT, Goldberg AL. What do we really know about the ubiquitin-proteasome pathway in muscle atrophy? Curr Opin Clin Nutr Metab Care 2001;4:183-190.
    • (2001) Curr Opin Clin Nutr Metab Care , vol.4 , pp. 183-190
    • Jagoe, R.T.1    Goldberg, A.L.2
  • 37
    • 0037432191 scopus 로고    scopus 로고
    • A forkhead transcription factor FKHR upregulates lipoprotein lipase expression in skeletal muscle
    • Kamei Y, Mizukami J, Miura S, Suzuki M, Takahashi N, Kawada T, et al. A forkhead transcription factor FKHR upregulates lipoprotein lipase expression in skeletal muscle. FEBS Lett 2003;536:232-236.
    • (2003) FEBS Lett , vol.536 , pp. 232-236
    • Kamei, Y.1    Mizukami, J.2    Miura, S.3    Suzuki, M.4    Takahashi, N.5    Kawada, T.6
  • 38
    • 4544358547 scopus 로고    scopus 로고
    • Skeletal muscle FOXO1 (FKHR) transgenic mice have less skeletal muscle mass, down-regulated Type I (slow twitch/red muscle) fiber genes, and impaired glycemic control
    • Kamei Y, Miura S, Suzuki M, Kai Y, Mizukami J, Taniguchi T, et al. Skeletal muscle FOXO1 (FKHR) transgenic mice have less skeletal muscle mass, down-regulated Type I (slow twitch/red muscle) fiber genes, and impaired glycemic control. J Biol Chem 2004;279:41114-41123.
    • (2004) J Biol Chem , vol.279 , pp. 41114-41123
    • Kamei, Y.1    Miura, S.2    Suzuki, M.3    Kai, Y.4    Mizukami, J.5    Taniguchi, T.6
  • 39
    • 0035990341 scopus 로고    scopus 로고
    • Molecular events in skeletal muscle during disuse atrophy
    • Kandarian SC, Stevenson EJ. Molecular events in skeletal muscle during disuse atrophy. Exerc Sport Sci Rev 2002;30:111-116.
    • (2002) Exerc Sport Sci Rev , vol.30 , pp. 111-116
    • Kandarian, S.C.1    Stevenson, E.J.2
  • 40
    • 6544264325 scopus 로고    scopus 로고
    • Intratumoral injection of oligonucleotides to the NF-kappaB binding site inhibits cachexia in a mouse tumor model
    • Kawamura I, Morishita R, Tomita N, Lacey E, Aketa M, Tsujimoto S, et al. Intratumoral injection of oligonucleotides to the NF-kappaB binding site inhibits cachexia in a mouse tumor model. Gene Ther 1999;6:91-97.
    • (1999) Gene Ther , vol.6 , pp. 91-97
    • Kawamura, I.1    Morishita, R.2    Tomita, N.3    Lacey, E.4    Aketa, M.5    Tsujimoto, S.6
  • 41
    • 11144237310 scopus 로고    scopus 로고
    • Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I
    • Kedar V, McDonough H, Arya R, Li HH, Rockman HA, Patterson C. Muscle-specific RING finger 1 is a bona fide ubiquitin ligase that degrades cardiac troponin I. Proc Natl Acad Sci USA 2004;101:18135-18140.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 18135-18140
    • Kedar, V.1    McDonough, H.2    Arya, R.3    Li, H.H.4    Rockman, H.A.5    Patterson, C.6
  • 42
    • 0033045401 scopus 로고    scopus 로고
    • The physiological consequences of bed rest and inactivity
    • Krasnoff J, Painter P. The physiological consequences of bed rest and inactivity. Adv Ren Replace Ther 1999;6:124-132.
