메뉴 건너뛰기




Volumn 22, Issue 2, 2012, Pages 207-216

Proteomic analysis of rat skeletal muscle submitted to one bout of incremental exercise

Author keywords

Exercise; Mass spectrometry; Skeletal muscle; Two dimensional electrophoresis

Indexed keywords

MUSCLE PROTEIN; PROTEOME;

EID: 84858266421     PISSN: 09057188     EISSN: 16000838     Source Type: Journal    
DOI: 10.1111/j.1600-0838.2010.01235.x     Document Type: Article
Times cited : (11)

References (63)
  • 1
    • 0026348925 scopus 로고
    • A two-dimensional gel database of rat liver proteins useful in gene regulation and drug effects studies
    • Anderson NL, Esquer-Blasco R, Hofmann JP, Anderson NG.A two-dimensional gel database of rat liver proteins useful in gene regulation and drug effects studies. Electrophoresis 1991: 12: 907-930.
    • (1991) Electrophoresis , vol.12 , pp. 907-930
    • Anderson, N.L.1    Esquer-Blasco, R.2    Hofmann, J.P.3    Anderson, N.G.4
  • 2
    • 34548366259 scopus 로고    scopus 로고
    • Resistance exercise, muscle loading/unloading and the control of muscle mass
    • Baar K, Nader G, Bodine S. Resistance exercise, muscle loading/unloading and the control of muscle mass. Essays Biochem 2006: 42: 61-74.
    • (2006) Essays Biochem , vol.42 , pp. 61-74
    • Baar, K.1    Nader, G.2    Bodine, S.3
  • 3
    • 48849097164 scopus 로고    scopus 로고
    • Quantitative proteomics as a new piece of the systems biology puzzle
    • Bachi A, Bonaldi T. Quantitative proteomics as a new piece of the systems biology puzzle. J Proteomics 2008: 71: 357-367.
    • (2008) J Proteomics , vol.71 , pp. 357-367
    • Bachi, A.1    Bonaldi, T.2
  • 4
    • 0033983159 scopus 로고    scopus 로고
    • Research in the exercise sciences
    • J Appl Physiol
    • Baldwin KM. Research in the exercise sciences: where do we go from here? J Appl Physiol 2000: 88: 332-336.
    • (2000) where do we go from here? , vol.88 , pp. 332-336
    • Baldwin, K.M.1
  • 5
    • 58349091041 scopus 로고    scopus 로고
    • Chronic endurance exercise induces quadriceps nitrosative stress in patients with severe COPD
    • Barreiro E, Rabinovich R, Marin-Corral J, Barbera JA, Gea J, Roca J. Chronic endurance exercise induces quadriceps nitrosative stress in patients with severe COPD. Thorax 2009: 64: 13-19.
    • (2009) Thorax , vol.64 , pp. 13-19
    • Barreiro, E.1    Rabinovich, R.2    Marin-Corral, J.3    Barbera, J.A.4    Gea, J.5    Roca, J.6
  • 7
    • 2942529230 scopus 로고    scopus 로고
    • Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry
    • Bouley J, Chambon C, Picard B. Mapping of bovine skeletal muscle proteins using two-dimensional gel electrophoresis and mass spectrometry. Proteomics 2004: 4: 1811-1824.
    • (2004) Proteomics , vol.4 , pp. 1811-1824
    • Bouley, J.1    Chambon, C.2    Picard, B.3
  • 9
    • 52449135519 scopus 로고    scopus 로고
    • Changes in the rat skeletal muscle proteome induced by moderate-intensity endurance exercise
    • Burniston JG. Changes in the rat skeletal muscle proteome induced by moderate-intensity endurance exercise. Biochim Biophys Acta 2008: 1784: 1077-1086.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1077-1086
    • Burniston, J.G.1
  • 10
    • 33846968823 scopus 로고    scopus 로고
    • Anabolic effects of a non-myotoxic dose of the beta2-adrenergic receptor agonist clenbuterol on rat plantaris muscle
    • Burniston JG, McLean L, Beynon RJ, Goldspink DF. Anabolic effects of a non-myotoxic dose of the beta2-adrenergic receptor agonist clenbuterol on rat plantaris muscle. Muscle Nerve 2007: 35: 217-223.
