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Volumn 111, Issue 11, 2011, Pages 2763-2773

Proteomic assessment of the acute phase of dystrophin deficiency in mdx mice

Author keywords

Autophagy; Duchenne muscular dystrophy; Glycolysis; Heat shock protein; Mitochondria; Proteomics

Indexed keywords

ACUTE PHASE PROTEIN; DYSTROPHIN; MUSCLE PROTEIN;

EID: 84855685420     PISSN: 14396319     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00421-011-1906-3     Document Type: Article
Times cited : (48)

References (50)
  • 1
    • 77952959405 scopus 로고    scopus 로고
    • Effect of creatine monohydrate in improving cellular energetics and muscle strength in ambulatory Duchenne muscular dystrophy patients: A randomized, placebo-controlled 31P MRS study
    • Banerjee B, Sharma U, Balasubramanian K, Kalaivani M, Kalra V, Jagannathan NR (2010) Effect of creatine monohydrate in improving cellular energetics and muscle strength in ambulatory Duchenne muscular dystrophy patients: a randomized, placebo-controlled 31P MRS study. Magn Reson Imaging 28:698-707
    • (2010) Magn Reson Imaging , vol.28 , pp. 698-707
    • Banerjee, B.1    Sharma, U.2    Balasubramanian, K.3    Kalaivani, M.4    Kalra, V.5    Jagannathan, N.R.6
  • 2
    • 0028813406 scopus 로고
    • Expression of heat-shock/stress proteins in Duchenne muscular dystrophy
    • Bornman L, Polla BS, Lotz BP, Gericke GS (1995) Expression of heat-shock/stress proteins in Duchenne muscular dystrophy. Muscle Nerve 18:23-31
    • (1995) Muscle Nerve , vol.18 , pp. 23-31
    • Bornman, L.1    Polla, B.S.2    Lotz, B.P.3    Gericke, G.S.4
  • 3
    • 0032531046 scopus 로고    scopus 로고
    • Effects of iron deprivation on the pathology and stress protein expression in murine X-linked muscular dystrophy
    • DOI 10.1016/S0006-2952(98)00055-0, PII S0006295298000550
    • Bornman L, Rossouw H, Gericke GS, Polla BS (1998) Effects of iron deprivation on the pathology and stress protein expression in murine X-linked muscular dystrophy. Biochem Pharmacol 56:751-757 (Pubitemid 28454586)
    • (1998) Biochemical Pharmacology , vol.56 , Issue.6 , pp. 751-757
    • Bornman, L.1    Rossouw, H.2    Gericke, G.S.3    Polla, B.S.4
  • 6
    • 33646176985 scopus 로고    scopus 로고
    • Targeted inhibition of Ca2+/calmodulin signaling exacerbates the dystrophic phenotype in mdx mouse muscle
    • Chakkalakal JV, Michel SA, Chin ER, Michel RN, Jasmin BJ (2006) Targeted inhibition of Ca2+/calmodulin signaling exacerbates the dystrophic phenotype in mdx mouse muscle. Hum Mol Genet 15:1423-1435
    • (2006) Hum Mol Genet , vol.15 , pp. 1423-1435
    • Chakkalakal, J.V.1    Michel, S.A.2    Chin, E.R.3    Michel, R.N.4    Jasmin, B.J.5
  • 8
    • 0023395716 scopus 로고
    • Effect of Duchenne muscular dystrophy on enzymes of energy metabolism in individual muscle fibers
    • Chi MM, Hintz CS, Mc Kee D, Felder S, Grant N, Kaiser KK, Lowry OH (1987) Effect of Duchenne muscular dystrophy on enzymes of energy metabolism in individual muscle fibers. Metabolism 36:761-767
    • (1987) Metabolism , vol.36 , pp. 761-767
    • Chi, M.M.1    Hintz, C.S.2    Mc Kee, D.3    Felder, S.4    Grant, N.5    Kaiser, K.K.6    Lowry, O.H.7
  • 9
    • 0036167216 scopus 로고    scopus 로고
    • A quantitative study of bioenergetics in skeletal muscle lacking utrophin and dystrophin
    • DOI 10.1016/S0960-8966(01)00278-4, PII S0960896601002784
    • Cole MA, Rafael JA, Taylor DJ, Lodi R, Davies KE, Styles P (2002) A quantitative study of bioenergetics in skeletal muscle lacking utrophin and dystrophin. Neuromuscul Disord 12:247-257 (Pubitemid 34136907)