    • (1999) Adv Ren Replace Ther , vol.6 , pp. 124-132
    • Krasnoff, J.1    Painter, P.2
  • 43
    • 20644440418 scopus 로고    scopus 로고
    • The kinase domain of titin controls muscle gene expression and protein turnover
    • Lange S, Xiang F, Yakovenko A, Vihola A, Hackman P, Rostkova E, et al. The kinase domain of titin controls muscle gene expression and protein turnover. Science 2005;308:1599-1603.
    • (2005) Science , vol.308 , pp. 1599-1603
    • Lange, S.1    Xiang, F.2    Yakovenko, A.3    Vihola, A.4    Hackman, P.5    Rostkova, E.6
  • 44
    • 13244298415 scopus 로고    scopus 로고
    • Insulin-like growth factor-1 (IGF-1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway
    • Latres E, Amini AR, Amini AA, Griffiths J, Martin FJ, Wei Y, et al. Insulin-like growth factor-1 (IGF-1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway. J Biol Chem 2005;280:2737-2744.
    • (2005) J Biol Chem , vol.280 , pp. 2737-2744
    • Latres, E.1    Amini, A.R.2    Amini, A.A.3    Griffiths, J.4    Martin, F.J.5    Wei, Y.6
  • 45
    • 0032947267 scopus 로고    scopus 로고
    • Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states
    • Lecker SH, Solomon V, Mitch WE, Goldberg AL. Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states. J Nutr 1999;129(Suppl):227S-237S.
    • (1999) J Nutr , vol.129 , Issue.SUPPL.
    • Lecker, S.H.1    Solomon, V.2    Mitch, W.E.3    Goldberg, A.L.4
  • 46
    • 0032751546 scopus 로고    scopus 로고
    • Ubiquitin conjugation by the N-end rule pathway and mRNAs for its components increase in muscles of diabetic rats
    • Lecker SH, Solomon V, Price SR, Kwon YT, Mitch WE, Goldberg AL. Ubiquitin conjugation by the N-end rule pathway and mRNAs for its components increase in muscles of diabetic rats. J Clin Invest 1999;104:1411-1420.
    • (1999) J Clin Invest , vol.104 , pp. 1411-1420
    • Lecker, S.H.1    Solomon, V.2    Price, S.R.3    Kwon, Y.T.4    Mitch, W.E.5    Goldberg, A.L.6
  • 47
    • 0347285363 scopus 로고    scopus 로고
    • Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression
    • Lecker SH, Jagoe RT, Gilbert A, Gomes M, Baracos V, Bailey J, et al. Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression. FASEB J 2004;18:39-51.
    • (2004) FASEB J , vol.18 , pp. 39-51
    • Lecker, S.H.1    Jagoe, R.T.2    Gilbert, A.3    Gomes, M.4    Baracos, V.5    Bailey, J.6
  • 48
    • 2542496898 scopus 로고    scopus 로고
    • Regulation of muscle protein degradation: Coordinated control of apoptotic and ubiquitin-proteasome systems by phosphatidylinositol 3 kinase
    • Lee SW, Dai G, Hu Z, Wang X, Du J, Mitch WE. Regulation of muscle protein degradation: coordinated control of apoptotic and ubiquitin-proteasome systems by phosphatidylinositol 3 kinase. J Am Soc Nephrol 2004;15:1537-1545.
    • (2004) J Am Soc Nephrol , vol.15 , pp. 1537-1545
    • Lee, S.W.1    Dai, G.2    Hu, Z.3    Wang, X.4    Du, J.5    Mitch, W.E.6
  • 50
    • 0348134742 scopus 로고    scopus 로고
    • Mono-versus polyubiquitination: Differential control of p53 fate by Mdm2
    • Li M, Brooks CL, Wu-Baer F, Chen D, Baer R, Gu W. Mono-versus polyubiquitination: differential control of p53 fate by Mdm2. Science 2003;302:1972-1975.
