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Volumn 1752, Issue 2, 2005, Pages 166-176

Differential expression of the fast skeletal muscle proteome following chronic low-frequency stimulation

Author keywords

Chronic low frequency stimulation; Muscle plasticity; Muscle proteomics; Muscle transformation; Skeletal muscle proteome

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); ALBUMIN; CALSEQUESTRIN; CHAPERONE; CREATINE KINASE; CRYSTALLIN; ENOLASE; FRUCTOSE BISPHOSPHATE ALDOLASE; GLYCOLYTIC ENZYME; HEAT SHOCK PROTEIN; ISOPROTEIN; MUSCLE ENZYME; MUSCLE PROTEIN; MYOGLOBIN; MYOSIN HEAVY CHAIN; MYOSIN LIGHT CHAIN; OXYGEN; PROTEOME; TROPONIN T;

EID: 25144518100     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2005.08.005     Document Type: Article
Times cited : (57)

References (57)
  • 1
    • 0035116376 scopus 로고    scopus 로고
    • Historical perspectives: Plasticity of mammalian skeletal muscle
    • D. Pette Historical perspectives: plasticity of mammalian skeletal muscle J. Appl. Physiol. 90 2001 1119 1124
    • (2001) J. Appl. Physiol. , vol.90 , pp. 1119-1124
    • Pette, D.1
  • 2
    • 0031023872 scopus 로고    scopus 로고
    • Mammalian skeletal muscle fiber type transitions
    • D. Pette, and R.S. Staron Mammalian skeletal muscle fiber type transitions Int. Rev. Cytol. 170 1997 143 223
    • (1997) Int. Rev. Cytol. , vol.170 , pp. 143-223
    • Pette, D.1    Staron, R.S.2
  • 4
    • 0030021957 scopus 로고    scopus 로고
    • Clinical cardiomyoplasty: Review of the 10-year United States experience
    • G.J. Magovern, and K.A. Simpson Clinical cardiomyoplasty: review of the 10-year United States experience Ann. Thorac. Surg. 61 1996 13 409
    • (1996) Ann. Thorac. Surg. , vol.61 , pp. 13-409
    • Magovern, G.J.1    Simpson, K.A.2
  • 5
    • 0036690310 scopus 로고    scopus 로고
    • The adaptive potential of skeletal muscle fibers
    • D. Pette The adaptive potential of skeletal muscle fibers Can. J. Appl. Physiol. 27 2002 423 448
    • (2002) Can. J. Appl. Physiol. , vol.27 , pp. 423-448
    • Pette, D.1
  • 6
    • 0026450106 scopus 로고
    • Adaptation of mammalian skeletal muscle fibers to chronic electrical stimulation
    • D. Pette, and G. Vrbova Adaptation of mammalian skeletal muscle fibers to chronic electrical stimulation Rev. Physiol. Biochem. Pharmacol. 120 1992 115 202
    • (1992) Rev. Physiol. Biochem. Pharmacol. , vol.120 , pp. 115-202
    • Pette, D.1    Vrbova, G.2
  • 7
    • 0030861193 scopus 로고    scopus 로고
    • Early functional and biochemical adaptations to low-frequency stimulation of rabbit fast-twitch muscle
    • A. Hicks, K. Ohlendieck, S.O. Göpel, and D. Pette Early functional and biochemical adaptations to low-frequency stimulation of rabbit fast-twitch muscle Am. J. Physiol., Cell Physiol. 273 1997 C297 C305
    • (1997) Am. J. Physiol., Cell Physiol. , vol.273
    • Hicks, A.1    Ohlendieck, K.2    Göpel, S.O.3    Pette, D.4
  • 8
    • 0034665188 scopus 로고    scopus 로고
    • Myosin isoforms, muscle fiber types, and transitions
    • D. Pette, and R.S. Staron Myosin isoforms, muscle fiber types, and transitions Microsc. Res. Tech. 50 2000 500 509
    • (2000) Microsc. Res. Tech. , vol.50 , pp. 500-509
    • Pette, D.1    Staron, R.S.2
  • 10
    • 0034212222 scopus 로고    scopus 로고
    • 2+-regulatory membrane proteins in fast-twitch, slow-twitch, cardiac, neonatal and chronic low-frequency stimulated muscle fibres
    • 2+- regulatory membrane proteins in fast-twitch, slow-twitch, cardiac, neonatal and chronic low-frequency stimulated muscle fibres Biochim. Biophys. Acta 1466 2000 151 168
    • (2000) Biochim. Biophys. Acta , vol.1466 , pp. 151-168
    • Froemming, G.R.1    Murray, B.E.2    Harmon, S.3    Pette, D.4    Ohlendieck, K.5
  • 11