    • (2002) Neuromuscular Disorders , vol.12 , Issue.3 , pp. 247-257
    • Cole, M.A.1    Rafael, J.A.2    Taylor, D.J.3    Lodi, R.4    Davies, K.E.5    Styles, P.6
  • 11
    • 4944230808 scopus 로고    scopus 로고
    • 2+-binding proteins demonstrates decreased calsequestrin expression in dystrophic mouse skeletal muscle
    • DOI 10.1111/j.1432-1033.2004.04332.x
    • Doran P, Dowling P, Lohan J, Mc Donnell K, Poetsch S, Ohlendieck K (2004) Subproteomics analysis of Ca+-binding proteins demonstrates decreased calsequestrin expression in dystrophic mouse skeletal muscle. Eur J Biochem 271:3943-3952 (Pubitemid 39331443)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.19 , pp. 3943-3952
    • Doran, P.1    Dowling, P.2    Lohan, J.3    McDonnell, K.4    Poetsch, S.5    Ohlendieck, K.6
  • 12
    • 33748339008 scopus 로고    scopus 로고
    • Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP
    • DOI 10.1002/pmic.200600082
    • Doran P, Martin G, Dowling P, Jockusch H, Ohlendieck K (2006) Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cv HSP. Proteomics 6:4610-4621 (Pubitemid 44336975)
    • (2006) Proteomics , vol.6 , Issue.16 , pp. 4610-4621
    • Doran, P.1    Martin, G.2    Dowling, P.3    Jockusch, H.4    Ohlendieck, K.5
  • 13
    • 38949107303 scopus 로고    scopus 로고
    • Opposite pathobiochemical fate of pyruvate kinase and adenylate kinase in aged rat skeletal muscle as revealed by proteomic DIGE analysis
    • DOI 10.1002/pmic.200700475
    • Doran P, O'Connell K, Gannon J, Kavanagh M, Ohlendieck K (2008) Opposite pathobiochemical fate of pyruvate kinase and adenyl- ate kinase in aged rat skeletal muscle as revealed by proteomic DIGE analysis. Proteomics 8:364-377 (Pubitemid 351212333)
    • (2008) Proteomics , vol.8 , Issue.2 , pp. 364-377
    • Doran, P.1    O'Connell, K.2    Gannon, J.3    Kavanagh, M.4    Ohlendieck, K.5
  • 14
    • 60549096114 scopus 로고    scopus 로고
    • Proteomic profiling of antisense-induced exon skipping reveals reversal of pathobiochemical abnormalities in dystrophic mdx diaphragm
    • Doran P, Wilton SD, Fletcher S, Ohlendieck K (2009) Proteomic profiling of antisense-induced exon skipping reveals reversal of pathobiochemical abnormalities in dystrophic mdx diaphragm. Proteomics 9:671-685
    • (2009) Proteomics , vol.9 , pp. 671-685
    • Doran, P.1    Wilton, S.D.2    Fletcher, S.3    Ohlendieck, K.4
  • 15
    • 33750466222 scopus 로고    scopus 로고
    • Microtubule: A common target for Parkin and Parkinson's disease toxins
    • DOI 10.1177/1073858406293853
    • Feng J (2006) Microtubule: a common target for parkin and Parkinson's disease toxins. Neuroscientist 12:469-476 (Pubitemid 44657962)
    • (2006) Neuroscientist , vol.12 , Issue.6 , pp. 469-476
    • Feng, J.1
  • 16
    • 0023909619 scopus 로고
    • EMG computerized analysis of localized fatigue in Duchenne muscular dystrophy
    • Frascarelli M, Rocchi L, Feola I (1988) EMG computerized analysis of localized fatigue in Duchenne muscular dystrophy. Muscle Nerve 11:757-761
    • (1988) Muscle Nerve , vol.11 , pp. 757-761
    • Frascarelli, M.1    Rocchi, L.2    Feola, I.3
  • 17
    • 40549116289 scopus 로고    scopus 로고
    • Optimizing the difference gel electrophoresis (DIGE) technology
    • In: Vlahou A (ed Humana Press, Totowa, NJ
    • Friedman DB, Lilley KS (2008) Optimizing the difference gel electrophoresis (DIGE) technology. In: Vlahou A (ed) Clinical proteomics: methods and protocols. Humana Press, Totowa, NJ, pp 93-124
    • (2008) Clinical Proteomics: Methods and Protocols , pp. 93-124