    • (2003) Science , vol.302 , pp. 1972-1975
    • Li, M.1    Brooks, C.L.2    Wu-Baer, F.3    Chen, D.4    Baer, R.5    Gu, W.6
  • 51
    • 0141791457 scopus 로고    scopus 로고
    • Hydrogen peroxide stimulates ubiquitin-conjugating activity and expression of genes for specific E2 and E3 proteins in skeletal muscle myotubes
    • Li YP, Chen Y, Li AS, Reid MB. Hydrogen peroxide stimulates ubiquitin-conjugating activity and expression of genes for specific E2 and E3 proteins in skeletal muscle myotubes. Am J Physiol Cell Physiol 2003;285:C806-C812.
    • (2003) Am J Physiol Cell Physiol , vol.285
    • Li, Y.P.1    Chen, Y.2    Li, A.S.3    Reid, M.B.4
  • 52
    • 14644400387 scopus 로고    scopus 로고
    • TNF-alpha acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle
    • Li YP, Chen Y, John J, Moylan J, Jin B, Mann DL, et al. TNF-alpha acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle. FASEB J 2005;19:362-370.
    • (2005) FASEB J , vol.19 , pp. 362-370
    • Li, Y.P.1    Chen, Y.2    John, J.3    Moylan, J.4    Jin, B.5    Mann, D.L.6
  • 53
    • 0037449755 scopus 로고    scopus 로고
    • Determinants of nuclear and cytoplasmic ubiquitin-mediated degradation of MyoD
    • Lingbeck JM, Trausch-Azar JS, Ciechanover A, Schwartz AL. Determinants of nuclear and cytoplasmic ubiquitin-mediated degradation of MyoD. J Biol Chem 2003;278:1817-1823.
    • (2003) J Biol Chem , vol.278 , pp. 1817-1823
    • Lingbeck, J.M.1    Trausch-Azar, J.S.2    Ciechanover, A.3    Schwartz, A.L.4
  • 54
    • 0017170909 scopus 로고
    • Skeletal muscle metabolism in patients with malignant tumor
    • Lundholm K, Bylund AC, Holm J, Schersten T. Skeletal muscle metabolism in patients with malignant tumor. Eur J Cancer 1976;12:465-473.
    • (1976) Eur J Cancer , vol.12 , pp. 465-473
    • Lundholm, K.1    Bylund, A.C.2    Holm, J.3    Schersten, T.4
  • 55
    • 0031922009 scopus 로고    scopus 로고
    • Maintenance of myonuclear domain size in rat soleus after overload and growth hormone/IGF-1 treatment
    • McCall GE, Allen DL, Linderman JK, Grindeland RE, Roy RR, Mukku VR, et al. Maintenance of myonuclear domain size in rat soleus after overload and growth hormone/IGF-1 treatment. J Appl Physiol 1998;84:1407-1412.
    • (1998) J Appl Physiol , vol.84 , pp. 1407-1412
    • McCall, G.E.1    Allen, D.L.2    Linderman, J.K.3    Grindeland, R.E.4    Roy, R.R.5    Mukku, V.R.6
  • 56
    • 0036544533 scopus 로고    scopus 로고
    • Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1
    • McElhinny AS, Kakinuma K, Sorimachi H, Labeit S, Gregorio CC. Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1. J Cell Biol 2002;157:125-136.
    • (2002) J Cell Biol , vol.157 , pp. 125-136
    • McElhinny, A.S.1    Kakinuma, K.2    Sorimachi, H.3    Labeit, S.4    Gregorio, C.C.5
  • 57
    • 11144324372 scopus 로고    scopus 로고
    • Molecular mechanisms of muscle atrophy
    • McKinnell IW, Rudnicki MA. Molecular mechanisms of muscle atrophy. Cell 2004;119:907-910.
    • (2004) Cell , vol.119 , pp. 907-910
    • McKinnell, I.W.1    Rudnicki, M.A.2
  • 58
    • 0030593939 scopus 로고    scopus 로고
    • Mechanisms of muscle wasting. The role of the ubiquitin-proteasome pathway
    • Mitch WE, Goldberg AL. Mechanisms of muscle wasting. The role of the ubiquitin-proteasome pathway. N Engl J Med 1996;335:1897-1905.
