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Volumn 37, Issue SUPPL. 10, 2009, Pages

Physical inactivity and muscle weakness in the critically ill

Author keywords

Atrophy; Bed rest; Cachexia; Catabolism; Critical illness myopathy; Frailty; Microgravity; Rehabilitation; Skeletal muscle; Strength

Indexed keywords

ATROGIN 1; CALPAIN; CATHEPSIN B; CATHEPSIN D; CATHEPSIN H; CATHEPSIN L; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MAMMALIAN TARGET OF RAPAMYCIN; REACTIVE OXYGEN METABOLITE; SOMATOMEDIN C;

EID: 70350520677     PISSN: 00903493     EISSN: 15300293     Source Type: Journal    
DOI: 10.1097/CCM.0b013e3181b6e974     Document Type: Conference Paper
Times cited : (98)

References (108)
  • 1
    • 0344845330 scopus 로고    scopus 로고
    • Skeletal muscle unweighting: Spaceflight and ground-based models
    • Adams GR, Caiozzo VJ, Baldwin KM: Skeletal muscle unweighting: Spaceflight and ground-based models. J Appl Physiol 2003; 95:2185-2201
    • (2003) J Appl Physiol , vol.95 , pp. 2185-2201
    • Adams, G.R.1    Caiozzo, V.J.2    Baldwin, K.M.3
  • 2
    • 0036092597 scopus 로고    scopus 로고
    • Hindlimb unloading rodent model: Technical aspects
    • Morey-Holton ER, Globus RK: Hindlimb unloading rodent model: Technical aspects. J Appl Physiol 2002; 92:1367-1377
    • (2002) J Appl Physiol , vol.92 , pp. 1367-1377
    • Morey-Holton, E.R.1    Globus, R.K.2
  • 3
    • 0021691051 scopus 로고
    • Atrophy and growth failure of rat hindlimb muscles in tail-cast suspension
    • Jaspers SR, Tischler ME: Atrophy and growth failure of rat hindlimb muscles in tail-cast suspension. J. Appl Physiol 1984; 57:1472-1479
    • (1984) J. Appl Physiol , vol.57 , pp. 1472-1479
    • Jaspers, S.R.1    Tischler, M.E.2
  • 4
    • 0018508958 scopus 로고
    • Recovery of skeletal muscle after 3 mo of hindlimb immobilization in rats
    • 4. Booth FW, Seider MJ: Recovery of skeletal muscle after 3 mo of hindlimb immobilization in rats. J Appl Physiol 1979; 47: 435-439 (Pubitemid 10109507)
    • (1979) European Journal of Pharmacology , vol.58 , Issue.4 , pp. 435-439
    • Booth, F.W.1    Seider, M.J.2
  • 5
    • 0017224854 scopus 로고
    • The effects of denervation on protein turnover of rat skeletal muscle
    • Goldspink DF: The effects of denervation on protein turnover of rat skeletal muscle. Biochem J 1976; 156:71-80
    • (1976) Biochem J , vol.156 , pp. 71-80
    • Goldspink, D.F.1
  • 7
    • 33749478450 scopus 로고    scopus 로고
    • Determinants of disuse-induced skeletal muscle atrophy: Exercise and nutrition countermeasures to prevent protein loss
    • 7. Bajotto G, Shimomura Y: Determinants of disuse-induced skeletal muscle atrophy: Exercise and nutrition countermeasures to prevent protein loss. J Nutr Sci Vitaminol (Tokyo) 2006; 52:233-247 (Pubitemid 44520051)
    • (2006) Journal of Nutritional Science and Vitaminology , vol.52 , Issue.4 , pp. 233-247
    • Bajotto, G.1    Shimomura, Y.2
  • 8
    • 34447509808 scopus 로고    scopus 로고
    • Oxidative stress and disuse muscle atrophy
    • DOI 10.1152/japplphysiol.01202.2006
    • 8. Powers SK, Kavazis AN, McClung JM: Oxidative stress and disuse muscle atrophy. J Appl Physiol 2007; 102:2389-2397 (Pubitemid 47080773)
    • (2007) Journal of Applied Physiology , vol.102 , Issue.6 , pp. 2389-2397
    • Powers, S.K.1    Kavazis, A.N.2    McClung, J.M.3
  • 9
    • 1642527377 scopus 로고    scopus 로고
    • Muscle wasting and energy balance in critical illness
    • Reid CL, Campbell IT, Little RA: Muscle wasting and energy balance in critical illness. Clin Nutr 2004; 23:273-280
    • (2004) Clin Nutr , vol.23 , pp. 273-280
    • Reid, C.L.1    Campbell, I.T.2    Little, R.A.3
  • 10
    • 0032442182 scopus 로고    scopus 로고
    • Muscle fibre atrophy in critically ill patients is associated with the loss of myosin filaments and the presence of lysosomal enzymes and ubiquitin
    • DOI 10.1046/j.1365-2990.1998.00144.x
    • 10. Helliwell TR, Wilkinson A, Griffiths RD, et al: Muscle fibre atrophy in critically ill patients is associated with the loss of myosin filaments and the presence of lysosomal enzymes and ubiquitin. Neuropathol Appl Neurobiol 1998; 24:507-517 (Pubitemid 29002282)