    • Friedman, D.B.1    Lilley, K.S.2
  • 18
    • 0142182391 scopus 로고    scopus 로고
    • Proteomic analysis of mdx skeletal muscle: Great reduction of adenylate kinase 1 expression and enzymatic activity
    • DOI 10.1002/pmic.200300561
    • Ge Y, Molloy MP, Chamberlain JS, Andrews PC (2003) Proteomic analysis of mdx skeletal muscle: great reduction of adenylate kinase 1 expression and enzymatic activity. Proteomics 3:1895-1903 (Pubitemid 37305883)
    • (2003) Proteomics , vol.3 , Issue.10 , pp. 1895-1903
    • Ge, Y.1    Molloy, M.P.2    Chamberlain, J.S.3    Andrews, P.C.4
  • 19
    • 4444267191 scopus 로고    scopus 로고
    • Differential expression of the skeletal muscle proteome in mdx mice at different ages
    • DOI 10.1002/elps.200406013
    • Ge Y, Molloy MP, Chamberlain JS, Andrews PC (2004) Differential expression of the skeletal muscle proteome in mdx mice at different ages. Electrophoresis 25:2576-2585 (Pubitemid 39193668)
    • (2004) Electrophoresis , vol.25 , Issue.15 , pp. 2576-2585
    • Ge, Y.1    Molloy, M.P.2    Chamberlain, J.S.3    Andrews, P.C.4
  • 24
    • 33745183090 scopus 로고    scopus 로고
    • Naturally occurring utrophin correlates with disease severity in Duchenne muscular dystrophy
    • DOI 10.1093/hmg/ddl083
    • Kleopa KA, Drousiotou A, Mavrikiou E, Ormiston A, Kyriakides T (2006) Naturally occurring utrophin correlates with disease severity in Duchenne muscular dystrophy. Hum Mol Genet 15:1623-1628 (Pubitemid 43904828)
    • (2006) Human Molecular Genetics , vol.15 , Issue.10 , pp. 1623-1628
    • Kleopa, K.A.1    Drousiotou, A.2    Mavrikiou, E.3    Ormiston, A.4    Kyriakides, T.5
  • 25
    • 4043176138 scopus 로고    scopus 로고
    • Identification of myofibrillar substrates for mu-calpain
    • Lametsch R, Roepstorff P, Moller HS, Bendixen E (2004) Identification of myofibrillar substrates for mu-calpain. Meat Sci 68:515-521
    • (2004) Meat Sci , vol.68 , pp. 515-521
    • Lametsch, R.1    Roepstorff, P.2    Moller, H.S.3    Bendixen, E.4
  • 26
    • 0032959413 scopus 로고    scopus 로고
    • 31P magnetic resonance spectroscopy study
    • DOI 10.1093/brain/122.1.121
    • Lodi R, Kemp GJ, Muntoni F, Thompson CH, Rae C, Taylor J, Styles P, Taylor DJ (1999) Reduced cytosolic acidification during exercise suggests defective glycolytic activity in skeletal muscle of patients with Becker muscular dystrophy. An in vivo 31P magneticresonance spectroscopy study. Brain 122(Pt 1):121-130 (Pubitemid 29046278)
    • (1999) Brain , vol.122 , Issue.1 , pp. 121-130
    • Lodi, R.1    Kemp, G.J.2    Muntoni, F.3    Thompson, C.H.4    Rae, C.5    Taylor, J.6    Styles, P.7    Taylor, D.J.8
  • 29
    • 28444475607 scopus 로고    scopus 로고
    • Correlation between mRNA and protein abundance in Desulfovibrio vulgaris: A multiple regression to identify sources of variations
    • DOI 10.1016/j.bbrc.2005.11.055, PII S0006291X05025842
    • Nie L, Wu G, Zhang W (2006) Correlation between m RNA and protein abundance in Desulfovibrio vulgaris: a multiple regression to identify sources of variations. Biochem Biophys Res Commun 339:603-610 (Pubitemid 41739710)
    • (2006) Biochemical and Biophysical Research Communications , vol.339 , Issue.2 , pp. 603-610
    • Nie, L.1    Wu, G.2    Zhang, W.3
  • 31
    • 0036133699 scopus 로고    scopus 로고
    • Creatine supplementation reduces skeletal muscle degeneration and enhances mitochondrial function in mdx mice
    • DOI 10.1016/S0960-8966(01)00273-5, PII S0960896601002735