    • (1996) N Engl J Med , vol.335 , pp. 1897-1905
    • Mitch, W.E.1    Goldberg, A.L.2
  • 59
    • 0035835974 scopus 로고    scopus 로고
    • Transcription factors and muscle cachexia: Is there a therapeutic target?
    • Mitch WE, Price SR. Transcription factors and muscle cachexia: is there a therapeutic target? Lancet 2001;357:734-735.
    • (2001) Lancet , vol.357 , pp. 734-735
    • Mitch, W.E.1    Price, S.R.2
  • 60
    • 0346041564 scopus 로고    scopus 로고
    • Transcriptional profiling identifies extensive downregulation of extracellular matrix gene expression in sarcopenic rat soleus muscle
    • Pattison JS, Folk LC, Madsen RW, Childs TE, Booth FW. Transcriptional profiling identifies extensive downregulation of extracellular matrix gene expression in sarcopenic rat soleus muscle. Physiol Genomics 2003;15:34-43.
    • (2003) Physiol Genomics , vol.15 , pp. 34-43
    • Pattison, J.S.1    Folk, L.C.2    Madsen, R.W.3    Childs, T.E.4    Booth, F.W.5
  • 61
    • 0348133552 scopus 로고    scopus 로고
    • Expression profiling identifies dysregulation of myosin heavy chains IIb and IIx during limb immobilization in the soleus muscles of old rats
    • Pattison JS, Folk LC, Madsen RW, Childs TE, Spangenburg EE, Booth FW. Expression profiling identifies dysregulation of myosin heavy chains IIb and IIx during limb immobilization in the soleus muscles of old rats. J Physiol (Lond) 2003;553:357-368.
    • (2003) J Physiol (Lond) , vol.553 , pp. 357-368
    • Pattison, J.S.1    Folk, L.C.2    Madsen, R.W.3    Childs, T.E.4    Spangenburg, E.E.5    Booth, F.W.6
  • 62
    • 0038624395 scopus 로고    scopus 로고
    • Dwarfism, impaired skin development, skeletal muscle atrophy, delayed bone development, and impeded adipogenesis in mice lacking Akt1 and Akt2
    • Peng XD, Xu PZ, Chen ML, Hahn-Windgassen A, Skeen J, Jacobs J, et al. Dwarfism, impaired skin development, skeletal muscle atrophy, delayed bone development, and impeded adipogenesis in mice lacking Akt1 and Akt2. Genes Dev 2003;17:1352-1365.
    • (2003) Genes Dev , vol.17 , pp. 1352-1365
    • Peng, X.D.1    Xu, P.Z.2    Chen, M.L.3    Hahn-Windgassen, A.4    Skeen, J.5    Jacobs, J.6
  • 63
    • 12244291970 scopus 로고    scopus 로고
    • Transient association of titin and myosin with microtubules in nascent myofibrils directed by the MURF2 RING-finger protein
    • Pizon V, Iakovenko A, Van Der Ven PF, Kelly R, Fatu C, Furst DO, et al. Transient association of titin and myosin with microtubules in nascent myofibrils directed by the MURF2 RING-finger protein. J Cell Sci 2002;115:4469-4482.
    • (2002) J Cell Sci , vol.115 , pp. 4469-4482
    • Pizon, V.1    Iakovenko, A.2    Van Der Ven, P.F.3    Kelly, R.4    Fatu, C.5    Furst, D.O.6
  • 65
    • 0035722694 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha and muscle wasting: A cellular perspective
    • Reid MB, Li YP. Tumor necrosis factor-alpha and muscle wasting: a cellular perspective. Respir Res 2001;2:269-272.
