메뉴 건너뛰기




Volumn 3, Issue 4, 2009, Pages 486-497

Proteomics identification of differentially expressed proteins in the muscle of dysferlin myopathy patients

Author keywords

2 DE; Dysferlin; Facioscapulohumerial muscular dystrophy; Limb girdle muscular dystrophy 2A; Muscular dystrophies

Indexed keywords

ACTININ; ACYL COENZYME A DEHYDROGENASE; ALPHA ACTIN; ALPHA CRYSTALLIN; ANKYRIN; ANKYRIN REPEAT PROTEIN 2; CARBONATE DEHYDRATASE III; DYSFERLIN; ENOLASE; FRUCTOSE BISPHOSPHATE ALDOLASE; HEAT SHOCK PROTEIN; MYOSIN III; MYOSIN LIGHT CHAIN; MYOSIN LIGHT CHAIN 2; PROTEIN TRIM 72; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; TROPONIN T; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 65549125590     PISSN: 18628346     EISSN: None     Source Type: Journal    
DOI: 10.1002/prca.200800087     Document Type: Article
Times cited : (13)

References (36)
  • 1
    • 30744443289 scopus 로고    scopus 로고
    • Common pathological mechanisms in mouse models for muscular dystrophies
    • Turk, R., Sterrenburg, E., van der Wees, C. G., de Meijer, E. J. et al., Common pathological mechanisms in mouse models for muscular dystrophies. FASEB J. 2006, 20, 127-129.
    • (2006) FASEB J , vol.20 , pp. 127-129
    • Turk, R.1    Sterrenburg, E.2    van der Wees, C.G.3    de Meijer, E.J.4
  • 2
    • 17344365600 scopus 로고    scopus 로고
    • Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy
    • Liu, J., Aoki, M., Illa, I., Wu, C. et al., Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy. Nat. Genet. 1998, 20, 31-36.
    • (1998) Nat. Genet , vol.20 , pp. 31-36
    • Liu, J.1    Aoki, M.2    Illa, I.3    Wu, C.4
  • 3
    • 17344363640 scopus 로고    scopus 로고
    • A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B
    • Bashir, R., Britton, S., Strachan, T., Keers, S. et al., A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B. Nat Genet 1998, 20, 37-42.
    • (1998) Nat Genet , vol.20 , pp. 37-42
    • Bashir, R.1    Britton, S.2    Strachan, T.3    Keers, S.4
  • 4
    • 0035109410 scopus 로고    scopus 로고
    • Distal anterior compartment myopathy: A dysferlin mutation causing a new muscular dystrophy phenotype
    • Illa, I., Serrano-Munuera, C., Gallardo, E., Lasa, A. et al., Distal anterior compartment myopathy: a dysferlin mutation causing a new muscular dystrophy phenotype. Ann. Neurol. 2001, 49, 130-134.
    • (2001) Ann. Neurol , vol.49 , pp. 130-134
    • Illa, I.1    Serrano-Munuera, C.2    Gallardo, E.3    Lasa, A.4
  • 5
    • 0037738510 scopus 로고    scopus 로고
    • Defective membrane repair in dysferlin-deficient muscular dystrophy
    • Bansal, D., Miyake, K., Vogel, S. S., Groh, S. et al., Defective membrane repair in dysferlin-deficient muscular dystrophy. Nature 2003, 423, 168-172.
    • (2003) Nature , vol.423 , pp. 168-172
    • Bansal, D.1    Miyake, K.2    Vogel, S.S.3    Groh, S.4
  • 6
    • 31344467095 scopus 로고    scopus 로고
    • Proteomic investigation of the molecular pathophysiology of dysferlinopathy
    • De Palma, S., Morandi, L., Mariani, E., Begum, S. et al., Proteomic investigation of the molecular pathophysiology of dysferlinopathy. Proteomics 2006, 6, 379-385.