    • (2007) Muscle Nerve , vol.35 , pp. 217-223
    • Burniston, J.G.1    McLean, L.2    Beynon, R.J.3    Goldspink, D.F.4
  • 12
    • 0025262319 scopus 로고
    • Radioisotopic assays of CoASH and carnitine and their acetylated forms in human skeletal muscle
    • Cederblad G, Carlin JI, Constantin-Teodosiu D, Harper P, Hultman E. Radioisotopic assays of CoASH and carnitine and their acetylated forms in human skeletal muscle. Anal Biochem 1990: 185: 274-278.
    • (1990) Anal Biochem , vol.185 , pp. 274-278
    • Cederblad, G.1    Carlin, J.I.2    Constantin-Teodosiu, D.3    Harper, P.4    Hultman, E.5
  • 15
    • 31944446983 scopus 로고    scopus 로고
    • The glycolytic enzymes, glyceraldehyde-3-phosphate dehydrogenase, triose-phosphate isomerase, and pyruvate kinase are components of the K(ATP) channel macromolecular complex and regulate its function
    • Dhar-Chowdhury P, Harrell MD, Han SY, Jankowska D, Parachuru L, Morrissey A, Srivastava S, Liu W, Malester B, Yoshida H, Coetzee WA. The glycolytic enzymes, glyceraldehyde-3-phosphate dehydrogenase, triose-phosphate isomerase, and pyruvate kinase are components of the K(ATP) channel macromolecular complex and regulate its function. J Biol Chem 2005: 280: 38464-38470.
    • (2005) J Biol Chem , vol.280 , pp. 38464-38470
    • Dhar-Chowdhury, P.1    Harrell, M.D.2    Han, S.Y.3    Jankowska, D.4    Parachuru, L.5    Morrissey, A.6    Srivastava, S.7    Liu, W.8    Malester, B.9    Yoshida, H.10    Coetzee, W.A.11
  • 16
    • 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
  • 17
    • 66149097065 scopus 로고    scopus 로고
    • Nutritional and contractile regulation of human skeletal muscle protein synthesis and mTORC1 signaling
    • Drummond MJ, Dreyer HC, Fry CS, Glynn EL, Rasmussen BB. Nutritional and contractile regulation of human skeletal muscle protein synthesis and mTORC1 signaling. J Appl Physiol 2009: 106: 1374-1384.
    • (2009) J Appl Physiol , vol.106 , pp. 1374-1384
    • Drummond, M.J.1    Dreyer, H.C.2    Fry, C.S.3    Glynn, E.L.4    Rasmussen, B.B.5
  • 18
    • 33745528140 scopus 로고    scopus 로고
    • Proteomic analysis of altered protein expression in skeletal muscle of rats in a hypermetabolic state induced by burn sepsis
    • Duan X, Berthiaume F, Yarmush D, Yarmush ML. Proteomic analysis of altered protein expression in skeletal muscle of rats in a hypermetabolic state induced by burn sepsis. Biochem J 2006: 397: 149-158.
    • (2006) Biochem J , vol.397 , pp. 149-158
    • Duan, X.1    Berthiaume, F.2    Yarmush, D.3    Yarmush, M.L.4
  • 19
    • 33746012931 scopus 로고    scopus 로고
    • Functional, structural and molecular plasticity of mammalian skeletal muscle in response to exercise stimuli
    • Fluck M. Functional, structural and molecular plasticity of mammalian skeletal muscle in response to exercise stimuli. J Exp Biol 2006: 209: 2239-2248.
    • (2006) J Exp Biol , vol.209 , pp. 2239-2248
    • Fluck, M.1
  • 22
    • 33748888361 scopus 로고    scopus 로고
    • A proteomic analysis of the acute effects of high-intensity exercise on skeletal muscle proteins in fasted rats
    • Guelfi KJ, Casey TM, Giles JJ, Fournier PA, Arthur PG.A proteomic analysis of the acute effects of high-intensity exercise on skeletal muscle proteins in fasted rats. Clin Exp Pharmacol Physiol 2006: 33: 952-957.