    • (1998) Neuropathology and Applied Neurobiology , vol.24 , Issue.6 , pp. 507-517
    • Helliwell, T.R.1    Wilkinson, A.2    Griffiths, R.D.3    McClelland, P.4    Palmer, T.E.A.5    Bone, J.M.6
  • 12
    • 3042755596 scopus 로고    scopus 로고
    • Allopurinol mitigates muscle contractile dysfunction caused by hindlimb unloading in mice
    • 12. Matuszczak Y, Arbogast S, Reid MB: Allopurinol mitigates muscle contractile dysfunction caused by hindlimb unloading in mice. Aviat Space Environ Med 2004; 75: 581-588 (Pubitemid 38857377)
    • (2004) Aviation Space and Environmental Medicine , vol.75 , Issue.7 SEC. 2 , pp. 581-588
    • Matuszczak, Y.1    Arbogast, S.2    Reid, M.B.3
  • 14
    • 0025727193 scopus 로고
    • Effects of lower limb unloading on skeletal muscle mass and function in humans
    • Berg HE, Dudley GA, Haggmark T, et al: Effects of lower limb unloading on skeletal muscle mass and function in humans. J Appl Physiol 1991; 70:1882-1885
    • (1991) J Appl Physiol , vol.70 , pp. 1882-1885
    • Berg, H.E.1    Dudley, G.A.2    Haggmark, T.3
  • 15
    • 0033974488 scopus 로고    scopus 로고
    • Decreased thin filament density and length in human atrophic soleus muscle fibers after spaceflight
    • Riley DA, Bain JL, Thompson JL, et al: Decreased thin filament density and length in human atrophic soleus muscle fibers after spaceflight. J Appl Physiol 2000; 88: 567-572
    • (2000) J Appl Physiol , vol.88 , pp. 567-572
    • Riley, D.A.1    Bain, J.L.2    Thompson, J.L.3
  • 16
    • 27944484046 scopus 로고    scopus 로고
    • Differential activation of stress-responsive signalling proteins associated with altered loading in a rat skeletal muscle
    • DOI 10.1002/jcb.20616
    • 16. Choi I, Lee K, Kim M, et al: Differential activation of stress-responsive signalling proteins associated with altered loading in a rat skeletal muscle. J Cell Biochem 2005; 96:1231-1243 (Pubitemid 41681865)
    • (2005) Journal of Cellular Biochemistry , vol.96 , Issue.6 , pp. 1231-1243
    • Choi, I.1    Lee, K.2    Kim, M.3    Lee, M.4    Park, K.5
  • 17
    • 0036778207 scopus 로고    scopus 로고
    • Critical illness myopathy
    • Lacomis D: Critical illness myopathy. Curr Rheumatol Rep 2002; 4:403-408
    • (2002) Curr Rheumatol Rep , vol.4 , pp. 403-408
    • Lacomis, D.1
  • 18
    • 0141788373 scopus 로고    scopus 로고
    • Electrophoretic determination of the myosin/actin ratio in the diagnosis of critical illness myopathy
    • DOI 10.1007/s00134-003-1894-9
    • 18. Stibler H, Edstrom L, Ahlbeck K, et al: Electrophoretic determination of the myosin/actin ratio in the diagnosis of critical illness myopathy. Intensive Care Med 2003; 9:1515-1527 (Pubitemid 37153596)
    • (2003) Intensive Care Medicine , vol.29 , Issue.9 , pp. 1515-1527
    • Stibler, H.1    Edstrom, L.2    Ahlbeck, K.3    Remahl, S.4    Ansved, T.5
  • 19
    • 0024457063 scopus 로고
    • Protein metabolism and beta-myosin heavychain mRNA in unweighted soleus muscle
    • Thomason DB, Biggs RB, Booth FW: Protein metabolism and beta-myosin heavychain mRNA in unweighted soleus muscle. Am J Physiol 1989; 257:R300-305
    • (1989) Am J Physiol , vol.257
    • Thomason, D.B.1    Biggs, R.B.2    Booth, F.W.3
  • 20
    • 0037123438 scopus 로고    scopus 로고
    • Control of Ser2448 phosphorylation in the mammalian target of rapamycin by insulin and skeletal muscle load
    • Reynolds THt, 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
    • Tht, R.1    Bodine, S.C.2    Lawrence Jr., J.C.3
  • 21
    • 4043171462 scopus 로고    scopus 로고
    • Upstream and downstream of mTOR
    • Hay N, Sonenberg N: Upstream and downstream of mTOR. Genes Dev 2004; 18: 1926-1945
    • (2004) Genes Dev , vol.18 , pp. 1926-1945
    • Hay, N.1    Sonenberg, N.2
  • 24
    • 0032693586 scopus 로고    scopus 로고
    • Regulation of IGF-I, IGFBP-4 and IGFBP-5 gene expression by loading in mouse skeletal muscle
    • DOI 10.1016/S0014-5793(99)01469-6, PII S0014579399014696
    • 24. Awede B, Thissen J, Gailly P, et al: Regulation of IGF-I, IGFBP-4 and IGFBP-5 gene expression by loading in mouse skeletal muscle. FEBS Lett 1999; 461:263-267 (Pubitemid 29533344)