    • Passaquin AC, Renard M, Kay L, Challet C, Mokhtarian A, Wallimann T, Ruegg UT (2002) Creatine supplementation reduces skeletal muscle degeneration and enhances mitochon-drial function in mdx mice. Neuromuscul Disord 12:174-182 (Pubitemid 33152736)
    • (2002) Neuromuscular Disorders , vol.12 , Issue.2 , pp. 174-182
    • Passaquin, A.-C.1    Renard, M.2    Kay, L.3    Challet, C.4    Mokhtarian, A.5    Wallimann, T.6    Ruegg, U.T.7
  • 32
    • 34548591279 scopus 로고    scopus 로고
    • RAAV6-Microdystrophin rescues aberrant Golgi complex organization in mdx skeletal muscles
    • DOI 10.1111/j.1600-0854.2007.00622.x
    • Percival JM, Gregorevic P, Odom GL, Banks GB, Chamberlain JS, Froehner SC (2007) r AAV6-microdystrophin rescues aberrant golgi complex organization in mdx skeletal muscles. Traffic 8:1424-1439 (Pubitemid 47394246)
    • (2007) Traffic , vol.8 , Issue.10 , pp. 1424-1439
    • Percival, J.M.1    Gregorevic, P.2    Odom, G.L.3    Banks, G.B.4    Chamberlain, J.S.5    Froehner, S.C.6
  • 34
    • 0031788804 scopus 로고    scopus 로고
    • 2+ handling and survival in mdx skeletal muscle cells
    • DOI 10.1016/S0014-5793(98)01399-4, PII S0014579398013994
    • Pulido SM, Passaquin AC, Leijendekker WJ, Challet C, Wallimann T, Ruegg UT (1998) Creatine supplementation improves intracel-lular Ca2+ handling and survival in mdx skeletal muscle cells. FEBS Lett 439:357-362 (Pubitemid 28546675)
    • (1998) FEBS Letters , vol.439 , Issue.3 , pp. 357-362
    • Pulido, S.M.1    Passaquin, A.C.2    Leijendekker, W.J.3    Challet, C.4    Wallimann, T.5    Ruegg, U.T.6
  • 36
    • 0026546263 scopus 로고
    • Contractile properties and susceptibility to exercise-induced damage of normal and mdx mouse tibialis anterior muscle
    • Sacco P, Jones DA, Dick JR, Vrbova G (1992) Contractile properties and susceptibility to exercise-induced damage of normal and mdx mouse tibialis anterior muscle. Clin Sci (Lond) 82: 227-236
    • (1992) Clin Sci (Lond) , vol.82 , pp. 227-236
    • Sacco, P.1    Jones, D.A.2    Dick, J.R.3    Vrbova, G.4
  • 37
    • 78751498734 scopus 로고    scopus 로고
    • Increased catalase expression improves muscle function in mdx mice
    • Selsby JT (2011) Increased catalase expression improves muscle function in mdx mice. Exp Physiol 96:194-202
    • (2011) Exp Physiol , vol.96 , pp. 194-202
    • Selsby, J.T.1
  • 39
    • 68149117477 scopus 로고    scopus 로고
    • Reciprocal amplification of ROS and Ca(2+) signals in stressed mdx dystrophic skeletal muscle fibers
    • Shkryl VM, Martins AS, Ullrich ND, Nowycky MC, Niggli E, Shirokova N (2009) Reciprocal amplification of ROS and Ca(2+) signals in stressed mdx dystrophic skeletal muscle fibers. Pflugers Arch 458:915-928
    • (2009) Pflugers Arch , vol.458 , pp. 915-928
    • Shkryl, V.M.1    Martins, A.S.2    Ullrich, N.D.3    Nowycky, M.C.4    Niggli, E.5    Shirokova, N.6
  • 40
    • 0024353559 scopus 로고
    • The molecular basis of muscular dystrophy in the mdx mouse: A point mutation
    • Sicinski P, Geng Y, Ryder-Cook AS, Barnard EA, Darlison MG, Barnard PJ (1989) The molecular basis ofmuscular dystrophy in the mdx mouse: a point mutation. Science 244:1578-1580 (Pubitemid 19189735)
    • (1989) Science , vol.244 , Issue.4912 , pp. 1578-1580
    • Sicinski, P.1    Geng, Y.2    Ryder-Cook, A.S.3    Barnard, E.A.4    Darlison, M.G.5    Barnard, P.J.6
  • 41
    • 0028932618 scopus 로고
    • Calpains are activated in necrotic fibers from mdx dystrophic mice
    • Spencer MJ, Croall DE, Tidball JG (1995) Calpains are activated in necrotic fibers from mdx dystrophic mice. J Biol Chem 270:10909-10914