    • (2006) Proteomics , vol.6 , pp. 379-385
    • De Palma, S.1    Morandi, L.2    Mariani, E.3    Begum, S.4
  • 7
    • 16844364725 scopus 로고    scopus 로고
    • Increased levels of adenine nucleotide translocator 1 protein and response to oxidative stress are early events in facioscapulohumeral muscular dystrophy muscle
    • Laoudj-Chenivesse, D., Carnac, G., Bisbal, C., Hugon, G. et al., Increased levels of adenine nucleotide translocator 1 protein and response to oxidative stress are early events in facioscapulohumeral muscular dystrophy muscle. J. Mol. Med. 2005, 83, 216-224.
    • (2005) J. Mol. Med , vol.83 , pp. 216-224
    • Laoudj-Chenivesse, D.1    Carnac, G.2    Bisbal, C.3    Hugon, G.4
  • 8
    • 33749605124 scopus 로고    scopus 로고
    • Parallel protein and transcript profiles of FSHD patient muscles correlate to the D4Z4 arrangement and reveal a common impairment of slow to fast fiber differentiation and a general deregulation of MyoD-dependent genes
    • Celegato, B., Capitanio, D., Pescatori, M., Romualdi, C. et al., Parallel protein and transcript profiles of FSHD patient muscles correlate to the D4Z4 arrangement and reveal a common impairment of slow to fast fiber differentiation and a general deregulation of MyoD-dependent genes. Proteomics 2006, 6, 5303-5321.
    • (2006) Proteomics , vol.6 , pp. 5303-5321
    • Celegato, B.1    Capitanio, D.2    Pescatori, M.3    Romualdi, C.4
  • 9
    • 0035846620 scopus 로고    scopus 로고
    • Inflammation in dysferlin myopathy: Immunohistochemical characterization of 13 patients
    • Gallardo, E., Rojas-Garcia, R., de Luna, N., Pou, A. et al., Inflammation in dysferlin myopathy: immunohistochemical characterization of 13 patients. Neurology 2001, 57, 2136-2138.
    • (2001) Neurology , vol.57 , pp. 2136-2138
    • Gallardo, E.1    Rojas-Garcia, R.2    de Luna, N.3    Pou, A.4
  • 10
    • 0033784812 scopus 로고    scopus 로고
    • Secondary reduction in calpain 3 expression in patients with limb girdle muscular dystrophy type 2B and Miyoshi myopathy (primary dysferlinopathies)
    • Anderson, L. V., Harrison, R. M., Pogue, R., Vafiadaki, E. et al., Secondary reduction in calpain 3 expression in patients with limb girdle muscular dystrophy type 2B and Miyoshi myopathy (primary dysferlinopathies). Neuromuscul. Disord. 2000, 10, 553-559.
    • (2000) Neuromuscul. Disord , vol.10 , pp. 553-559
    • Anderson, L.V.1    Harrison, R.M.2    Pogue, R.3    Vafiadaki, E.4
  • 11
    • 0028961960 scopus 로고
    • Inflammatory response in facioscapulohumeral muscular dystrophy (FSHD): Immunocytochemical and genetic analyses
    • Arahata, K., Ishihara, T., Fukunaga, H., Orimo, S. et al., Inflammatory response in facioscapulohumeral muscular dystrophy (FSHD): immunocytochemical and genetic analyses. Muscle Nerve 1995, 2, S56-66.
    • (1995) Muscle Nerve , vol.2
    • Arahata, K.1    Ishihara, T.2    Fukunaga, H.3    Orimo, S.4
  • 12
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels
    • Shevchenko, A., Wilm, M., Vorm, O., Mann, M., Mass spectrometric sequencing of proteins silver-stained polyacrylamide gels. Anal. Chem. 1996, 68, 850-858.
    • (1996) Anal. Chem , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 13
    • 0038000050 scopus 로고    scopus 로고
    • Detection of arginine dimethylated peptides by parallel precursor ion scanning mass spectrometry in positive ion mode
    • Rappsilber, J., Friesen, W. J., Paushkin, S., Dreyfuss, G., Mann, M., Detection of arginine dimethylated peptides by parallel precursor ion scanning mass spectrometry in positive ion mode. Anal. Chem. 2003, 75, 3107-3114.
