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Volumn 14, Issue 4, 2015, Pages 841-853

Deep proteomics of mouse skeletal muscle enables quantitation of protein isoforms, metabolic pathways, and transcription factors

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); ALPHA ACTIN; CONNECTIN; CREATINE KINASE; FATTY ACID TRANSPORTER; GLUCOSE TRANSPORTER; GLUCOSE TRANSPORTER 1; GLYCOGEN PHOSPHORYLASE; GLYCOGEN SYNTHASE KINASE 3; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; ISOPROTEIN; MYOSIN; NEBULIN; TRANSCRIPTION FACTOR; GLUCOSE; INSULIN; PROTEOME;

EID: 84926454873     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M114.044222     Document Type: Article
Times cited : (226)

References (47)
  • 1
    • 0021994683 scopus 로고
    • Effects of insulin on peripheral and splanchnic glucose metabolism in noninsulin-dependent (type II) diabetes mellitus
    • DeFronzo, R. A., Gunnarsson, R., Bjorkman, O., Olsson, M., and Wahren, J. (1985) Effects of insulin on peripheral and splanchnic glucose metabolism in noninsulin-dependent (type II) diabetes mellitus. J. Clin. Invest. 76, 149-155
    • (1985) J. Clin. Invest. , vol.76 , pp. 149-155
    • DeFronzo, R.A.1    Gunnarsson, R.2    Bjorkman, O.3    Olsson, M.4    Wahren, J.5
  • 2
    • 0034602675 scopus 로고    scopus 로고
    • Exercise-induced changes in expression and activity of proteins involved in insulin signal transduction in skeletal muscle: Differential effects on insulin-receptor substrates 1 and 2
    • Chibalin, A. V., Yu, M., Ryder, J. W., Song, X. M., Galuska, D., Krook, A., Wallberg-Henriksson, H., and Zierath, J. R. (2000) Exercise-induced changes in expression and activity of proteins involved in insulin signal transduction in skeletal muscle: differential effects on insulin-receptor substrates 1 and 2. Proc. Natl. Acad. Sci. U.S.A. 97, 38-43
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 38-43
    • Chibalin, A.V.1    Yu, M.2    Ryder, J.W.3    Song, X.M.4    Galuska, D.5    Krook, A.6    Wallberg-Henriksson, H.7    Zierath, J.R.8
  • 3
    • 0025782887 scopus 로고
    • Molecular and cellular adaptation of muscle in response to exercise: Perspectives of various models
    • Booth, F. W., and Thomason, D. B. (1991) Molecular and cellular adaptation of muscle in response to exercise: perspectives of various models. Physiol. Rev. 71, 541-585
    • (1991) Physiol. Rev. , vol.71 , pp. 541-585
    • Booth, F.W.1    Thomason, D.B.2
  • 4
    • 0036128097 scopus 로고    scopus 로고
    • Adaptations of skeletal muscle to prolonged, intense endurance training
    • Hawley, J. A. (2002) Adaptations of skeletal muscle to prolonged, intense endurance training. Clin. Exp. Pharmacol. Physiol. 29, 218-222
    • (2002) Clin. Exp. Pharmacol. Physiol. , vol.29 , pp. 218-222
    • Hawley, J.A.1
  • 6
    • 84874285042 scopus 로고    scopus 로고
    • Electrophysiology of neuromuscular disorders in critical illness
    • Lacomis, D. (2013) Electrophysiology of neuromuscular disorders in critical illness. Muscle Nerve 47, 452-463
    • (2013) Muscle Nerve , vol.47 , pp. 452-463
    • Lacomis, D.1
  • 9
    • 84870780979 scopus 로고    scopus 로고
    • Mechanisms responsible for disuse muscle atrophy: Potential role of protein provision and exercise as countermeasures