    • (1999) FEBS Letters , vol.461 , Issue.3 , pp. 263-267
    • Awede, B.1    Thissen, J.-P.2    Gailly, P.3    Lebacq, J.4
  • 25
    • 39049169099 scopus 로고    scopus 로고
    • Rat hindlimb unloading down-regulates insulin like growth factor-1 signaling and AMP-activated protein kinase, and leads to severe atrophy of the soleus muscle
    • Han B, Zhu MJ, Ma C, et al: Rat hindlimb unloading down-regulates insulin like growth factor-1 signaling and AMP-activated protein kinase, and leads to severe atrophy of the soleus muscle. Appl Physiol Nutr Metab 2007; 32:1115-1123
    • (2007) Appl Physiol Nutr Metab , vol.32 , pp. 1115-1123
    • Han, B.1    Zhu, M.J.2    Ma, C.3
  • 26
    • 0035861644 scopus 로고    scopus 로고
    • 5′-AMP-activated Protein Kinase Phosphorylates IRS-1 on Ser-789 in Mouse C2C12 Myotubes in Response to 5-Aminoimidazole-4-carboxamide Riboside
    • DOI 10.1074/jbc.C100483200
    • 26. Jakobsen SN, Hardie DG, Morrice N, et al: 5′-AMP-activated protein kinase phosphorylates IRS-1 on Ser-789 in mouse C2C12 myotubes in response to 5-aminoimidazole4-carboxamide riboside. J Biol Chem 2001; 276:46912-46916 (Pubitemid 37373061)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.50 , pp. 46912-46916
    • Jakobsen, S.N.1    Hardie, D.G.2    Morrice, N.3    Tornqvist, H.E.4
  • 29
    • 0023928154 scopus 로고
    • Activation of a calmodulin-dependent phosphatase by a Ca2+-dependent protease
    • Tallant EA, Brumley LM, Wallace RW: Activation of a calmodulin-dependent phosphatase by a Ca2+-dependent protease. Biochemistry 1988; 27:2205-2211
    • (1988) Biochemistry , vol.27 , pp. 2205-2211
    • Tallant, E.A.1    Brumley, L.M.2    Wallace, R.W.3
  • 30
    • 0029956781 scopus 로고    scopus 로고
    • Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts
    • DOI 10.1074/jbc.271.43.26690
    • 30. 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 (Pubitemid 26359075)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.43 , pp. 26690-26697
    • Solomon, V.1    Goldberg, A.L.2
  • 32
    • 55649083093 scopus 로고    scopus 로고
    • Calpain mediates cardiac troponin degradation and contractile dysfunction in atrial fibrillation
    • Ke L, Qi XY, Dijkhuis AJ, et al: Calpain mediates cardiac troponin degradation and contractile dysfunction in atrial fibrillation. J Mol Cell Cardiol 2008; 45:685-693
    • (2008) J Mol Cell Cardiol , vol.45 , pp. 685-693
    • Ke, L.1    Qi, X.Y.2    Dijkhuis, A.J.3
  • 34
    • 34248677314 scopus 로고    scopus 로고
    • Calpain/calpastatin activities and substrate depletion patterns during hindlimb unweighting and reweighting in skeletal muscle
    • DOI 10.1007/s00421-007-0445-4
    • 34. Enns DL, Raastad T, Ugelstad I, et al: Calpain/calpastatin activities and substrate depletion patterns during hindlimb unweighting and reweighting in skeletal muscle. Eur J Appl Physiol 2007; 100:445-455 (Pubitemid 46773994)
    • (2007) European Journal of Applied Physiology , vol.100 , Issue.4 , pp. 445-455
    • Enns, D.L.1    Raastad, T.2    Ugelstad, I.3    Belcastro, A.N.4
  • 35
    • 0035348487 scopus 로고    scopus 로고
    • Space shuttle flight (STS-90) enhances degradation of rat myosin heavy chain in association with activation of ubiquitin-proteasome pathway
    • Ikemoto M, Nikawa T, Takeda S, et al: Space shuttle flight (STS-90) enhances degradation of rat myosin heavy chain in association with activation of ubiquitin-proteasome pathway. FASEB J 2001; 15: 1279-1281
    • (2001) FASEB J , vol.15 , pp. 1279-1281
    • Ikemoto, M.1    Nikawa, T.2    Takeda, S.3
  • 36
    • 0037115363 scopus 로고    scopus 로고
    • Expression of a calpastatin transgene slows muscle wasting and obviates changes in myosin isoform expression during murine muscle disuse
    • Tidball JG, Spencer MJ: Expression of a calpastatin transgene slows muscle wasting and obviates changes in myosin isoform expression during murine muscle disuse. J Physiol 2002; 545:819-828
    • (2002) J Physiol , vol.545 , pp. 819-828
    • Tidball, J.G.1    Spencer, M.J.2
  • 37
    • 33846807633 scopus 로고    scopus 로고
    • Prevention of unloading-induced atrophy by vitamin e supplementation: Links between oxidative stress and soleus muscle proteolysis?