    • (2003) Anal. Chem , vol.75 , pp. 3107-3114
    • Rappsilber, J.1    Friesen, W.J.2    Paushkin, S.3    Dreyfuss, G.4    Mann, M.5
  • 14
    • 0034837026 scopus 로고    scopus 로고
    • a possible active factor in dermatomyositis
    • Cathepsins are upregulated by IFN-gamma/STAT1 in human muscle culture
    • Gallardo, E., de Andres, I., Illa, I., Cathepsins are upregulated by IFN-gamma/STAT1 in human muscle culture: a possible active factor in dermatomyositis. J. Neuropathol. Exp. Neurol. 2001, 60, 847-855.
    • (2001) J. Neuropathol. Exp. Neurol , vol.60 , pp. 847-855
    • Gallardo, E.1    de Andres, I.2    Illa, I.3
  • 15
    • 0037439275 scopus 로고    scopus 로고
    • Myotilin, the limb-girdle muscular dystrophy 1A (LGMD1A) protein, cross-links actin filaments and controls sarcomere assembly
    • Salmikangas, P., van der Ven, P. F., Lalowski, M., Taivainen, A. et al., Myotilin, the limb-girdle muscular dystrophy 1A (LGMD1A) protein, cross-links actin filaments and controls sarcomere assembly. Hum. Mol. Genet. 2003, 12, 189-203.
    • (2003) Hum. Mol. Genet , vol.12 , pp. 189-203
    • Salmikangas, P.1    van der Ven, P.F.2    Lalowski, M.3    Taivainen, A.4
  • 16
    • 0030827949 scopus 로고    scopus 로고
    • Actinin-associated LIM protein: Identification of a domain interaction between PDZ and spectrin-like repeat motifs
    • Xia, H., Winokur, S. T., Kuo, W. L., Altherr, M. R., Bredt, D. S., Actinin-associated LIM protein: identification of a domain interaction between PDZ and spectrin-like repeat motifs. J. Cell. Biol. 1997, 139, 507-515.
    • (1997) J. Cell. Biol , vol.139 , pp. 507-515
    • Xia, H.1    Winokur, S.T.2    Kuo, W.L.3    Altherr, M.R.4    Bredt, D.S.5
  • 17
    • 0029963979 scopus 로고    scopus 로고
    • Juvenile limb-girdle muscular dystrophy. Clinical, histopathological and genetic data from a small community living in the Reunion Island
    • Fardeau, M., Hillaire, D., Mignard, C., Feingold, N. et al., Juvenile limb-girdle muscular dystrophy. Clinical, histopathological and genetic data from a small community living in the Reunion Island. Brain 1996, 119, 295-308.
    • (1996) Brain , vol.119 , pp. 295-308
    • Fardeau, M.1    Hillaire, D.2    Mignard, C.3    Feingold, N.4
  • 18
    • 2142713041 scopus 로고    scopus 로고
    • Modulation of actomyosin contractility by myosin light chain phosphorylation/dephosphorylation through Rho GTPases signaling specifies axon formation in neurons
    • Kim, Y., Chang, S., Modulation of actomyosin contractility by myosin light chain phosphorylation/dephosphorylation through Rho GTPases signaling specifies axon formation in neurons. Biochem. Biophys. Res. Commun. 2004, 318, 579-587.
    • (2004) Biochem. Biophys. Res. Commun , vol.318 , pp. 579-587
    • Kim, Y.1    Chang, S.2
  • 19
  • 20
    • 19444383095 scopus 로고    scopus 로고
    • Expression of Ankrd2 in fast and slow muscles and its response to stretch are consistent with a role in slow muscle function
    • discussion 2320
    • McKoy, G., Hou, Y., Yang, S. Y., Vega Avelaira, D. et al., Expression of Ankrd2 in fast and slow muscles and its response to stretch are consistent with a role in slow muscle function. J. Appl. Physiol. 2005, 98, 2337-2343; discussion 2320.