    • 0025860820 scopus 로고
    • Enzyme activities of fatty acid oxidation and the respiratory chain in chronically stimulated fast-twitch muscle of the rabbit
    • H. Reichmann, R. Wasl, J.A. Simoneau, and D. Pette Enzyme activities of fatty acid oxidation and the respiratory chain in chronically stimulated fast-twitch muscle of the rabbit Pflügers Arch. 418 1991 572 574
    • (1991) Pflügers Arch. , vol.418 , pp. 572-574
    • Reichmann, H.1    Wasl, R.2    Simoneau, J.A.3    Pette, D.4
  • 12
    • 0037427514 scopus 로고    scopus 로고
    • Increased expression of the nicotinic acetylcholine receptor in stimulated muscle
    • C. O'Reilly, D. Pette, and K. Ohlendieck Increased expression of the nicotinic acetylcholine receptor in stimulated muscle Biochem. Biophys. Res. Commun. 300 2003 585 591
    • (2003) Biochem. Biophys. Res. Commun. , vol.300 , pp. 585-591
    • O'Reilly, C.1    Pette, D.2    Ohlendieck, K.3
  • 14
    • 0027258491 scopus 로고
    • Coordinate changes in the expression of troponin subunit and myosin heavy-chain isoforms during fast-to-slow transition of low-frequency-stimulated rabbit muscle
    • T. Leeuw, and D. Pette Coordinate changes in the expression of troponin subunit and myosin heavy-chain isoforms during fast-to-slow transition of low-frequency-stimulated rabbit muscle Eur. J. Biochem. 213 1993 1039 1046
    • (1993) Eur. J. Biochem. , vol.213 , pp. 1039-1046
    • Leeuw, T.1    Pette, D.2
  • 16
    • 0024504584 scopus 로고
    • Electrostimulation-induced increases in fatty acid-binding protein and myoglobin in rat fast-twitch muscle and comparison with tissue levels in heart
    • M. Kaufmann, J.A. Simoneau, J.H. Veerkamp, and D. Pette Electrostimulation-induced increases in fatty acid-binding protein and myoglobin in rat fast-twitch muscle and comparison with tissue levels in heart FEBS Lett. 245 1989 181 184
    • (1989) FEBS Lett. , vol.245 , pp. 181-184
    • Kaufmann, M.1    Simoneau, J.A.2    Veerkamp, J.H.3    Pette, D.4
  • 17
    • 0021837948 scopus 로고
    • Biochemical and ultrastructural changes of skeletal muscle mitochondria after chronic electrical stimulation in rabbits
    • H. Reichmann, H. Hoppeler, O. Mathieu-Costello, F. von Bergen, and D. Pette Biochemical and ultrastructural changes of skeletal muscle mitochondria after chronic electrical stimulation in rabbits Pflügers Arch. 404 1985 1 9
    • (1985) Pflügers Arch. , vol.404 , pp. 1-9
    • Reichmann, H.1    Hoppeler, H.2    Mathieu-Costello, O.3    Von Bergen, F.4    Pette, D.5
  • 18
    • 0037435030 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics
    • R. Aebersold, and M. Mann Mass spectrometry-based proteomics Nature 422 2003 198 207
    • (2003) Nature , vol.422 , pp. 198-207
    • Aebersold, R.1    Mann, M.2
  • 20
    • 0037023852 scopus 로고    scopus 로고
    • Proteomic analysis of striated muscle
    • R.J. Isfort Proteomic analysis of striated muscle J. Chromatogr. B771 2002 155 165
    • (2002) J. Chromatogr. , vol.771 , pp. 155-165
    • Isfort, R.J.1
  • 22
    • 0035294573 scopus 로고    scopus 로고
    • Separation and identification of rat skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry
    • J.X. Yan, R.A. Harry, R. Wait, S.Y. Welson, P.W. Emery, V.R. Preedy, and M.J. Dunn Separation and identification of rat skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry Proteomics 1 2001 424 434
    • (2001) Proteomics , vol.1 , pp. 424-434
    • Yan, J.X.1    Harry, R.A.2    Wait, R.3    Welson, S.Y.4    Emery, P.W.5    Preedy, V.R.6    Dunn, M.J.7
  • 23
    • 3042815335 scopus 로고    scopus 로고
    • Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry
    • C. Cieniewski-Bernard, B. Bastide, T. Lefebvre, J. Lemoine, Y. Mounier, and J.C. Michalski Identification of O-linked N-acetylglucosamine proteins in rat skeletal muscle using two-dimensional gel electrophoresis and mass spectrometry Mol. Cell. Proteomics 3 2004 577 585
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 577-585
    • Cieniewski-Bernard, C.1    Bastide, B.2    Lefebvre, T.3    Lemoine, J.4    Mounier, Y.5    Michalski, J.C.6
  • 24
    • 0242321030 scopus 로고    scopus 로고
    • Proteomic identification of age-dependent protein nitration in rat skeletal muscle
    • J. Kanski, M.A. Alterman, and C. Schöneich Proteomic identification of age-dependent protein nitration in rat skeletal muscle Free Radic. Biol. Med. 35 2003 1229 1239
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 1229-1239
    • Kanski, J.1    Alterman, M.A.2    Schöneich, C.3
  • 27
    • 0142182391 scopus 로고    scopus 로고
    • Proteomic analysis of mdx skeletal muscle: Great reduction of adenylate kinase 1 expression and enzymatic activity
    • Y. Ge, M.P. Molloy, J.S. Chamberlain, and P.C. Andrews Proteomic analysis of mdx skeletal muscle: great reduction of adenylate kinase 1 expression and enzymatic activity Proteomics 3 2003 895 903
    • (2003) Proteomics , vol.3 , pp. 895-903
    • Ge, Y.1    Molloy, M.P.2    Chamberlain, J.S.3    Andrews, P.C.4
  • 28
    • 4444267191 scopus 로고    scopus 로고
    • Differential expression of the skeletal muscle proteome in mdx mice at different ages
    • Y. Ge, M.P. Molloy, J.S. Chamberlain, and P.C. Andrews Differential expression of the skeletal muscle proteome in mdx mice at different ages Electrophoresis 25 2004 2576 2585
    • (2004) Electrophoresis , vol.25 , pp. 2576-2585
    • Ge, Y.1    Molloy, M.P.2    Chamberlain, J.S.3    Andrews, P.C.4
  • 31
    • 0036092560 scopus 로고    scopus 로고
    • Drastic reduction of calsequestrin-like proteins and impaired calcium binding in dystrophic mdx muscle
    • K. Culligan, N. Banville, P. Dowling, and K. Ohlendieck Drastic reduction of calsequestrin-like proteins and impaired calcium binding in dystrophic mdx muscle J. Appl. Physiol. 92 2002 435 445
    • (2002) J. Appl. Physiol. , vol.92 , pp. 435-445
    • Culligan, K.1    Banville, N.2    Dowling, P.3    Ohlendieck, K.4
  • 32
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 33
    • 0030968771 scopus 로고    scopus 로고
    • Cross-linking analysis of the ryanodine receptor and α- dihydropyridine receptor in rabbit skeletal muscle triads
    • B.E. Murray, and K. Ohlendieck Cross-linking analysis of the ryanodine receptor and α-dihydropyridine receptor in rabbit skeletal muscle triads Biochem. J. 324 1997 689 696
    • (1997) Biochem. J. , vol.324 , pp. 689-696
    • Murray, B.E.1    Ohlendieck, K.2
  • 34
    • 0035106676 scopus 로고    scopus 로고
    • Native skeletal muscle dihydropyridine receptor exists as a supramolecular triad complex
    • G.R. Froemming, and K. Ohlendieck Native skeletal muscle dihydropyridine receptor exists as a supramolecular triad complex Cell. Mol. Life Sci. 58 2001 312 320
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 312-320
    • Froemming, G.R.1    Ohlendieck, K.2
  • 35
    • 2342614190 scopus 로고    scopus 로고
    • Drastic reduction of sarcalumenin in Dp427-deficient fibres indicates that abnormal calcium handling plays a key role in muscular dystrophy
    • P. Dowling, P. Doran, and K. Ohlendieck Drastic reduction of sarcalumenin in Dp427-deficient fibres indicates that abnormal calcium handling plays a key role in muscular dystrophy Biochem. J. 379 2004 479 488
    • (2004) Biochem. J. , vol.379 , pp. 479-488
    • Dowling, P.1    Doran, P.2    Ohlendieck, K.3
  • 36
    • 0027350105 scopus 로고
    • Separation and analysis of membrane proteins by SDS-polyacrylamide gel electrophoresis