    • DOI 10.1016/j.freeradbiomed.2006.12.001, PII S0891584906007714
    • 37. Servais S, Letexier D, Favier R, et al: Prevention of unloading-induced atrophy by vitamin E supplementation: Links between oxidative stress and soleus muscle proteolysis? Free Radic Biol Med 2007; 42:627-635 (Pubitemid 46210130)
    • (2007) Free Radical Biology and Medicine , vol.42 , Issue.5 , pp. 627-635
    • Servais, S.1    Letexier, D.2    Favier, R.3    Duchamp, C.4    Desplanches, D.5
  • 41
    • 2442701924 scopus 로고    scopus 로고
    • Skeletal muscle gene expression in spaceflown rats
    • Nikawa T, Ishidoh K, Hirasaka K, et al: Skeletal muscle gene expression in spaceflown rats. FASEB J 2004; 18:522-524
    • (2004) FASEB J , vol.18 , pp. 522-524
    • Nikawa, T.1    Ishidoh, K.2    Hirasaka, K.3
  • 42
    • 0035807969 scopus 로고    scopus 로고
    • Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
    • Gomes MD, Lecker SH, Jagoe RT, et al: Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proc Natl Acad Sci USA 2001; 98: 14440-14445
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14440-14445
    • Gomes, M.D.1    Lecker, S.H.2    Jagoe, R.T.3
  • 43
    • 6944226810 scopus 로고    scopus 로고
    • Disuse atrophy and exercise rehabilitation in humans profoundly affects the expression of genes associated with the regulation of skeletal muscle mass
    • Jones SW, Hill RJ, Krasney PA, et al: Disuse atrophy and exercise rehabilitation in humans profoundly affects the expression of genes associated with the regulation of skeletal muscle mass. FASEB J 2004; 18: 1025-1027
    • (2004) FASEB J , vol.18 , pp. 1025-1027
    • Jones, S.W.1    Hill, R.J.2    Krasney, P.A.3
  • 44
    • 63249134179 scopus 로고    scopus 로고
    • MAFbx/Atrogin-1 controls the activity of the initiation factor eIF3-f in skeletal muscle atrophy by targeting multiple C-terminal lysines
    • Epub 2008 Dec 10
    • Csibi A, Leibovitch MP, Cornille K, et al: MAFbx/Atrogin-1 controls the activity of the initiation factor eIF3-f in skeletal muscle atrophy by targeting multiple C-terminal lysines. J Biol Chem 2009; 284:4413-4421. Epub 2008 Dec 10
    • (2009) J Biol Chem , vol.284 , pp. 4413-4421
    • Csibi, A.1    Leibovitch, M.P.2    Cornille, K.3
  • 45
    • 56449095862 scopus 로고    scopus 로고
    • The involvement of the ubiquitin proteasome system in human skeletal muscle remodelling and atrophy
    • Murtón AJ, Constantin D, Greenhaff PL: The involvement of the ubiquitin proteasome system in human skeletal muscle remodelling and atrophy. Biochim Biophys Acta 2008; 1782:730-743
    • (2008) Biochim Biophys Acta , vol.1782 , pp. 730-743
    • Murtón, A.J.1    Constantin, D.2    Greenhaff, P.L.3
  • 47
    • 3042614035 scopus 로고    scopus 로고
    • Enhanced insulin action on glucose transport and insulin signaling in 7-day unweighted rat soleus muscle
    • O'Keefe MP, Perez FR, Sloniger JA, et al: Enhanced insulin action on glucose transport and insulin signaling in 7-day unweighted rat soleus muscle. J Appl Physiol 2004; 97:63-71
    • (2004) J Appl Physiol , vol.97 , pp. 63-71
    • O'Keefe, M.P.1    Perez, F.R.2    Sloniger, J.A.3
  • 50
    • 0347363477 scopus 로고    scopus 로고
    • Responsiveness of cell signaling pathways during the failed 15-day regrowth of aged skeletal muscle
    • Morris RT, Spangenburg EE, Booth FW: Responsiveness of cell signaling pathways during the failed 15-day regrowth of aged skeletal muscle. J Appl Physiol 2004; 96: 398-404
    • (2004) J Appl Physiol , vol.96 , pp. 398-404
    • Morris, R.T.1    Spangenburg, E.E.2    Booth, F.W.3
  • 52
    • 52549133171 scopus 로고    scopus 로고
    • Nuclear factorkappa B signaling in skeletal muscle atrophy
    • Li H, Malhotra S, Kumar A: Nuclear factorkappa B signaling in skeletal muscle atrophy. J Mol Med 2008; 86:1113-1126
    • (2008) J Mol Med , vol.86 , pp. 1113-1126
    • Li, H.1    Malhotra, S.2    Kumar, A.3
  • 53
    • 24944508641 scopus 로고    scopus 로고
    • Effects of dietary curcumin or N-acetylcysteine on NF-κB activity and contractile performance in ambulatory and unloaded murine soleus
    • DOI 10.1186/1743-7075-2-20
    • 53. Farid M, Reid MB, Li YP, et al: Effects of dietary curcumin or N-acetylcysteine on NF-kappaB activity and contractile performance in ambulatory and unloaded murine soleus. Nutr Metab (Lond) 2005; 2:20 (Pubitemid 41317459)
    • (2005) Nutrition and Metabolism , vol.2 , pp. 20
    • Farid, M.1    Reid, M.B.2    Li, Y.-P.3    Gerken, E.4    Durham, W.J.5
  • 54
    • 11144317940 scopus 로고    scopus 로고
    • Disruption of either the Nfkbl or the Bcl3 gene inhibits skeletal muscle atrophy