    • (1995) J Biol Chem , vol.270 , pp. 10909-10914
    • Spencer, M.J.1    Croall, D.E.2    Tidball, J.G.3
  • 43
    • 0029906168 scopus 로고    scopus 로고
    • Amelioration of the dystrophic phenotype of mdx mice using a truncated utrophin transgene
    • DOI 10.1038/384349a0
    • Tinsley JM, Potter AC, Phelps SR, Fisher R, Trickett JI, Davies KE (1996) Amelioration of the dystrophic phenotype of mdx mice using a truncated utrophin transgene. Nature 384:349-353 (Pubitemid 26408514)
    • (1996) Nature , vol.384 , Issue.6607 , pp. 349-353
    • Tinsley, J.M.1    Potter, A.C.2    Phelps, S.R.3    Fisher, R.4    Trickett, J.I.5    Davies, K.E.6
  • 44
    • 0035068170 scopus 로고    scopus 로고
    • Identification of altered gene expression in skeletal muscles from Duchenne muscular dystrophy patients
    • DOI 10.1016/S0960-8966(00)00198-X, PII S096089660000198X
    • Tkatchenko AV, Pietu G, Cros N, Gannoun-Zaki L, Auffray C, Leger JJ, Dechesne CA (2001) Identification ofaltered gene expression in skeletal muscles from Duchenne muscular dystrophy patients. Neuromuscul Disord 11:269-277 (Pubitemid 32288797)
    • (2001) Neuromuscular Disorders , vol.11 , Issue.3 , pp. 269-277
    • Tkatchenko, A.V.1    Pietu, G.2    Cros, N.3    Gannoun-Zaki, L.4    Auffray, C.5    Leger, J.J.6    Dechesne, C.A.7
  • 45
    • 0343376097 scopus 로고    scopus 로고
    • Difference gel electrophoresis: A single gel method for detecting changes in protein extracts
    • Unlu M, Morgan ME, Minden JS (1997) Difference gel electropho-resis: a single gel method for detecting changes in protein extracts. Electrophoresis 18:2071-2077 (Pubitemid 27501267)
    • (1997) Electrophoresis , vol.18 , Issue.11 , pp. 2071-2077
    • Unlu, M.1    Morgan, M.E.2    Minden, J.S.3
  • 46
    • 0023832469 scopus 로고
    • Fast muscle fibers are preferentially affected in Duchenne muscular dystrophy
    • DOI 10.1016/0092-8674(88)90463-1
    • Webster C, Silberstein L, Hays AP, Blau HM (1988) Fast muscle fibers are preferentially affected in Duchenne muscular dystro-phy. Cell 52:503-513 (Pubitemid 18067515)
    • (1988) Cell , vol.52 , Issue.4 , pp. 503-513
    • Webster, C.1    Silberstein, L.2    Hays, A.P.3    Blau, H.M.4
  • 47
    • 69449101150 scopus 로고    scopus 로고
    • Loss of positive allosteric interactions between neuronal nitric oxide synthase and phosphofructokinase contributes to defects in glycolysis and increased fatigability in muscular dystrophy
    • Wehling-Henricks M, Oltmann M, Rinaldi C, Myung KH, Tidball JG (2009) Loss of positive allosteric interactions between neuronal nitric oxide synthase and phosphofructokinase contributes to defects in glycolysis and increased fatigability in muscular dystrophy. Hum Mol Genet 18:3439-3451
    • (2009) Hum Mol Genet , vol.18 , pp. 3439-3451
    • Wehling-Henricks, M.1    Oltmann, M.2    Rinaldi, C.3    Myung, K.H.4    Tidball, J.G.5
  • 49
    • 40149091415 scopus 로고    scopus 로고
    • Dystrophin deficiency in canine X-linked muscular dystrophy in Japan (CXMDJ) alters myosin heavy chain expression profiles in the diaphragm more markedly than in the tibialis cranialis muscle
    • Yuasa K, Nakamura A, Hijikata T, Takeda S (2008) Dystrophin deficiency in canine X-linked muscular dystrophy in Japan (CXMDJ) alters myosin heavy chain expression profiles in the diaphragm more markedly than in the tibialis cranialis muscle. BMC Musculoskelet Disord 9:1
    • (2008) BMC Musculoskelet Disord , vol.9 , pp. 1
    • Yuasa, K.1    Nakamura, A.2    Hijikata, T.3    Takeda, S.4


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