    • Mallinson, J. E., and Murton, A. J. (2013) Mechanisms responsible for disuse muscle atrophy: potential role of protein provision and exercise as countermeasures. Nutrition 29, 22-28
    • (2013) Nutrition , vol.29 , pp. 22-28
    • Mallinson, J.E.1    Murton, A.J.2
  • 10
    • 0028914964 scopus 로고
    • Three muscular dystrophies: Loss of cytoskeleton-extracellular matrix linkage
    • Campbell, K. P. (1995) Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage. Cell 80, 675-679
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 12
    • 33748339008 scopus 로고    scopus 로고
    • Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP
    • Doran, P., Yi, Z., Hwang, H., Bowen, B., Lefort, N., Flynn, C. R., Langlais, P., Weintraub, S. T., and Mandarino, L. J. (2006) Proteome analysis of the dystrophin-deficient MDX diaphragm reveals a drastic increase in the heat shock protein cvHSP. Proteomics 6, 4610-4621
    • (2006) Proteomics , vol.6 , pp. 4610-4621
    • Doran, P.1    Yi, Z.2    Hwang, H.3    Bowen, B.4    Lefort, N.5    Flynn, C.R.6    Langlais, P.7    Weintraub, S.T.8    Mandarino, L.J.9
  • 14
    • 77950795909 scopus 로고    scopus 로고
    • Proteomics of skeletal muscle differentiation, neuromuscular disorders, and fiber aging
    • Ohlendieck, K. (2010) Proteomics of skeletal muscle differentiation, neuromuscular disorders, and fiber aging. Expert Rev. Proteomics 7, 283-296
    • (2010) Expert Rev. Proteomics , vol.7 , pp. 283-296
    • Ohlendieck, K.1
  • 17
    • 84871297843 scopus 로고    scopus 로고
    • Next-generation proteomics: Towards an integrative view of proteome dynamics
    • Altelaar, A. F., Munoz, J., and Heck, A. J. (2013) Next-generation proteomics: towards an integrative view of proteome dynamics. Nat Rev Genet, 14, 35-48
    • (2013) Nat Rev Genet , vol.14 , pp. 35-48
    • Altelaar, A.F.1    Munoz, J.2    Heck, A.J.3
  • 20
    • 78049353457 scopus 로고    scopus 로고
    • Palmitate-induced down-regulation of sortilin and impaired GLUT4 trafficking in C2C12 myotubes
    • Tsuchiya, Y., Hatakeyama, H., Emoto, N., Wagatsuma, F., Matsushita, S., and Kanzaki, M. (2010) Palmitate-induced down-regulation of sortilin and impaired GLUT4 trafficking in C2C12 myotubes. J. Biol. Chem. 285, 34371-34381
    • (2010) J. Biol. Chem. , vol.285 , pp. 34371-34381
    • Tsuchiya, Y.1    Hatakeyama, H.2    Emoto, N.3    Wagatsuma, F.4    Matsushita, S.5    Kanzaki, M.6
  • 21
    • 77956523695 scopus 로고    scopus 로고
    • C2 and C2C12 murine skeletal myoblast models of atrophic and hypertrophic potential: Relevance to disease and aging?
    • Sharples, A. P., Al-Shanti, N., and Stewart, C. E. (2010) C2 and C2C12 murine skeletal myoblast models of atrophic and hypertrophic potential: relevance to disease and aging? J. Cell. Physiol. 225, 240-250
    • (2010) J. Cell. Physiol. , vol.225 , pp. 240-250
    • Sharples, A.P.1    Al-Shanti, N.2    Stewart, C.E.3
  • 22
    • 0032803005 scopus 로고    scopus 로고
    • Overexpression of myotonic dystrophy protein kinase in C2C12 myogenic culture involved in the expression of ferritin heavy chain and interleukin-1alpha mRNAs
    • Watanabe, T., Sasagawa, N., Usuki, F., Koike, H., Saitoh, N., Sorimachi, H., Maruyama, K., Nakase, H., Takagi, A., Ishiura, S., and Suzuki, K. (1999) Overexpression of myotonic dystrophy protein kinase in C2C12 myogenic culture involved in the expression of ferritin heavy chain and interleukin-1alpha mRNAs. J. Neurol. Sci. 167, 26-33