    • (2006) Clin Exp Pharmacol Physiol , vol.33 , pp. 952-957
    • Guelfi, K.J.1    Casey, T.M.2    Giles, J.J.3    Fournier, P.A.4    Arthur, P.G.5
  • 23
    • 38049144357 scopus 로고    scopus 로고
    • Pyruvate dehydrogenase complex deficiency caused by ubiquitination and proteasome-mediated degradation of the E1 subunit
    • Han Z, Zhong L, Srivastava A, Stacpoole PW. Pyruvate dehydrogenase complex deficiency caused by ubiquitination and proteasome-mediated degradation of the E1 subunit. J Biol Chem 2008: 283: 237-243.
    • (2008) J Biol Chem , vol.283 , pp. 237-243
    • Han, Z.1    Zhong, L.2    Srivastava, A.3    Stacpoole, P.W.4
  • 24
    • 34250822402 scopus 로고    scopus 로고
    • Antioxidant supplementation enhances the exercise-induced increase in mitochondrial uncoupling protein 3 and endothelial nitric oxide synthase mRNA content in human skeletal muscle
    • Hellsten Y, Nielsen JJ, Lykkesfeldt J, Bruhn M, Silveira L, Pilegaard H, Bangsbo J. Antioxidant supplementation enhances the exercise-induced increase in mitochondrial uncoupling protein 3 and endothelial nitric oxide synthase mRNA content in human skeletal muscle. Free Radic Biol Med 2007: 43: 353-361.
    • (2007) Free Radic Biol Med , vol.43 , pp. 353-361
    • Hellsten, Y.1    Nielsen, J.J.2    Lykkesfeldt, J.3    Bruhn, M.4    Silveira, L.5    Pilegaard, H.6    Bangsbo, J.7
  • 29
    • 33746009957 scopus 로고    scopus 로고
    • Coordination of metabolic plasticity in skeletal muscle
    • Hood DA, Irrcher I, Ljubicic V, Joseph AM. Coordination of metabolic plasticity in skeletal muscle. J Exp Biol 2006: 209: 2265-2275.
    • (2006) J Exp Biol , vol.209 , pp. 2265-2275
    • Hood, D.A.1    Irrcher, I.2    Ljubicic, V.3    Joseph, A.M.4
  • 30
    • 66149107037 scopus 로고    scopus 로고
    • Coingestion of protein with carbohydrate during recovery from endurance exercise stimulates skeletal muscle protein synthesis in humans
    • Howarth KR, Moreau NA, Phillips SM, Gibala MJ. Coingestion of protein with carbohydrate during recovery from endurance exercise stimulates skeletal muscle protein synthesis in humans. J Appl Physiol 2009: 106: 1394-1402.
    • (2009) J Appl Physiol , vol.106 , pp. 1394-1402
    • Howarth, K.R.1    Moreau, N.A.2    Phillips, S.M.3    Gibala, M.J.4
  • 31
    • 0037108887 scopus 로고    scopus 로고
    • Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search
    • Keller A, Nesvizhskii AI, Kolker E, Aebersold R. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal Chem 2002: 74: 5383-5392.
    • (2002) Anal Chem , vol.74 , pp. 5383-5392
    • Keller, A.1    Nesvizhskii, A.I.2    Kolker, E.3    Aebersold, R.4
  • 32
    • 0034717940 scopus 로고    scopus 로고
    • Fatty acid import into mitochondria
    • Kerner J, Hoppel C. Fatty acid import into mitochondria. Biochim Biophys Acta 2000: 1486: 1-17.
    • (2000) Biochim Biophys Acta , vol.1486 , pp. 1-17
    • Kerner, J.1    Hoppel, C.2
  • 34
    • 14744284637 scopus 로고    scopus 로고
    • Multifaceted roles of glycolytic enzymes
    • Kim JW, Dang CV. Multifaceted roles of glycolytic enzymes. Trends Biochem Sci 2005: 30: 142-150.
    • (2005) Trends Biochem Sci , vol.30 , pp. 142-150
    • Kim, J.W.1    Dang, C.V.2
  • 35
    • 66149154785 scopus 로고    scopus 로고
    • Human muscle protein synthesis and breakdown during and after exercise
    • Kumar V, Atherton P, Smith K, Rennie MJ. Human muscle protein synthesis and breakdown during and after exercise. J Appl Physiol 2009: 106: 2026-2039.