    • (2001) Respir Res , vol.2 , pp. 269-272
    • Reid, M.B.1    Li, Y.P.2
  • 66
    • 0037123438 scopus 로고    scopus 로고
    • Control of Ser2448 phosphorylation in the mammalian target of rapamycin by insulin and skeletal muscle load
    • Reynolds TH, Bodine SC, Lawrence JC Jr. Control of Ser2448 phosphorylation in the mammalian target of rapamycin by insulin and skeletal muscle load. J Biol Chem 2002;277:17657-17662.
    • (2002) J Biol Chem , vol.277 , pp. 17657-17662
    • Reynolds, T.H.1    Bodine, S.C.2    Lawrence Jr., J.C.3
  • 67
    • 0035735902 scopus 로고    scopus 로고
    • Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways
    • Rommel C, Bodine SC, Clarke BA, Rossman R, Nunez L, Stitt TN, et al. Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways. Nat Cell Biol 2001;3:1009-1013.
    • (2001) Nat Cell Biol , vol.3 , pp. 1009-1013
    • Rommel, C.1    Bodine, S.C.2    Clarke, B.A.3    Rossman, R.4    Nunez, L.5    Stitt, T.N.6
  • 68
    • 4544293878 scopus 로고    scopus 로고
    • IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1
    • Sacheck JM, Ohtsuka A, McLary SC, Goldberg AL. IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1. Am J Physiol Endocrinol Metab 2004;287:E591-E601.
    • (2004) Am J Physiol Endocrinol Metab , vol.287
    • Sacheck, J.M.1    Ohtsuka, A.2    McLary, S.C.3    Goldberg, A.L.4
  • 69
    • 11144356337 scopus 로고    scopus 로고
    • Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy
    • Sandri M, Sandri C, Gilbert A, Skurk C, Calabria E, Picard A, et al. Foxo transcription factors induce the atrophy-related ubiquitin ligase atrogin-1 and cause skeletal muscle atrophy. Cell 2004;117:399-412.
    • (2004) Cell , vol.117 , pp. 399-412
    • Sandri, M.1    Sandri, C.2    Gilbert, A.3    Skurk, C.4    Calabria, E.5    Picard, A.6
  • 70
    • 4043140199 scopus 로고    scopus 로고
    • Molecular and cellular determinants of skeletal muscle atrophy and hypertrophy
    • Sartorelli V, Fulco M. Molecular and cellular determinants of skeletal muscle atrophy and hypertrophy. Sci STKE 2004;2004:re11.
    • (2004) Sci STKE , vol.2004
    • Sartorelli, V.1    Fulco, M.2
  • 72
    • 19444369714 scopus 로고    scopus 로고
    • Mitochondria-associated apoptotic signalling in denervated rat skeletal muscle
    • Siu PM, Alway SE. Mitochondria-associated apoptotic signalling in denervated rat skeletal muscle. J Physiol (Lond) 2005;565:309-323.
    • (2005) J Physiol (Lond) , vol.565 , pp. 309-323
    • Siu, P.M.1    Alway, S.E.2
  • 73
    • 12144284036 scopus 로고    scopus 로고
    • Aging influences cellular and molecular responses of apoptosis to skeletal muscle unloading
    • Siu PM, Pistilli EE, Butler DC, Alway SE. Aging influences cellular and molecular responses of apoptosis to skeletal muscle unloading. Am J Physiol Cell Physiol 2005;288:C338-C349.
    • (2005) Am J Physiol Cell Physiol , vol.288
    • Siu, P.M.1    Pistilli, E.E.2    Butler, D.C.3    Alway, S.E.4
  • 74
    • 0029956781 scopus 로고    scopus 로고
    • Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts
    • Solomon V, Goldberg AL. Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts. J Biol Chem 1996;271:26690-26697.
    • (1996) J Biol Chem , vol.271 , pp. 26690-26697
    • Solomon, V.1    Goldberg, A.L.2
  • 75
    • 0032566716 scopus 로고    scopus 로고
    • The N-end rule pathway catalyzes a major fraction of the protein degradation in skeletal muscle
    • Solomon V, Lecker SH, Goldberg AL. The N-end rule pathway catalyzes a major fraction of the protein degradation in skeletal muscle. J Biol Chem 1998;273:25216-25222.