    • (1999) J. Neurol. Sci. , vol.167 , pp. 26-33
    • Watanabe, T.1    Sasagawa, N.2    Usuki, F.3    Koike, H.4    Saitoh, N.5    Sorimachi, H.6    Maruyama, K.7    Nakase, H.8    Takagi, A.9    Ishiura, S.10    Suzuki, K.11
  • 23
    • 67349266694 scopus 로고    scopus 로고
    • Universal sample preparation method for proteome analysis
    • Wisniewski, J. R., Zougman, A., Nagaraj, N., and Mann, M. (2009) Universal sample preparation method for proteome analysis. Nat. Methods 6, 359-362
    • (2009) Nat. Methods , vol.6 , pp. 359-362
    • Wisniewski, J.R.1    Zougman, A.2    Nagaraj, N.3    Mann, M.4
  • 24
    • 57649187385 scopus 로고    scopus 로고
    • Peptide separation with immobilized pI strips is an attractive alternative to in-gel protein digestion for proteome analysis
    • Hubner, N. C., S. Ren, and M. Mann (2008) Peptide separation with immobilized pI strips is an attractive alternative to in-gel protein digestion for proteome analysis. Proteomics 8, 4862-4872
    • (2008) Proteomics , vol.8 , pp. 4862-4872
    • Hubner, N.C.1    Ren, S.2    Mann, M.3
  • 26
    • 57449099865 scopus 로고    scopus 로고
    • MaxQuant enables high peptide identification rates, individualized p. p. b.-range mass accuracies and proteome-wide protein quantification
    • Cox, J., and Mann, M. (2008) MaxQuant enables high peptide identification rates, individualized p. p. b.-range mass accuracies and proteome-wide protein quantification. Nat. Biotechnol. 26, 1367-1372
    • (2008) Nat. Biotechnol. , vol.26 , pp. 1367-1372
    • Cox, J.1    Mann, M.2
  • 28
    • 84907197082 scopus 로고    scopus 로고
    • MaxLFQ allows accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction
    • Cox, J., Hein, M. Y., Luber, C. A., Paron, I., Nagaraj, N., and Mann, M. (2014) MaxLFQ allows accurate proteome-wide label-free quantification by delayed normalization and maximal peptide ratio extraction. Mol. Cell. Proteomics 13, 2513-2526
    • (2014) Mol. Cell. Proteomics , vol.13 , pp. 2513-2526
    • Cox, J.1    Hein, M.Y.2    Luber, C.A.3    Paron, I.4    Nagaraj, N.5    Mann, M.6
  • 29
    • 84873508256 scopus 로고    scopus 로고
    • 1D and 2D annotation enrichment: A statistical method integrating quantitative proteomics with complementary high-throughput data
    • Cox, J., and Mann, M. (2012) 1D and 2D annotation enrichment: a statistical method integrating quantitative proteomics with complementary high-throughput data. BMC Bioinformatics 13, S12
    • (2012) BMC Bioinformatics , vol.13 , pp. S12
    • Cox, J.1    Mann, M.2
  • 30
    • 84872685287 scopus 로고    scopus 로고
    • Extensive quantitative remodeling of the proteome between normal colon tissue and adenocarcinoma
    • Wisniewski, J. R., Ostasiewicz, P., Dus, K., Zielinska, D. F., Gnad, F., and Mann, M. (2012) Extensive quantitative remodeling of the proteome between normal colon tissue and adenocarcinoma. Mol. Syst. Biol. 8, 611
    • (2012) Mol. Syst. Biol. , vol.8 , pp. 611
    • Wisniewski, J.R.1    Ostasiewicz, P.2    Dus, K.3    Zielinska, D.F.4    Gnad, F.5    Mann, M.6
  • 31
    • 84857938446 scopus 로고    scopus 로고
    • Comparative proteomic analysis of eleven common cell lines reveals ubiquitous but varying expression of most proteins
    • M111 014050
