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Volumn 121, Issue 1, 2014, Pages 115-126

Inhibition of the ubiquitin-proteasome pathway does not protect against ventilator-induced accelerated proteolysis or atrophy in the diaphragm

Author keywords

[No Author keywords available]

Indexed keywords

ATROGIN 1; CALPAIN; CASPASE 3; EPOXOMICIN; MUSCLE RING FINGER 1 PROTEIN; PROTEASOME; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3;

EID: 84902870086     PISSN: 00033022     EISSN: 15281175     Source Type: Journal    
DOI: 10.1097/ALN.0000000000000245     Document Type: Article
Times cited : (31)

References (51)
  • 5
    • 33845292563 scopus 로고    scopus 로고
    • Critical illness and mechanical ventilation: Effects on the diaphragm
    • discussion 1062-4
    • Jubran A: Critical illness and mechanical ventilation: Effects on the diaphragm. Respir Care 2006; 51:1054-61; discussion 1062-4
    • (2006) Respir Care , vol.51 , pp. 1054-1061
    • Jubran, A.1
  • 7
    • 77951969406 scopus 로고    scopus 로고
    • Oxidative stress is required for mechanical ventilation- induced protease activation in the diaphragm
    • Whidden MA, Smuder AJ, Wu M, Hudson MB, Nelson WB, Powers SK: Oxidative stress is required for mechanical ventilation- induced protease activation in the diaphragm. J Appl Physiol (1985) 2010; 108:1376-82
    • (2010) J Appl Physiol (1985) , vol.108 , pp. 1376-1382
    • Whidden, M.A.1    Smuder, A.J.2    Wu, M.3    Hudson, M.B.4    Nelson, W.B.5    Powers, S.K.6
  • 11
    • 84861528128 scopus 로고    scopus 로고
    • Cross-talk between the calpain and caspase-3 proteolytic systems in the diaphragm during prolonged mechanical ventilation
    • Nelson WB, Smuder AJ, Hudson MB, Talbert EE, Powers SK: Cross-talk between the calpain and caspase-3 proteolytic systems in the diaphragm during prolonged mechanical ventilation. Crit Care Med 2012; 40:1857-63
    • (2012) Crit Care Med , vol.40 , pp. 1857-1863
    • Nelson, W.B.1    Smuder, A.J.2    Hudson, M.B.3    Talbert, E.E.4    Powers, S.K.5
  • 12
    • 33644670831 scopus 로고    scopus 로고
    • Hindlimb casting decreases muscle mass in part by proteasome- dependent proteolysis but independent of protein synthesis
    • Krawiec BJ, Frost RA, Vary TC, Jefferson LS, Lang CH: Hindlimb casting decreases muscle mass in part by proteasome- dependent proteolysis but independent of protein synthesis. Am J Physiol Endocrinol Metab 2005; 289:E969-80
    • (2005) Am J Physiol Endocrinol Metab , vol.289
    • Krawiec, B.J.1    Frost, R.A.2    Vary, T.C.3    Jefferson, L.S.4    Lang, C.H.5
  • 15
    • 0022501701 scopus 로고
    • Architecture, composition, and contractile properties of rat soleus muscle grafts
    • Segal SS, White TP, Faulkner JA: Architecture, composition, and contractile properties of rat soleus muscle grafts. Am J Physiol 1986; 250(3 Pt 1):C474-9
    • (1986) Am J Physiol , vol.250 , Issue.3 PART 1
    • Segal, S.S.1    White, T.P.2    Faulkner, J.A.3
  • 16
    • 37849040918 scopus 로고    scopus 로고
    • Free radicals and muscle fatigue: Of ROS, canaries, and the IOC
    • Reid MB: Free radicals and muscle fatigue: Of ROS, canaries, and the IOC. Free Radic Biol Med 2008; 44:169-79
    • (2008) Free Radic Biol Med , vol.44 , pp. 169-179
    • Reid, M.B.1
  • 19
    • 21244450623 scopus 로고    scopus 로고
    • Selective downregulation of ubiquitin conjugation cascade mRNA occurs in the senescent rat soleus muscle
    • Deruisseau KC, Kavazis AN, Powers SK: Selective downregulation of ubiquitin conjugation cascade mRNA occurs in the senescent rat soleus muscle. Exp Gerontol 2005; 40:526-31
    • (2005) Exp Gerontol , vol.40 , pp. 526-531
    • Deruisseau, K.C.1    Kavazis, A.N.2    Powers, S.K.3
  • 21
    • 0029886022 scopus 로고    scopus 로고
    • Kinetic characterization of the chymotryptic activity of the 20S proteasome
    • Stein RL, Melandri F, Dick L: Kinetic characterization of the chymotryptic activity of the 20S proteasome. Biochemistry 1996; 35:3899-908
    • (1996) Biochemistry , vol.35 , pp. 3899-3908
    • Stein, R.L.1    Melandri, F.2    Dick, L.3
  • 23
    • 84857648793 scopus 로고    scopus 로고
    • Nuclear factor-B signaling contributes to mechanical ventilation- induced diaphragm weakness
    • Smuder AJ, Hudson MB, Nelson WB, Kavazis AN, Powers SK: Nuclear factor-B signaling contributes to mechanical ventilation- induced diaphragm weakness. Crit Care Med 2012; 40:927-34
    • (2012) Crit Care Med , vol.40 , pp. 927-934
    • Smuder, A.J.1    Hudson, M.B.2    Nelson, W.B.3    Kavazis, A.N.4    Powers, S.K.5
  • 25
    • 80053420374 scopus 로고    scopus 로고