    • (1998) J Biol Chem , vol.273 , pp. 25216-25222
    • Solomon, V.1    Lecker, S.H.2    Goldberg, A.L.3
  • 76
    • 0032514735 scopus 로고    scopus 로고
    • Rates of ubiquitin conjugation increase when muscles atrophy, largely through activation of the N-end rule pathway
    • Solomon V, Baracos V, Sarraf P, Goldberg AL. Rates of ubiquitin conjugation increase when muscles atrophy, largely through activation of the N-end rule pathway. Proc Natl Acad Sci USA 1998;95:12602-12607.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12602-12607
    • Solomon, V.1    Baracos, V.2    Sarraf, P.3    Goldberg, A.L.4
  • 77
    • 14844336534 scopus 로고    scopus 로고
    • Muscle-specific expression of IGF-1 blocks angiotensin II-induced skeletal muscle wasting
    • Song YH, Li Y, Du J, Mitch WE, Rosenthal N, Delafontaine P. Muscle-specific expression of IGF-1 blocks angiotensin II-induced skeletal muscle wasting. J Clin Invest 2005;115:451-458.
    • (2005) J Clin Invest , vol.115 , pp. 451-458
    • Song, Y.H.1    Li, Y.2    Du, J.3    Mitch, W.E.4    Rosenthal, N.5    Delafontaine, P.6
  • 78
    • 0034698695 scopus 로고    scopus 로고
    • Regulation of microtubule dynamics and myogenic differentiation by MURF, a striated muscle RING-finger protein
    • Spencer JA, Eliazer S, Ilaria RL Jr, Richardson JA, Olson EN. Regulation of microtubule dynamics and myogenic differentiation by MURF, a striated muscle RING-finger protein. J Cell Biol 2000;150:771-784.
    • (2000) J Cell Biol , vol.150 , pp. 771-784
    • Spencer, J.A.1    Eliazer, S.2    Ilaria Jr., R.L.3    Richardson, J.A.4    Olson, E.N.5
  • 80
    • 0041353459 scopus 로고    scopus 로고
    • Global analysis of gene expression patterns during disuse atrophy in rat skeletal muscle
    • Stevenson EJ, Giresi PG, Koncarevic A, Kandarian SC. Global analysis of gene expression patterns during disuse atrophy in rat skeletal muscle. J Physiol (Lond) 2003;551:33-48.
    • (2003) J Physiol (Lond) , vol.551 , pp. 33-48
    • Stevenson, E.J.1    Giresi, P.G.2    Koncarevic, A.3    Kandarian, S.C.4
  • 81
    • 2042425906 scopus 로고    scopus 로고
    • The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors
    • Stitt TN, Drujan D, Clarke BA, Panaro F, Timofeyva Y, Kline WO, et al. The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. Mol Cell 2004;14:395-403.
    • (2004) Mol Cell , vol.14 , pp. 395-403
    • Stitt, T.N.1    Drujan, D.2    Clarke, B.A.3    Panaro, F.4    Timofeyva, Y.5    Kline, W.O.6
  • 82
    • 1842339868 scopus 로고    scopus 로고
    • Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles
    • Tawa NE Jr, Odessey R, Goldberg AL. Inhibitors of the proteasome reduce the accelerated proteolysis in atrophying rat skeletal muscles. J Clin Invest 1997;100:197-203.
    • (1997) J Clin Invest , vol.100 , pp. 197-203
    • Tawa Jr., N.E.1    Odessey, R.2    Goldberg, A.L.3
  • 83
    • 4744354410 scopus 로고    scopus 로고
    • Akt phosphorylation and NFkappaB activation are counter-regulated under conditions of oxidative stress
    • Taylor JM, Crack PJ, Gould JA, Ali U, Hertzog PJ, Iannello RC. Akt phosphorylation and NFkappaB activation are counter-regulated under conditions of oxidative stress. Exp Cell Res 2004;300:463-475.