    • (2009) J Appl Physiol , vol.106 , pp. 2026-2039
    • Kumar, V.1    Atherton, P.2    Smith, K.3    Rennie, M.J.4
  • 36
    • 0028253627 scopus 로고
    • Branched-chain amino acids augment ammonia metabolism while attenuating protein breakdown during exercise
    • MacLean DA, Graham TE, Saltin B. Branched-chain amino acids augment ammonia metabolism while attenuating protein breakdown during exercise. Am J Physiol 1994: 267: E1010-E1022.
    • (1994) Am J Physiol , vol.267
    • MacLean, D.A.1    Graham, T.E.2    Saltin, B.3
  • 37
    • 43149088019 scopus 로고    scopus 로고
    • Inducible heat shock protein 70 and its role in preconditioning and exercise
    • Madden LA, Sandstrom ME, Lovell RJ, McNaughton L. Inducible heat shock protein 70 and its role in preconditioning and exercise. Amino Acids 2008: 34: 511-516.
    • (2008) Amino Acids , vol.34 , pp. 511-516
    • Madden, L.A.1    Sandstrom, M.E.2    Lovell, R.J.3    McNaughton, L.4
  • 38
    • 24644478044 scopus 로고    scopus 로고
    • Analysis of global mRNA expression in human skeletal muscle during recovery from endurance exercise
    • Mahoney DJ, Parise G, Melov S, Safdar A, Tarnopolsky MA. Analysis of global mRNA expression in human skeletal muscle during recovery from endurance exercise. FASEB J 2005: 19: 1498-1500.
    • (2005) FASEB J , vol.19 , pp. 1498-1500
    • Mahoney, D.J.1    Parise, G.2    Melov, S.3    Safdar, A.4    Tarnopolsky, M.A.5
  • 42
    • 67651120134 scopus 로고    scopus 로고
    • The exercise-induced stress response of skeletal muscle, with specific emphasis on humans
    • Morton JP, Kayani AC, McArdle A, Drust B. The exercise-induced stress response of skeletal muscle, with specific emphasis on humans. Sports Med 2009: 39: 643-662.
    • (2009) Sports Med , vol.39 , pp. 643-662
    • Morton, J.P.1    Kayani, A.C.2    McArdle, A.3    Drust, B.4
  • 44
    • 0042338362 scopus 로고    scopus 로고
    • A statistical model for identifying proteins by tandem mass spectrometry
    • Nesvizhskii AI, Keller A, Kolker E, Aebersold R.A statistical model for identifying proteins by tandem mass spectrometry. Anal Chem 2003: 75: 4646-4658.
    • (2003) Anal Chem , vol.75 , pp. 4646-4658
    • Nesvizhskii, A.I.1    Keller, A.2    Kolker, E.3    Aebersold, R.4
  • 46
    • 0034786119 scopus 로고    scopus 로고
    • An evaluation of the use of two-dimensional gel electrophoresis in proteomics
    • Ong SE, Pandey A. An evaluation of the use of two-dimensional gel electrophoresis in proteomics. Biomol Eng 2001: 18: 195-205.
    • (2001) Biomol Eng , vol.18 , pp. 195-205
    • Ong, S.E.1    Pandey, A.2
  • 47
    • 12944269065 scopus 로고
    • Rapid identification of proteins by peptide-mass fingerprinting
    • Pappin DJ, Hojrup P, Bleasby AJ. Rapid identification of proteins by peptide-mass fingerprinting. Curr Biol 1993: 3: 327-332.
    • (1993) Curr Biol , vol.3 , pp. 327-332
    • Pappin, D.J.1    Hojrup, P.2    Bleasby, A.J.3
  • 48
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins DN, Pappin DJ, Creasy DM, Cottrell JS. Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 1999: 20: 3551-3567.
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 51
    • 63649123163 scopus 로고    scopus 로고
    • Turning down lipid oxidation during heavy exercise-what is the mechanism?
    • Sahlin K, Sallstedt EK, Bishop D, Tonkonogi M. Turning down lipid oxidation during heavy exercise-what is the mechanism?J Physiol Pharmacol 2008: 59(Suppl. 7): 19-30.