    • Geiger, T., Wehner, A., Schaab, C., Cox, J., and Mann, M. (2012) Comparative proteomic analysis of eleven common cell lines reveals ubiquitous but varying expression of most proteins. Mol. Cell. Proteomics, 11, M111 014050
    • (2012) Mol. Cell. Proteomics , vol.11
    • Geiger, T.1    Wehner, A.2    Schaab, C.3    Cox, J.4    Mann, M.5
  • 32
    • 84857980282 scopus 로고    scopus 로고
    • Analysis of high accuracy, quantitative proteomics data in the MaxQB database
    • M111 014068
    • Schaab, C., Geiger, T., Stoehr, G., Cox, J., and Mann, M. (2012) Analysis of high accuracy, quantitative proteomics data in the MaxQB database. Mol. Cell. Proteomics 11, M111 014068
    • (2012) Mol. Cell. Proteomics , vol.11
    • Schaab, C.1    Geiger, T.2    Stoehr, G.3    Cox, J.4    Mann, M.5
  • 33
    • 50049121953 scopus 로고    scopus 로고
    • Exercise-induced phospho-proteins in skeletal muscle
    • Deshmukh, A. S., Hawley, J. A., and Zierath, J. R. (2008) Exercise-induced phospho-proteins in skeletal muscle. Int. J. Obes. 32, S18-S23
    • (2008) Int. J. Obes. , vol.32 , pp. S18-S23
    • Deshmukh, A.S.1    Hawley, J.A.2    Zierath, J.R.3
  • 34
    • 0032555928 scopus 로고    scopus 로고
    • Analysis of GLUT4 distribution in whole skeletal muscle fibers: Identification of distinct storage compartments that are recruited by insulin and muscle contractions
    • Ploug, T., van Deurs, B., Ai, H., Cushman, S. W., and Ralston, E. (1998) Analysis of GLUT4 distribution in whole skeletal muscle fibers: identification of distinct storage compartments that are recruited by insulin and muscle contractions. J. Cell Biol. 142, 1429-1446
    • (1998) J. Cell Biol. , vol.142 , pp. 1429-1446
    • Ploug, T.1    Van Deurs, B.2    Ai, H.3    Cushman, S.W.4    Ralston, E.5
  • 35
    • 84873378527 scopus 로고    scopus 로고
    • Exercise metabolism and the molecular regulation of skeletal muscle adaptation
    • Egan, B., and Zierath, J. R. (2013) Exercise metabolism and the molecular regulation of skeletal muscle adaptation. Cell Metab. 17, 162-184
    • (2013) Cell Metab. , vol.17 , pp. 162-184
    • Egan, B.1    Zierath, J.R.2
  • 38
    • 50349099779 scopus 로고    scopus 로고
    • Emerging role for AS160/TBC1D4 and TBC1D1 in the regulation of GLUT4 traffic
    • Sakamoto, K., and Holman, G. D. (2008) Emerging role for AS160/TBC1D4 and TBC1D1 in the regulation of GLUT4 traffic. Am. J. Physiol. Endocrinol. Metab. 295, E29-E37
    • (2008) Am. J. Physiol. Endocrinol. Metab. , vol.295 , pp. E29-E37
    • Sakamoto, K.1    Holman, G.D.2
  • 39
    • 33745815985 scopus 로고    scopus 로고
    • AMP-activated protein kinase signaling in metabolic regulation
    • Long, Y. C., and Zierath, J. R. (2006) AMP-activated protein kinase signaling in metabolic regulation. J. Clin. Invest. 116, 1776-1783
    • (2006) J. Clin. Invest. , vol.116 , pp. 1776-1783
    • Long, Y.C.1    Zierath, J.R.2
  • 40
    • 70349921265 scopus 로고    scopus 로고
    • A-769662 activates AMPK beta1-containing complexes but induces glucose uptake through a PI3-kinase-dependent pathway in mouse skeletal muscle
    • Treebak, J. T., Birk, J. B., Hansen, B. F., Olsen, G. S., and Wojtaszewski, J. F. (2009) A-769662 activates AMPK beta1-containing complexes but induces glucose uptake through a PI3-kinase-dependent pathway in mouse skeletal muscle. Am. J. Physiol. Cell Physiol. 297, C1041-C1052
    • (2009) Am. J. Physiol. Cell Physiol. , vol.297 , pp. C1041-C1052