    • (2004) Exp Cell Res , vol.300 , pp. 463-475
    • Taylor, J.M.1    Crack, P.J.2    Gould, J.A.3    Ali, U.4    Hertzog, P.J.5    Iannello, R.C.6
  • 84
    • 0025019455 scopus 로고
    • Atrophy of the soleus muscle by hindlimb unweighting
    • Thomason DB, Booth FW. Atrophy of the soleus muscle by hindlimb unweighting. J Appl Physiol 1990;68:1-12.
    • (1990) J Appl Physiol , vol.68 , pp. 1-12
    • Thomason, D.B.1    Booth, F.W.2
  • 85
    • 0024457063 scopus 로고
    • Protein metabolism and beta-myosin heavy-chain mRNA in unweighted soleus muscle
    • Thomason DB, Biggs RB, Booth FW. Protein metabolism and beta-myosin heavy-chain mRNA in unweighted soleus muscle. Am J Physiol 1989;257:R300-R305.
    • (1989) Am J Physiol , vol.257
    • Thomason, D.B.1    Biggs, R.B.2    Booth, F.W.3
  • 87
    • 0031020503 scopus 로고    scopus 로고
    • Cancer cachexia: Metabolic alterations and clinical manifestations
    • Tisdale MJ. Cancer cachexia: metabolic alterations and clinical manifestations. Nutrition 1997;13:1-7.
    • (1997) Nutrition , vol.13 , pp. 1-7
    • Tisdale, M.J.1
  • 89
  • 90
    • 0030988261 scopus 로고    scopus 로고
    • Regulation of NFkB1 proteins by the candidate oncoprotein Bcl-3: Generation of NF-kappaB homodimers from the cytoplasmic pool of p50-p105 and nuclear translocation
    • Watanabe N, Iwamura T, Shinoda T, Fujita T. Regulation of NFkB1 proteins by the candidate oncoprotein Bcl-3: generation of NF-kappaB homodimers from the cytoplasmic pool of p50-p105 and nuclear translocation. EMBOJ 1997;16:3609-3620.
    • (1997) EMBOJ , vol.16 , pp. 3609-3620
    • Watanabe, N.1    Iwamura, T.2    Shinoda, T.3    Fujita, T.4
  • 92
    • 0141887308 scopus 로고    scopus 로고
    • Increased expression of the ubiquitin-proteasome pathway in murine myotubes by proteolysis-inducing factor (PIF) is associated with activation of the transcription factor NF-kappaB
    • Whitehouse AS, Tisdale MJ. Increased expression of the ubiquitin-proteasome pathway in murine myotubes by proteolysis-inducing factor (PIF) is associated with activation of the transcription factor NF-kappaB. Br J Cancer 2003;89:1116-1122.
    • (2003) Br J Cancer , vol.89 , pp. 1116-1122
    • Whitehouse, A.S.1    Tisdale, M.J.2
  • 93
    • 14944352786 scopus 로고    scopus 로고
    • NF-kappaB mediates proteolysis-inducing factor induced protein degradation and expression of the ubiquitin-proteasome system in skeletal muscle
    • Wyke SM, Tisdale MJ. NF-kappaB mediates proteolysis-inducing factor induced protein degradation and expression of the ubiquitin-proteasome system in skeletal muscle. Br J Cancer 2005;92:711-721.
    • (2005) Br J Cancer , vol.92 , pp. 711-721
    • Wyke, S.M.1    Tisdale, M.J.2
  • 94
    • 0442307969 scopus 로고    scopus 로고
    • IkappaB kinases: Key regulators of the NF-kappaB pathway
    • Yamamoto Y, Gaynor RB. IkappaB kinases: key regulators of the NF-kappaB pathway. Trends Biochem Sci 2004;29:72-79.
    • (2004) Trends Biochem Sci , vol.29 , pp. 72-79
    • Yamamoto, Y.1    Gaynor, R.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.