    • Hunter RB, Kandarian SC: Disruption of either the Nfkbl 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
  • 57
    • 9144264926 scopus 로고    scopus 로고
    • Induction of proteasome expression in skeletal muscle is attenuated by inhibitors of NF-kappaB activation
    • Wyke SM, Russell ST, Tisdale MJ: Induction of proteasome expression in skeletal muscle is attenuated by inhibitors of NF-kappaB activation. Br J Cancer 2004; 91:1742-1750
    • (2004) Br J Cancer , vol.91 , pp. 1742-1750
    • Wyke, S.M.1    Russell, S.T.2    Tisdale, M.J.3
  • 58
    • 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
    • 58. Li YP, Chen Y, Li AS, et al: 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 (Pubitemid 37158805)
    • (2003) American Journal of Physiology - Cell Physiology , vol.285 , Issue.4-54
    • Li, Y.-P.1    Chen, Y.2    Li, A.S.3    Reid, M.B.4
  • 59
    • 0037861856 scopus 로고    scopus 로고
    • Hindlimb unloading increases oxidative stress and disrupts antioxidant capacity in skeletal muscle
    • DOI 10.1016/S0891-5849(03)00186-2
    • 59. Lawler JM, Song W, Demaree SR: Hindlimb unloading increases oxidative stress and disrupts antioxidant capacity in skeletal muscle. Free Radic Biol Med 2003; 35:9-16 (Pubitemid 36782333)
    • (2003) Free Radical Biology and Medicine , vol.35 , Issue.1 , pp. 9-16
    • Lawler, J.M.1    Song, W.2    Demaree, S.R.3
  • 60
    • 57349109417 scopus 로고    scopus 로고
    • Agedependent increase in oxidative stress in gastrocnemius muscle with unloading
    • Siu PM, Pistilli EE, Alway SE: Agedependent increase in oxidative stress in gastrocnemius muscle with unloading. J Appl Physiol 2008; 105:1695-1705
    • (2008) J Appl Physiol , vol.105 , pp. 1695-1705
    • Siu, P.M.1    Pistilli, E.E.2    Alway, S.E.3
  • 61
    • 38849162112 scopus 로고    scopus 로고
    • Physiological, histological and biochemical properties of rat skeletal muscles in response to hindlimb suspension
    • DOI 10.1016/j.jelekin.2006.10.001, PII S1050641106001416
    • 61. Guillot C, Steinberg JG, Delliaux S, et al: Physiological, histological and biochemical properties of rat skeletal muscles in response to hindlimb suspension. J Electromyogr Kinesiol 2008; 18:276-283 (Pubitemid 351200046)
    • (2008) Journal of Electromyography and Kinesiology , vol.18 , Issue.2 , pp. 276-283
    • Guillot, C.1    Steinberg, J.G.2    Delliaux, S.3    Kipson, N.4    Jammes, Y.5    Badier, M.6
  • 62
    • 14644400387 scopus 로고    scopus 로고
    • TNF-α acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle
    • DOI 10.1096/fj.04-2364com
    • 62. Li YP, Chen Y, John J, et al: TNF-alpha acts via p38 MAPK to stimulate expression of the ubiquitin ligase atroginl/MAFbx in skeletal muscle. FASEB J 2005; 19:362-370 (Pubitemid 40316524)
    • (2005) FASEB Journal , vol.19 , Issue.3 , pp. 362-370
    • Li, Y.-P.1    Chen, Y.2    John, J.3    Moylan, J.4    Jin, B.5    Mann, D.L.6    Reid, M.B.7
  • 64
    • 0020688213 scopus 로고
    • Structures and functions of lysosomal thiol proteinases and their endogenous inhibitor
    • Katunuma N, Kominami E: Structures and functions of lysosomal thiol proteinases and their endogenous inhibitor. Curr Top Cell Regul 1983; 22:71-101
    • (1983) Curr Top Cell Regul , vol.22 , pp. 71-101
    • Katunuma, N.1    Kominami, E.2
  • 65
    • 0017709822 scopus 로고
    • Degradation of myofibrillar proteins by cathepsins B and D
    • Schwartz W, Bird JW: Degradation of myofibrillar proteins by cathepsins B and D. Biochem J 1977; 167:811-820
    • (1977) Biochem J , vol.167 , pp. 811-820
    • Schwartz, W.1    Bird, J.W.2
  • 66
    • 0019453703 scopus 로고
    • Susceptibilities of various myofibrillar proteins to cathepsin B and morphological alteration of isolated myofibrils by this enzyme
    • 66. Noda T, Isogai K, Hayashi H, et al: Susceptibilities of various myofibrillar proteins to cathepsin B and morphological alteration of isolated myofibrils by this enzyme. J Biochem 1981; 90:371-379 (Pubitemid 11012617)
    • (1981) Journal of Biochemistry , vol.90 , Issue.2 , pp. 371-379
    • Noda, T.1    Isogai, K.2    Hayashi, H.3    Katunuma, N.4
  • 67
    • 0019816949 scopus 로고
    • Mode of degradation of myofibrillar proteins by an endogenous protease, cathepsin L
    • 67. Matsukura U, Okitani A, Nishimuro T, et al: Mode of degradation of myofibrillar proteins by an endogenous protease, cathepsin L. Biochim Biophys Acta 1981; 662:41-47 (Pubitemid 12216171)
    • (1981) Biochimica et Biophysica Acta , vol.662 , Issue.1 , pp. 41-47
    • Matsukura, U.1    Okitani, A.2    Nishimuro, T.3    Kato, H.4
  • 69