    • (2005) J. Appl. Physiol , vol.98 , pp. 2337-2343
    • McKoy, G.1    Hou, Y.2    Yang, S.Y.3    Vega Avelaira, D.4
  • 21
    • 0038291908 scopus 로고    scopus 로고
    • Exercise-induced HSP27, HSP70 and MAPK responses in human skeletal muscle
    • Thompson, H. S., Maynard, E. B., Morales, E. R., Scordilis, S. P., Exercise-induced HSP27, HSP70 and MAPK responses in human skeletal muscle. Acta Physiol. Scand. 2003, 178, 61-72.
    • (2003) Acta Physiol. Scand , vol.178 , pp. 61-72
    • Thompson, H.S.1    Maynard, E.B.2    Morales, E.R.3    Scordilis, S.P.4
  • 22
    • 25144518100 scopus 로고    scopus 로고
    • Differential expression of the fast skeletal muscle proteome following chronic low-frequency stimulation
    • Donoghue, P., Doran, P., Dowling, P., Ohlendieck, K., Differential expression of the fast skeletal muscle proteome following chronic low-frequency stimulation. Biochim. Biophys. Acta 2005, 1752, 166-176.
    • (2005) Biochim. Biophys. Acta , vol.1752 , pp. 166-176
    • Donoghue, P.1    Doran, P.2    Dowling, P.3    Ohlendieck, K.4
  • 23
    • 0035105723 scopus 로고    scopus 로고
    • Fiber-type susceptibility to eccentric contraction-induced damage of hindlimb-unloaded rat AL muscles
    • Vijayan, K., Thompson, J. L., Norenberg, K. M., Fitts, R. H., Riley, D. A., Fiber-type susceptibility to eccentric contraction-induced damage of hindlimb-unloaded rat AL muscles. J. Appl. Physiol. 2001, 90, 770-776.
    • (2001) J. Appl. Physiol , vol.90 , pp. 770-776
    • Vijayan, K.1    Thompson, J.L.2    Norenberg, K.M.3    Fitts, R.H.4    Riley, D.A.5
  • 24
    • 0021952893 scopus 로고
    • Firing patterns of motor units in normal rats
    • Hennig, R., Lomo, T., Firing patterns of motor units in normal rats. Nature 1985, 314, 164-166.
    • (1985) Nature , vol.314 , pp. 164-166
    • Hennig, R.1    Lomo, T.2
  • 25
    • 8844276054 scopus 로고    scopus 로고
    • Regulation of muscle fiber type and running endurance by PPAR-delta
    • Wang, Y. X., Zhang, C. L., Yu, R. T., Cho, H. K. et al., Regulation of muscle fiber type and running endurance by PPAR-delta. PLoS Biol. 2004, 2, e294.
    • (2004) PLoS Biol , vol.2
    • Wang, Y.X.1    Zhang, C.L.2    Yu, R.T.3    Cho, H.K.4
  • 26
    • 0032791810 scopus 로고    scopus 로고
    • Correlation of muscle fiber type measurements with clinical and molecular genetic data in Duchenne muscular dystrophy
    • Wang, J. F., Forst, J., Schroder, S., Schroder, J. M., Correlation of muscle fiber type measurements with clinical and molecular genetic data in Duchenne muscular dystrophy. Neuromuscul. Disord. 1999, 9, 150-158.
    • (1999) Neuromuscul. Disord , vol.9 , pp. 150-158
    • Wang, J.F.1    Forst, J.2    Schroder, S.3    Schroder, J.M.4
  • 27
    • 0023832469 scopus 로고
    • Fast muscle fibers are preferentially affected in Duchenne muscular dystrophy
    • Webster, C., Silberstein, L., Hays, A. P., Blau, H. M., Fast muscle fibers are preferentially affected in Duchenne muscular dystrophy. Cell 1988, 52, 503-513.
    • (1988) Cell , vol.52 , pp. 503-513
    • Webster, C.1    Silberstein, L.2    Hays, A.P.3    Blau, H.M.4
  • 29
    • 0028115716 scopus 로고
    • Effects of age and training on skeletal muscle physiology and performance
    • Thompson, L. V., Effects of age and training on skeletal muscle physiology and performance. Phys. Ther. 1994, 74, 71-81.