    • Treebak, J.T.1    Birk, J.B.2    Hansen, B.F.3    Olsen, G.S.4    Wojtaszewski, J.F.5
  • 41
    • 23044432463 scopus 로고    scopus 로고
    • Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase
    • Hawley, S. A., Pan, D. A., Mustard, K. J., Ross, L., Bain, J., Edelman, A. M., Frenguelli, B. G., and Hardie, D. G. (2005) Calmodulin-dependent protein kinase kinase-beta is an alternative upstream kinase for AMP-activated protein kinase. Cell Metab. 2, 9-19
    • (2005) Cell Metab. , vol.2 , pp. 9-19
    • Hawley, S.A.1    Pan, D.A.2    Mustard, K.J.3    Ross, L.4    Bain, J.5    Edelman, A.M.6    Frenguelli, B.G.7    Hardie, D.G.8
  • 42
    • 33745668478 scopus 로고    scopus 로고
    • siRNA-based gene silencing reveals specialized roles of IRS-1/Akt2 and IRS-2/Akt1 in glucose and lipid metabolism in human skeletal muscle
    • Bouzakri, K., Zachrisson, A., Al-Khalili, L., Zhang, B. B., Koistinen, H. A., Krook, A., and Zierath, J. R. (2006) siRNA-based gene silencing reveals specialized roles of IRS-1/Akt2 and IRS-2/Akt1 in glucose and lipid metabolism in human skeletal muscle. Cell Metab. 4, 89-96
    • (2006) Cell Metab. , vol.4 , pp. 89-96
    • Bouzakri, K.1    Zachrisson, A.2    Al-Khalili, L.3    Zhang, B.B.4    Koistinen, H.A.5    Krook, A.6    Zierath, J.R.7
  • 44
    • 84895538371 scopus 로고    scopus 로고
    • Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells
    • Kulak, N. A., Pichler, G., Paron, I., Nagaraj, N., and Mann, M. (2014) Minimal, encapsulated proteomic-sample processing applied to copy-number estimation in eukaryotic cells. Nat. Methods 11, 319-324
    • (2014) Nat. Methods , vol.11 , pp. 319-324
    • Kulak, N.A.1    Pichler, G.2    Paron, I.3    Nagaraj, N.4    Mann, M.5
  • 45
    • 33845332346 scopus 로고    scopus 로고
    • Predominant alpha2/beta2/gamma3 AMPK activation during exercise in human skeletal muscle
    • Birk, J. B., and Wojtaszewski, J. F. (2006) Predominant alpha2/beta2/gamma3 AMPK activation during exercise in human skeletal muscle. J. Physiol. 577, 1021-1032
    • (2006) J. Physiol. , vol.577 , pp. 1021-1032
    • Birk, J.B.1    Wojtaszewski, J.F.2
  • 46
    • 33947173689 scopus 로고    scopus 로고
    • AS160 phosphorylation is associated with activation of alpha2beta2gamma1- But not alpha2beta2gamma3-AMPK trimeric complex in skeletal muscle during exercise in humans
    • Treebak, J. T., Birk, J. B., Rose, A. J., Kiens, B., Richter, E. A., and Wojtaszewski, J. F. (2007) AS160 phosphorylation is associated with activation of alpha2beta2gamma1- but not alpha2beta2gamma3-AMPK trimeric complex in skeletal muscle during exercise in humans. Am. J. Physiol. Endocrinol. Metab. 292, E715-E722
    • (2007) Am. J. Physiol. Endocrinol. Metab. , vol.292 , pp. E715-E722
    • Treebak, J.T.1    Birk, J.B.2    Rose, A.J.3    Kiens, B.4    Richter, E.A.5    Wojtaszewski, J.F.6
  • 47
    • 0035746163 scopus 로고    scopus 로고
    • Limits to sustainable muscle performance: Interaction between glycolysis and oxidative phosphorylation
    • Conley, K. E., Kemper, W. F., and Crowther, G. J. (2001) Limits to sustainable muscle performance: interaction between glycolysis and oxidative phosphorylation. J. Exp. Biol. 204, 3189-3194
    • (2001) J. Exp. Biol. , vol.204 , pp. 3189-3194
    • Conley, K.E.1    Kemper, W.F.2    Crowther, G.J.3


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