    • 0036582760 scopus 로고    scopus 로고
    • Apoptotic signaling in skeletal muscle fibers during atrophy
    • DOI 10.1097/00075197-200205000-00003
    • 69. Sandri M: Apoptotic signaling in skeletal muscle fibers during atrophy. Curr Opin Clin Nutr Metab Care 2002; 5:249-253 (Pubitemid 40684669)
    • (2002) Current Opinion in Clinical Nutrition and Metabolic Care , vol.5 , Issue.3 , pp. 249-253
    • Sandri, M.1
  • 71
    • 50449101139 scopus 로고    scopus 로고
    • Evidences of apoptosis during the early phases of soleus muscle atrophy in hindlimb suspended mice
    • Ferreira R, Neuparth MJ, Vitorino R, et al: Evidences of apoptosis during the early phases of soleus muscle atrophy in hindlimb suspended mice. Physiol Res 2008; 57: 601-611
    • (2008) Physiol Res , vol.57 , pp. 601-611
    • Ferreira, R.1    Neuparth, M.J.2    Vitorino, R.3
  • 73
    • 0037047326 scopus 로고    scopus 로고
    • Calpain and mitochondria in ischemia/reperfusion injury
    • Chen M, Won DJ, Krajewski S, et al: Calpain and mitochondria in ischemia/reperfusion injury. J Biol Chem 2002; 277:29181-29186
    • (2002) J Biol Chem , vol.277 , pp. 29181-29186
    • Chen, M.1    Won, D.J.2    Krajewski, S.3
  • 74
    • 16644386074 scopus 로고    scopus 로고
    • Quantitative ultrastructural changes in satellite cells of rats immobilized after soleus muscle denervation
    • DOI 10.1016/j.yexmp.2004.08.007, PII S0014480004000851
    • 74. Kujawa M, Baran W, Jankowska-Steifer E: Quantitative ultrastructural changes in satellite cells of rats immobilized after soleus muscle denervation. Exp Mol Pathol 2005; 78:78-85 (Pubitemid 41373321)
    • (2005) Experimental and Molecular Pathology , vol.78 , Issue.1 , pp. 78-85
    • Kujawa, M.1    Baran, W.2    Jankowska-Steifer, E.3
  • 75
    • 25844516560 scopus 로고    scopus 로고
    • Apoptotic responses to hindlimb suspension in gastrocnemius muscles from young adult and aged rats
    • Siu PM, Pistilli EE, Alway SE: Apoptotic responses to hindlimb suspension in gastrocnemius muscles from young adult and aged rats. Am J Physiol Regul Integr Comp Physiol 2005; 289:R1015-R1026
    • (2005) Am J Physiol Regul Integr Comp Physiol , vol.289
    • Siu, P.M.1    Pistilli, E.E.2    Alway, S.E.3
  • 76
    • 33645969578 scopus 로고    scopus 로고
    • Redox modulation of contractile function in respiratory and limb skeletal muscle
    • Smith MA, Reid MB: Redox modulation of contractile function in respiratory and limb skeletal muscle. Respir Physiol Neurobiol 2006; 151:229-241
    • (2006) Respir Physiol Neurobiol , vol.151 , pp. 229-241
    • Smith, M.A.1    Reid, M.B.2
  • 77
    • 0035143723 scopus 로고    scopus 로고
    • Invited review: Redox modulation of skeletal muscle contraction: What we know and what we don't
    • Reid MB: Invited review: Redox modulation of skeletal muscle contraction: What we know and what we don't. J Appl Physiol 2001; 90:724-731
    • (2001) J Appl Physiol , vol.90 , pp. 724-731
    • Reid, M.B.1
  • 79
    • 0031660717 scopus 로고    scopus 로고
    • Nitric oxide synthase inhibition reduces muscle inflammation and necrosis in modified muscle use
    • Pizza FX, Hernandez IJ, Tidball JG: Nitric oxide synthase inhibition reduces muscle inflammation and necrosis in modified muscle use. J Leukoc Biol 1998; 64: 427-433
    • (1998) J Leukoc Biol , vol.64 , pp. 427-433
    • Pizza, F.X.1    Hernandez, I.J.2    Tidball, J.G.3
  • 82
    • 0034085363 scopus 로고    scopus 로고
    • RyRl modulation by oxidation and calmodulin
    • Hamilton SL, Reid MB: RyRl modulation by oxidation and calmodulin. Antioxid Redox Signal 2000; 2:41-45
    • (2000) Antioxid Redox Signal , vol.2 , pp. 41-45
    • Hamilton, S.L.1    Reid, M.B.2
  • 83
    • 0030719457 scopus 로고    scopus 로고
    • In vivo aging of rat skeletal muscle sarcoplasmic reticulum Ca-ATPase. Chemical analysis and quantitative simulation by exposure to low levels of peroxyl radicals
    • Viner RI, Ferrington DA, Aced GI, et al: In vivo aging of rat skeletal muscle sarcoplasmic reticulum Ca-ATPase. Chemical analysis and quantitative simulation by exposure to low levels of peroxyl radicals. Biochim Biophys Acta 1997; 1329:321-335
    • (1997) Biochim Biophys Acta , vol.1329 , pp. 321-335
    • Viner, R.I.1    Ferrington, D.A.2    Aced, G.I.3
  • 84
    • 0042232778 scopus 로고    scopus 로고
    • High sensitivity of plasma membrane ion transport ATPases from human neutrophils towards 4-hydroxy-2,3-trans-nonenal
    • DOI 10.1016/S0024-3205(03)00661-1
    • 84. Siems W, Capuozzo E, Lucano A, et al: High sensitivity of plasma membrane ion transport ATPases from human neutrophils towards 4-hydroxy-2,3-trans-nonenal. Life Sci 2003; 73:2583-2590 (Pubitemid 37098298)