    • (1994) Phys. Ther , vol.74 , pp. 71-81
    • Thompson, L.V.1
  • 30
    • 25844491047 scopus 로고    scopus 로고
    • Actin-organising properties of the muscular dystrophy protein myotilin
    • von Nandelstadh, P., Gronholm, M., Moza, M., Lamberg, A. et al., Actin-organising properties of the muscular dystrophy protein myotilin. Exp. Cell. Res. 2005, 310, 131-139.
    • (2005) Exp. Cell. Res , vol.310 , pp. 131-139
    • von Nandelstadh, P.1    Gronholm, M.2    Moza, M.3    Lamberg, A.4
  • 31
    • 0023628665 scopus 로고
    • Myofibrillar M-band structure and composition of physiologically defined rat motor units
    • Thornell, L. E., Carlsson, E., Kugelberg, E., Grove, B. K., Myofibrillar M-band structure and composition of physiologically defined rat motor units. Am. J. Physiol. 1987, 253, C456-468.
    • (1987) Am. J. Physiol , vol.253
    • Thornell, L.E.1    Carlsson, E.2    Kugelberg, E.3    Grove, B.K.4
  • 32
    • 0031910828 scopus 로고    scopus 로고
    • The Rho family G proteins play a critical role in muscle differentiation
    • Takano, H., Komuro, I., Oka, T., Shiojima, I. et al., The Rho family G proteins play a critical role in muscle differentiation. Mol. Cell. Biol. 1998, 18, 1580-1589.
    • (1998) Mol. Cell. Biol , vol.18 , pp. 1580-1589
    • Takano, H.1    Komuro, I.2    Oka, T.3    Shiojima, I.4
  • 33
    • 33745223285 scopus 로고    scopus 로고
    • Absence of dysferlin alters myogenin expression and delays human muscle differentiation "in vitro
    • de Luna, N., Gallardo, E., Soriano, M., Dominguez-Perles, R. et al., Absence of dysferlin alters myogenin expression and delays human muscle differentiation "in vitro". J. Biol. Chem. 2006, 281, 17092-17098.
    • (2006) J. Biol. Chem , vol.281 , pp. 17092-17098
    • de Luna, N.1    Gallardo, E.2    Soriano, M.3    Dominguez-Perles, R.4
  • 34
    • 34248157682 scopus 로고    scopus 로고
    • The cytoskeleton-associated PDZ-LIM protein, ALP, acts on serum response factor activity to regulate muscle differentiation
    • Pomies, P., Pashmforoush, M., Vegezzi, C., Chien, K. R. et al., The cytoskeleton-associated PDZ-LIM protein, ALP, acts on serum response factor activity to regulate muscle differentiation. Mol. Biol. Cell 2007, 18, 1723-1733.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1723-1733
    • Pomies, P.1    Pashmforoush, M.2    Vegezzi, C.3    Chien, K.R.4
  • 35
    • 27644438336 scopus 로고    scopus 로고
    • Trim32 is a ubiquitin ligase mutated in limb girdle muscular dystrophy type 2H that binds to skeletal muscle myosin and ubiquitinates actin
    • Kudryashova, E., Kudryashov, D., Kramerova, I., Spencer, M. J., Trim32 is a ubiquitin ligase mutated in limb girdle muscular dystrophy type 2H that binds to skeletal muscle myosin and ubiquitinates actin. J. Mol. Biol. 2005, 354, 413-424.
    • (2005) J. Mol. Biol , vol.354 , pp. 413-424
    • Kudryashova, E.1    Kudryashov, D.2    Kramerova, I.3    Spencer, M.J.4
  • 36
    • 0036179479 scopus 로고    scopus 로고
    • Limb-girdle muscular dystrophy type 2H associated with mutation in TRIM32, a putative E3-ubiquitin-ligase gene
    • Frosk, P., Weiler, T., Nylen, E., Sudha, T. et al., Limb-girdle muscular dystrophy type 2H associated with mutation in TRIM32, a putative E3-ubiquitin-ligase gene. Am. J. Hum. Genet. 2002, 70, 663-672.
    • (2002) Am. J. Hum. Genet , vol.70 , pp. 663-672
    • Frosk, P.1    Weiler, T.2    Nylen, E.3    Sudha, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.