    • (2008) J Physiol Pharmacol , vol.59 , Issue.SUPPL. 7 , pp. 19-30
    • Sahlin, K.1    Sallstedt, E.K.2    Bishop, D.3    Tonkonogi, M.4
  • 52
    • 29944442461 scopus 로고    scopus 로고
    • Endurance training modulates the muscular transcriptome response to acute exercise
    • Schmutz S, Dapp C, Wittwer M, Vogt M, Hoppeler H, Fluck M. Endurance training modulates the muscular transcriptome response to acute exercise. Pflugers Arch 2006: 451: 678-687.
    • (2006) Pflugers Arch , vol.451 , pp. 678-687
    • Schmutz, S.1    Dapp, C.2    Wittwer, M.3    Vogt, M.4    Hoppeler, H.5    Fluck, M.6
  • 53
    • 33746302310 scopus 로고    scopus 로고
    • Universal metrics for quality assessment of protein identifications by mass spectrometry
    • Stead DA, Preece A, Brown AJ. Universal metrics for quality assessment of protein identifications by mass spectrometry. Mol Cell Proteom 2006: 5: 1205-1211.
    • (2006) Mol Cell Proteom , vol.5 , pp. 1205-1211
    • Stead, D.A.1    Preece, A.2    Brown, A.J.3
  • 55
    • 0035942271 scopus 로고    scopus 로고
    • Significance analysis of microarrays applied to the ionizing radiation response
    • Tusher VG, Tibshirani R, Chu G. Significance analysis of microarrays applied to the ionizing radiation response. Proc Natl Acad Sci USA 2001: 98: 5116-5121.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5116-5121
    • Tusher, V.G.1    Tibshirani, R.2    Chu, G.3
  • 56
    • 0032729732 scopus 로고    scopus 로고
    • Muscle protein degradation and amino acid metabolism during prolonged knee-extensor exercise in humans
    • Van Hall G, Saltin B, Wagenmakers AJ. Muscle protein degradation and amino acid metabolism during prolonged knee-extensor exercise in humans. Clin Sci (London) 1999: 97: 557-567.
    • (1999) Clin Sci (London) , vol.97 , pp. 557-567
    • Van Hall, G.1    Saltin, B.2    Wagenmakers, A.J.3
  • 57
    • 34548356702 scopus 로고    scopus 로고
    • Applications and current challenges of proteomic approaches, focusing on two-dimensional electrophoresis
    • Vercauteren FG, Arckens L, Quirion R. Applications and current challenges of proteomic approaches, focusing on two-dimensional electrophoresis. Amino Acids 2007: 33: 405-414.
    • (2007) Amino Acids , vol.33 , pp. 405-414
    • Vercauteren, F.G.1    Arckens, L.2    Quirion, R.3
  • 60
    • 38349178982 scopus 로고    scopus 로고
    • Sensitive, quantitative, and fast modifications for Coomassie Blue staining of polyacrylamide gels
    • Westermeier R. Sensitive, quantitative, and fast modifications for Coomassie Blue staining of polyacrylamide gels. Proteomics 2006: 6(Suppl. 2): 61-64.
    • (2006) Proteomics , vol.6 , Issue.SUPPL. 2 , pp. 61-64
    • Westermeier, R.1
  • 61
    • 48549107440 scopus 로고    scopus 로고
    • Differential effects of resistance and endurance exercise in the fed state on signalling molecule phosphorylation and protein synthesis in human muscle
    • Wilkinson SB, Phillips SM, Atherton PJ, Patel R, Yarasheski KE, Tarnopolsky MA, Rennie MJ. Differential effects of resistance and endurance exercise in the fed state on signalling molecule phosphorylation and protein synthesis in human muscle. J Physiol 2008: 586: 3701-3717.
    • (2008) J Physiol , vol.586 , pp. 3701-3717
    • Wilkinson, S.B.1    Phillips, S.M.2    Atherton, P.J.3    Patel, R.4    Yarasheski, K.E.5    Tarnopolsky, M.A.6    Rennie, M.J.7
  • 62
    • 0030026070 scopus 로고    scopus 로고
    • Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
    • Wilm M, Shevchenko A, Houthaeve T, Breit S, Schweigerer L, Fotsis T, Mann M. Femtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry. Nature 1996: 379: 466-469.
    • (1996) Nature , vol.379 , pp. 466-469
    • Wilm, M.1    Shevchenko, A.2    Houthaeve, T.3    Breit, S.4    Schweigerer, L.5    Fotsis, T.6    Mann, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.