    • (2003) Life Sciences , vol.73 , Issue.20 , pp. 2583-2590
    • Siems, W.1    Capuozzo, E.2    Lucano, A.3    Salerno, C.4    Crifo, C.5
  • 85
    • 14044277556 scopus 로고    scopus 로고
    • Redox regulation of NF-κB activation: Distinct redox regulation between the cytoplasm and the nucleus
    • DOI 10.1089/ars.2005.7.395
    • 85. Kabe Y, Ando K, Hirao S, et al: Redox regulation of NF-kappaB activation: distinct redox regulation between the cytoplasm and the nucleus. Antioxid Redox Signal 2005; 7:395-403 (Pubitemid 40279807)
    • (2005) Antioxidants and Redox Signaling , vol.7 , Issue.3-4 , pp. 395-403
    • Kabe, Y.1    Ando, K.2    Hirao, S.3    Yoshida, M.4    Handa, H.5
  • 86
    • 53749095835 scopus 로고    scopus 로고
    • Mobilizing patients in the intensive care unit: Improving neuromuscular weakness and physical function
    • Needham DM: Mobilizing patients in the intensive care unit: Improving neuromuscular weakness and physical function. JAMA 2008; 300:1685-1690
    • (2008) JAMA , vol.300 , pp. 1685-1690
    • Needham, D.M.1
  • 87
    • 0036550122 scopus 로고    scopus 로고
    • Effect of different dietary protein composition on skeletal muscle atrophy by suspension hypokinesia/hypodynamia in rats
    • 87. Tada O, Yokogoshi H: Effect of different dietary protein composition on skeletal muscle atrophy by suspension hypokinesia/hypodynamia in rats. J Nutr Sci Vitaminol (Tokyo) 2002; 48:115-119 (Pubitemid 34733442)
    • (2002) Journal of Nutritional Science and Vitaminology , vol.48 , Issue.2 , pp. 115-119
    • Tada, O.1    Yokogoshi, H.2
  • 89
  • 90
    • 31544435440 scopus 로고    scopus 로고
    • Modulations of muscle protein metabolism by branched-chain amino acids in normal and muscle-atrophying rats
    • 90. Kobayashi H, Kato H, Hirabayashi Y, et al: Modulations of muscle protein metabolism by branched-chain amino acids in normal and muscle-atrophying rats. J Nutr 2006; 136(1 Suppl):234S-236S. (Pubitemid 43156515)
    • (2006) Journal of Nutrition , vol.136 , Issue.1
    • Kobayashi, H.1    Kato, H.2    Hirabayashi, Y.3    Murakami, H.4    Suzuki, H.5
  • 92
    • 0027105781 scopus 로고
    • Alterations in glucose and protein metabolism in animals subjected to simulated microgravity
    • Mondon CE, Rodnick KJ, Dolkas CB, et al: Alterations in glucose and protein metabolism in animals subjected to simulated microgravity. Adv Space Res 1992; 12: 169-177
    • (1992) Adv Space Res , vol.12 , pp. 169-177
    • Mondon, C.E.1    Rodnick, K.J.2    Dolkas, C.B.3
  • 93
    • 0033639248 scopus 로고    scopus 로고
    • Immobilization depresses insulin signaling in skeletal muscle
    • Hirose M, Kaneki M, Sugita H, et al: Immobilization depresses insulin signaling in skeletal muscle. Am J Physiol Endocrinol Metab 2000; 279:E1235-E1241
    • (2000) Am J Physiol Endocrinol Metab , vol.279
    • Hirose, M.1    Kaneki, M.2    Sugita, H.3
  • 94
    • 4344705167 scopus 로고    scopus 로고
    • Development of whole-body and skeletal muscle insulin resistance after one day of hindlimb suspension
    • O'Keefe MP, Perez FR, Kinnick TR, et al: Development of whole-body and skeletal muscle insulin resistance after one day of hindlimb suspension. Metabolism 2004; 53: 1215-1222
    • (2004) Metabolism , vol.53 , pp. 1215-1222
    • O'Keefe, M.P.1    Perez, F.R.2    Kinnick, T.R.3
  • 95
    • 33746741630 scopus 로고    scopus 로고
    • Oxidant stress and skeletal muscle glucose transport: Roles of insulin signaling and p38 MAPK
    • DOI 10.1016/j.freeradbiomed.2006.05.031, PII S0891584906003613
    • 95. Kim JS, Saengsirisuwan V, Sloniger JA, et al: Oxidant stress and skeletal muscle glucose transport: Roles of insulin signaling and p38 MAPK. Free Radic Biol Med 2006; 41:818-824 (Pubitemid 44163415)
    • (2006) Free Radical Biology and Medicine , vol.41 , Issue.5 , pp. 818-824
    • Kim, J.S.1    Saengsirisuwan, V.2    Sloniger, J.A.3    Teachey, M.K.4    Henriksen, E.J.5
  • 96
    • 71649083541 scopus 로고    scopus 로고
    • Chromium supplement inhibits skeletal muscle atrophy in hindlimb-suspended mice
    • Dec [Epub ahead of print]
    • Dong F, Hua Y, Zhao P, et al: Chromium supplement inhibits skeletal muscle atrophy in hindlimb-suspended mice. J Nutr Biochem 2008 Dec 12 [Epub ahead of print]
    • (2008) J Nutr Biochem , vol.12
    • Dong, F.1    Hua, Y.2    Zhao, P.3
  • 97
    • 0036893386 scopus 로고    scopus 로고
    • Increased antioxidant capacity does not attenuate muscle atrophy caused by unweighting
    • Koesterer TJ, Dodd SL, Powers S: Increased antioxidant capacity does not attenuate muscle atrophy caused by unweighting. J Appl Physiol 2002; 93:1959-1965