    • Muscle sparing in muscle RING finger 1 null mice: Response to synthetic glucocorticoids
    • Baehr LM, Furlow JD, Bodine SC: Muscle sparing in muscle RING finger 1 null mice: Response to synthetic glucocorticoids. J Physiol 2011; 589(Pt 19):4759-76
    • (2011) J Physiol , vol.589 , Issue.PART 19 , pp. 4759-4776
    • Baehr, L.M.1    Furlow, J.D.2    Bodine, S.C.3
  • 28
    • 80053033764 scopus 로고    scopus 로고
    • Mechanistic links between oxidative stress and disuse muscle atrophy
    • Powers SK, Smuder AJ, Criswell DS: Mechanistic links between oxidative stress and disuse muscle atrophy. Antioxid Redox Signal 2011; 15:2519-28
    • (2011) Antioxid Redox Signal , vol.15 , pp. 2519-2528
    • Powers, S.K.1    Smuder, A.J.2    Criswell, D.S.3
  • 29
    • 0038239701 scopus 로고    scopus 로고
    • Selective degradation of oxidatively modified protein substrates by the proteasome
    • Grune T, Merker K, Sandig G, Davies KJ: Selective degradation of oxidatively modified protein substrates by the proteasome. Biochem Biophys Res Commun 2003; 305:709-18
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 709-718
    • Grune, T.1    Merker, K.2    Sandig, G.3    Davies, K.J.4
  • 31
    • 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; 4:183-90
    • (2001) Curr Opin Clin Nutr Metab Care , vol.4 , pp. 183-190
    • Jagoe, R.T.1    Goldberg, A.L.2
  • 33
    • 33750616737 scopus 로고    scopus 로고
    • Protein oxidation and proteolysis
    • Bader N, Grune T: Protein oxidation and proteolysis. Biol Chem 2006; 387:1351-5
    • (2006) Biol Chem , vol.387 , pp. 1351-1355
    • Bader, N.1    Grune, T.2
  • 34
    • 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; 151:229-41
    • (2006) Respir Physiol Neurobiol , vol.151 , pp. 229-241
    • Smith, M.A.1    Reid, M.B.2
  • 35
    • 14644400387 scopus 로고    scopus 로고
    • TNF- 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, Reid MB: TNF- acts via p38 MAPK to stimulate expression of the ubiquitin ligase atrogin1/MAFbx in skeletal muscle. FASEB J 2005; 19:362-70
    • (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    Reid, M.B.7
  • 36
    • 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:C806-12
    • (2003) Am J Physiol Cell Physiol , vol.285
    • Li, Y.P.1    Chen, Y.2    Li, A.S.3    Reid, M.B.4
  • 41
    • 66749160236 scopus 로고    scopus 로고
    • Properties of easily releasable myofilaments: Are they the first step in myofibrillar protein turnover?
    • Neti G, Novak SM, Thompson VF, Goll DE: Properties of easily releasable myofilaments: Are they the first step in myofibrillar protein turnover? Am J Physiol Cell Physiol 2009; 296:C1383-90
    • (2009) Am J Physiol Cell Physiol , vol.296
    • Neti, G.1    Novak, S.M.2    Thompson, V.F.3    Goll, D.E.4
  • 42
    • 0025287267 scopus 로고
    • Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy
    • Furuno K, Goodman MN, Goldberg AL: Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy. J Biol Chem 1990; 265:8550-7
    • (1990) J Biol Chem , vol.265 , pp. 8550-8557
    • Furuno, K.1    Goodman, M.N.2    Goldberg, A.L.3
  • 44
    • 19344372609 scopus 로고    scopus 로고
    • Response of the ubiquitin-proteasome pathway to changes in muscle activity
    • Reid MB: Response of the ubiquitin-proteasome pathway to changes in muscle activity. Am J Physiol Regul Integr Comp Physiol 2005; 288:R1423-31
    • (2005) Am J Physiol Regul Integr Comp Physiol , vol.288
    • Reid, M.B.1
  • 46
    • 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(1S suppl):227-37S
    • (1999) J Nutr , vol.129 , Issue.1 SUPPL.
    • Lecker, S.H.1    Solomon, V.2    Mitch, W.E.3    Goldberg, A.L.4
  • 47
    • 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; 335:1897-905
    • (1996) N Engl J Med , vol.335 , pp. 1897-1905
    • Mitch, W.E.1    Goldberg, A.L.2
  • 48
    • 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; 271:26690-7
    • (1996) J Biol Chem , vol.271 , pp. 26690-26697
    • Solomon, V.1    Goldberg, A.L.2
  • 49
    • 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(Pt 3):819-28
    • (2002) J Physiol , vol.545 , Issue.PART 3 , pp. 819-828
    • Tidball, J.G.1    Spencer, M.J.2
  • 50
    • 85047693596 scopus 로고    scopus 로고
    • Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions
    • Du J, Wang X, Miereles C, Bailey JL, Debigare R, Zheng B, Price SR, Mitch WE: Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions. J Clin Invest 2004; 113:115-23
    • (2004) J Clin Invest , vol.113 , pp. 115-123
    • Du, J.1    Wang, X.2    Miereles, C.3    Bailey, J.L.4    Debigare, R.5    Zheng, B.6    Price, S.R.7    Mitch, W.E.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.