    • M.J. Dunn, and S.J. Bradd Separation and analysis of membrane proteins by SDS-polyacrylamide gel electrophoresis Methods Mol. Biol. 19 1993 203 210
    • (1993) Methods Mol. Biol. , vol.19 , pp. 203-210
    • Dunn, M.J.1    Bradd, S.J.2
  • 37
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • H. Towbin, T. Staehelin, and J. Gordon Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications Proc. Natl. Acad. Sci. U. S. A. 76 1979 4350 4354
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 38
    • 0027347272 scopus 로고
    • Analysis of membrane proteins by Western blotting and enhanced chemiluminescence
    • S.J. Bradd, and M.J. Dunn Analysis of membrane proteins by Western blotting and enhanced chemiluminescence Methods Mol. Biol. 19 1993 211 218
    • (1993) Methods Mol. Biol. , vol.19 , pp. 211-218
    • Bradd, S.J.1    Dunn, M.J.2
  • 39
    • 3543043510 scopus 로고    scopus 로고
    • Two-dimensional electrophoresis for the isolation of integral membrane proteins and mass spectrometric identification
    • I. Rais, M. Karas, and H. Schagger Two-dimensional electrophoresis for the isolation of integral membrane proteins and mass spectrometric identification Proteomics 4 2004 2567 2571
    • (2004) Proteomics , vol.4 , pp. 2567-2571
    • Rais, I.1    Karas, M.2    Schagger, H.3
  • 42
    • 0022517995 scopus 로고
    • Degeneration-regeneration as a mechanism contributing to the fast to slow conversion of chronically stimulated fast-twitch rabbit muscle
    • A. Maier, B. Gambke, and D. Pette Degeneration-regeneration as a mechanism contributing to the fast to slow conversion of chronically stimulated fast-twitch rabbit muscle Cell Tissue Res. 244 1986 635 643
    • (1986) Cell Tissue Res. , vol.244 , pp. 635-643
    • Maier, A.1    Gambke, B.2    Pette, D.3
  • 45
    • 0023931570 scopus 로고
    • Albumin in rabbit skeletal muscle. Origin, distribution and regulation by contractile activity
    • A. Heilig, and D. Pette Albumin in rabbit skeletal muscle. Origin, distribution and regulation by contractile activity Eur. J. Biochem. 171 1988 503 508
    • (1988) Eur. J. Biochem. , vol.171 , pp. 503-508
    • Heilig, A.1    Pette, D.2
  • 46
    • 0037266936 scopus 로고    scopus 로고
    • Understanding ATP synthesis: Structure and mechanism of the F1-ATPase (Review)
    • J.A. Leyva, M.A. Bianchet, and L.M. Amzel Understanding ATP synthesis: structure and mechanism of the F1-ATPase (Review) Mol. Membr. Biol. 20 2003 27 33
    • (2003) Mol. Membr. Biol. , vol.20 , pp. 27-33
    • Leyva, J.A.1    Bianchet, M.A.2    Amzel, L.M.3
  • 47
    • 0022202081 scopus 로고
    • Increased mitochondrial creatine kinase in chronically stimulated fast-twitch rabbit muscle
    • T. Schmitt, and D. Pette Increased mitochondrial creatine kinase in chronically stimulated fast-twitch rabbit muscle FEBS Lett. 188 1985 341 344
    • (1985) FEBS Lett. , vol.188 , pp. 341-344
    • Schmitt, T.1    Pette, D.2
  • 48
    • 0034652181 scopus 로고    scopus 로고
    • Interactions between beta-enolase and creatine kinase in the cytosol of skeletal muscle cells
    • G. Foucault, M. Vacher, S. Cribier, and M. Arrio-Dupont Interactions between beta-enolase and creatine kinase in the cytosol of skeletal muscle cells Biochem. J. 346 2000 127 131
    • (2000) Biochem. J. , vol.346 , pp. 127-131
    • Foucault, G.1    Vacher, M.2    Cribier, S.3    Arrio-Dupont, M.4
  • 49
    • 0021891892 scopus 로고
    • The creatine-creatine phosphate energy shuttle
    • S.P. Bessman, and C.L. Carpenter The creatine-creatine phosphate energy shuttle Annu. Rev. Biochem. 54 1985 831 862
    • (1985) Annu. Rev. Biochem. , vol.54 , pp. 831-862
    • Bessman, S.P.1    Carpenter, C.L.2
  • 50
    • 0031969846 scopus 로고    scopus 로고
    • Sequential increases in capillarization and mitochondrial enzymes in low-frequency-stimulated rabbit muscle