    • (2002) J Appl Physiol , vol.93 , pp. 1959-1965
    • Koesterer, T.J.1    Dodd, S.L.2    Powers, S.3
  • 98
    • 27544510642 scopus 로고    scopus 로고
    • Attenuation of skeletal muscle atrophy via protease inhibition
    • DOI 10.1152/japplphysiol.01419.2004
    • 98. Morris CA, Morris LD, Kennedy AR, et al: Attenuation of skeletal muscle atrophy via protease inhibition. J Appl Physiol 2005; 99:1719-1727 (Pubitemid 41547168)
    • (2005) Journal of Applied Physiology , vol.99 , Issue.5 , pp. 1719-1727
    • Morris, C.A.1    Morris, L.D.2    Kennedy, A.R.3    Sweeney, H.L.4
  • 99
    • 0033065667 scopus 로고    scopus 로고
    • Reversal of weightlessness-induced musculoskeletal losses with androgens: Quantification by MRI
    • Wimalawansa SM, Chapa MT, Wei JN, et al: Reversal of weightlessness- induced musculoskeletal losses with androgens: Quantification by MRI. J Appl Physiol 1999; 86: 1841-1846
    • (1999) J Appl Physiol , vol.86 , pp. 1841-1846
    • Wimalawansa, S.M.1    Chapa, M.T.2    Wei, J.N.3
  • 100
    • 0023574441 scopus 로고
    • Effect of anabolic steroids on skeletal muscle mass during hindlimb suspension
    • 100. Tsika RW, Herrick RE, Baldwin KM: Effect of anabolic steroids on skeletal muscle mass during hindlimb suspension. J Appl Physiol 1987; 63:2122-2127 (Pubitemid 18016446)
    • (1987) Journal of Applied Physiology , vol.63 , Issue.5 , pp. 2122-2127
    • Tsika, R.W.1    Herrick, R.E.2    Baldwin, K.M.3
  • 101
    • 0036444476 scopus 로고    scopus 로고
    • Nandrolone decanoate pre-treatment attenuates unweighting-induced functional changes in rat soleus muscle
    • DOI 10.1046/j.1365-201X.2002.01035.x
    • 101. Joumaa WH, Bouhlel A, Bigard X, et al: Nandrolone decanoate pre-treatment attenuates unweighting-induced functional changes in rat soleus muscle. Acta Physiol Scand 2002; 176:301-309 (Pubitemid 35417384)
    • (2002) Acta Physiologica Scandinavica , vol.176 , Issue.4 , pp. 301-309
    • Joumaa, W.H.1    Bouhlel, A.2    Bigard, X.3    Leoty, C.4
  • 102
    • 34250876821 scopus 로고    scopus 로고
    • Estrogen administration attenuates immobilization-induced skeletal muscle atrophy in male rats
    • DOI 10.2170/physiolsci.RP006906
    • 102. Sugiura T, Ito N, Goto K, et al: Estrogen administration attenuates immobilization-induced skeletal muscle atrophy in male rats. J Physiol Sci 2006; 56:393-399 (Pubitemid 46974945)
    • (2006) Journal of Physiological Sciences , vol.56 , Issue.6 , pp. 393-399
    • Sugiura, T.1    Ito, N.2    Goto, K.3    Naito, H.4    Yoshioka, T.5    Powers, S.K.6
  • 103
    • 0026631464 scopus 로고
    • Reversal of diet-induced catabolism by infusion of recombinant insulin-like growth factor-I in humans
    • Clemmons DR, Smith-Banks A, Underwood LE: Reversal of diet-induced catabolism by infusion of recombinant insulin-like growth factor-I in humans. J Clin Endocrinol Metab 1992; 75:234-238
    • (1992) J Clin Endocrinol Metab , vol.75 , pp. 234-238
    • Clemmons, D.R.1    Smith-Banks, A.2    Underwood, L.E.3
  • 106
    • 0028152109 scopus 로고
    • Resistance exercise and growth hormone as countermeasures for skeletal muscle atrophy in hindlimb-suspended rats
    • 106. Linderman JK, Gosselink KL, Booth FW, et al: Resistance exercise and growth hormone as countermeasures for skeletal muscle atrophy in hindlimb-suspended rats. Am J Physiol 1994; 267:R365-R371 (Pubitemid 2132652)
    • (1994) AM.J.PHYSIOL. , vol.267 , Issue.2 PART 2
    • Linderman, J.K.1    Gosselink, K.L.2    Booth, F.W.3    Mukku, V.R.4    Grindeland, R.E.5
  • 107
    • 1342310797 scopus 로고    scopus 로고
    • Ectopic expression of IGF-I and Shh by skeletal muscle inhibits disuse-mediated skeletal muscle atrophy and bone osteopenia in vivo
    • Alzghoul MB, Gerrard D, Watkins BA, et al: Ectopic expression of IGF-I and Shh by skeletal muscle inhibits disuse-mediated skeletal muscle atrophy and bone osteopenia in vivo. FASEB J 2004; 18: 221-223
    • (2004) FASEB J , vol.18 , pp. 221-223
    • Alzghoul, M.B.1    Gerrard, D.2    Watkins, B.A.3
  • 108
    • 34247332956 scopus 로고    scopus 로고
    • FGFR1 inhibits skeletal muscle atrophy associated with hindlimb suspension
    • DOI 10.1186/1471-2474-8-32
    • 108. Eash J, Olsen A, Breur G, et al: FGFR1 inhibits skeletal muscle atrophy associated with hindlimb suspension. BMC Musculoskelet Disord 2007; 8:32 (Pubitemid 46633724)
    • (2007) BMC Musculoskeletal Disorders , vol.8 , pp. 32
    • Eash, J.1    Olsen, A.2    Breur, G.3    Gerrard, D.4    Hannon, K.5


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