    • D. Skorjanc, F. Jaschinski, G. Heine, and D. Pette Sequential increases in capillarization and mitochondrial enzymes in low-frequency-stimulated rabbit muscle Am. J. Physiol. 274 1998 C810 C818
    • (1998) Am. J. Physiol. , vol.274
    • Skorjanc, D.1    Jaschinski, F.2    Heine, G.3    Pette, D.4
  • 51
    • 6344277177 scopus 로고    scopus 로고
    • Myoglobin: An essential hemoprotein in striated muscle
    • G.A. Ordway, and D.J. Garry Myoglobin: an essential hemoprotein in striated muscle J. Exp. Biol. 207 2004 3441 3446
    • (2004) J. Exp. Biol. , vol.207 , pp. 3441-3446
    • Ordway, G.A.1    Garry, D.J.2
  • 52
    • 0034527014 scopus 로고    scopus 로고
    • Combining structural genomics and enzymology: Completing the picture in metabolic pathways and enzyme active sites
    • H. Erlandsen, E.E. Abola, and R.C. Stevens Combining structural genomics and enzymology: completing the picture in metabolic pathways and enzyme active sites Curr. Opin. Struct. Biol. 10 2000 719 730
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 719-730
    • Erlandsen, H.1    Abola, E.E.2    Stevens, R.C.3
  • 53
    • 0029161467 scopus 로고
    • Effects of low-frequency stimulation on soluble and structure-bound activities of hexokinase and phosphofructokinase in rat fast-twitch muscle
    • J. Parra, and D. Pette Effects of low-frequency stimulation on soluble and structure-bound activities of hexokinase and phosphofructokinase in rat fast-twitch muscle Biochim. Biophys. Acta 1251 1995 154 160
    • (1995) Biochim. Biophys. Acta , vol.1251 , pp. 154-160
    • Parra, J.1    Pette, D.2
  • 54
    • 0024587141 scopus 로고
    • Electrostimulation-induced fast-to-slow transitions of myosin light and heavy chains in rabbit fast-twitch muscle at the mRNA level
    • B.J. Kirschbaum, A. Heilig, K.T. Härtner, and D. Pette Electrostimulation-induced fast-to-slow transitions of myosin light and heavy chains in rabbit fast-twitch muscle at the mRNA level FEBS Lett. 243 1989 123 126
    • (1989) FEBS Lett. , vol.243 , pp. 123-126
    • Kirschbaum, B.J.1    Heilig, A.2    Härtner, K.T.3    Pette, D.4
  • 55
    • 0036156222 scopus 로고    scopus 로고
    • Protein variants of skeletal muscle regulatory myosin light chain isoforms: Prevalence in mammals, generation and transitions during muscle remodeling
    • B. Gonzalez, P. Negredo, R. Hernando, and R. Manso Protein variants of skeletal muscle regulatory myosin light chain isoforms: prevalence in mammals, generation and transitions during muscle remodeling Pflügers Arch. 443 2002 377 386
    • (2002) Pflügers Arch. , vol.443 , pp. 377-386
    • Gonzalez, B.1    Negredo, P.2    Hernando, R.3    Manso, R.4
  • 56
    • 0031888307 scopus 로고    scopus 로고
    • Transient regulation of c-fos, alpha B-crystallin, and hsp70 in muscle during recovery from contractile activity
    • P.D. Neufer, G.A. Ordway, and R.S. Williams Transient regulation of c-fos, alpha B-crystallin, and hsp70 in muscle during recovery from contractile activity Am. J. Physiol. 274 1998 C341 C346
    • (1998) Am. J. Physiol. , vol.274
    • Neufer, P.D.1    Ordway, G.A.2    Williams, R.S.3
  • 57
    • 0029661431 scopus 로고    scopus 로고
    • Differential expression of B-crystallin and Hsp27 in skeletal muscle during continuous contractile activity. Relationship to myogenic regulatory factors
    • P.D. Neufer, and I.J. Benjamin Differential expression of B-crystallin and Hsp27 in skeletal muscle during continuous contractile activity. Relationship to myogenic regulatory factors J. Biol. Chem. 271 1996 24089 24095
    • (1996) J. Biol. Chem. , vol.271 , pp. 24089-24095
    • Neufer, P.D.1    Benjamin, I.J.2


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