메뉴 건너뛰기




Volumn 197, Issue 2, 2009, Pages 151-159

The adaptive responses in several mediators linked with hypertrophy and atrophy of skeletal muscle after lower limb unloading in humans

Author keywords

Foxo; Human; P Akt; Skeletal muscle; Suspension

Indexed keywords

ATROGIN 1; BETA ACTIN; FOLLISTATIN RELATED PROTEIN; MESSENGER RNA; MYOSTATIN; PROTEIN KINASE B; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; SERUM RESPONSE FACTOR; SMAD2 PROTEIN; SMAD3 PROTEIN; TRANSCRIPTION FACTOR FKHR; TRANSCRIPTION FACTOR FKHRL1;

EID: 69949135816     PISSN: 17481708     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1748-1716.2009.01995.x     Document Type: Article
Times cited : (44)

References (47)
  • 1
    • 0027970860 scopus 로고
    • Effect of short-term unweighting on human skeletal muscle strength and size
    • Adams, G., Hather, B.M. Dudley, G.A. 1994. Effect of short-term unweighting on human skeletal muscle strength and size. Aviat Space Environ Med 65, 1116 1121.
    • (1994) Aviat Space Environ Med , vol.65 , pp. 1116-1121
    • Adams, G.1    Hather, B.M.2    Dudley, G.A.3
  • 2
    • 0344845330 scopus 로고    scopus 로고
    • Skeletal muscle unweighting: Spaceflight and ground-based models
    • Adams, G.R., Caiozzo, V.J. Baldwin, K.M. 2003. Skeletal muscle unweighting: spaceflight and ground-based models. J Appl Physiol 95, 2185 2201.
    • (2003) J Appl Physiol , vol.95 , pp. 2185-2201
    • Adams, G.R.1    Caiozzo, V.J.2    Baldwin, K.M.3
  • 6
    • 0033963218 scopus 로고    scopus 로고
    • Integrin signaling's potential for mediating gene expression in hypertrophying skeletal muscle
    • Carson, J.A. Wei, L. 2000. Integrin signaling's potential for mediating gene expression in hypertrophying skeletal muscle. J Appl Physiol 88, 337 343.
    • (2000) J Appl Physiol , vol.88 , pp. 337-343
    • Carson, J.A.1    Wei, L.2
  • 8
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival; A play in three Akts
    • Datta, S.R., Brunet, A. Greenberg, M.E. 1999. Cellular survival; a play in three Akts. Genes Dev 13, 2905 2927.
    • (1999) Genes Dev , vol.13 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 9
    • 0344224195 scopus 로고    scopus 로고
    • SRF protein is upregulated during stretch-induced hypertrophy of rooster ALD muscle
    • Flück, M., Carson, J.A., Schwartz, R.J. Booth, F.W. 1999. SRF protein is upregulated during stretch-induced hypertrophy of rooster ALD muscle. J Appl Physiol 86, 1793 1799.
    • (1999) J Appl Physiol , vol.86 , pp. 1793-1799
    • Flück, M.1    Carson, J.A.2    Schwartz, R.J.3    Booth, F.W.4
  • 10
    • 0029872733 scopus 로고    scopus 로고
    • Expression and activity of serum response factor is required for expression of the muscle-determining factor MyoD in both dividing and differentiating mouse C2C12 myoblasts
    • Gauthier-Rouviére, C., Vandromme, M., Tuil, D., Lautredou, N., Morris, M., Soulez, M., Kahn, A., Fernandez, A. Lamb, N. 1996. Expression and activity of serum response factor is required for expression of the muscle-determining factor MyoD in both dividing and differentiating mouse C2C12 myoblasts. Mol Biol Cell 7, 719 729.
    • (1996) Mol Biol Cell , vol.7 , pp. 719-729
    • Gauthier-Rouviére, C.1    Vandromme, M.2    Tuil, D.3    Lautredou, N.4    Morris, M.5    Soulez, M.6    Kahn, A.7    Fernandez, A.8    Lamb, N.9
  • 11
    • 0035109446 scopus 로고    scopus 로고
    • Skeletal muscle focal adhesion kinase, paxillin, and serum response factor are loading dependent
    • Gordon, S.E., Flück, M. Booth, F.W. 2001. Skeletal muscle focal adhesion kinase, paxillin, and serum response factor are loading dependent. J Appl Physiol 90, 1174 1183.
    • (2001) J Appl Physiol , vol.90 , pp. 1174-1183
    • Gordon, S.E.1    Flück, M.2    Booth, F.W.3
  • 12
    • 0037174939 scopus 로고    scopus 로고
    • The myostatin propeptide and the follistatin-related gene are inhibitory binding proteins of myostatin in normal serum
    • Hill, J.J., Davies, M.V., Pearson, A.A., Wang, J.H., Hewick, R.M., Wolfman, N.M. Qiu, Y. 2002. The myostatin propeptide and the follistatin-related gene are inhibitory binding proteins of myostatin in normal serum. J Biol Chem 277, 40735 40741.
    • (2002) J Biol Chem , vol.277 , pp. 40735-40741
    • Hill, J.J.1    Davies, M.V.2    Pearson, A.A.3    Wang, J.H.4    Hewick, R.M.5    Wolfman, N.M.6    Qiu, Y.7
  • 14
    • 36349015405 scopus 로고    scopus 로고
    • The effects of whey protein on myostatin and cell cycle-related gene expression responses to a single heavy resistance exercise bout in trained older men
    • Hulmi, J.J., Kovanen, V., Lisko, I., Selänne, H. Mero, A.A. 2008. The effects of whey protein on myostatin and cell cycle-related gene expression responses to a single heavy resistance exercise bout in trained older men. Eur J Appl Physiol 102, 205 213.
    • (2008) Eur J Appl Physiol , vol.102 , pp. 205-213
    • Hulmi, J.J.1    Kovanen, V.2    Lisko, I.3    Selänne, H.4    Mero, A.A.5
  • 15
    • 6944226810 scopus 로고    scopus 로고
    • Disuse atrophy and exercise rehabilitation in humans profoundly affects the expression of genes associated with the regulation of skeletal muscle mass
    • Jones, S.W., Hill, R.J., Krasney, P.A., O'Conner, B., Peirce, N. Greenhaff, P.L. 2004. Disuse atrophy and exercise rehabilitation in humans profoundly affects the expression of genes associated with the regulation of skeletal muscle mass. FASEB J 18, 1025 1027.
    • (2004) FASEB J , vol.18 , pp. 1025-1027
    • Jones, S.W.1    Hill, R.J.2    Krasney, P.A.3    O'Conner, B.4    Peirce, N.5    Greenhaff, P.L.6
  • 16
    • 34248324912 scopus 로고    scopus 로고
    • The myostatin gene: Physiology and pharmacological relevance
    • Joulia-Ekaza, D. Cabello, G. 2007. The myostatin gene: physiology and pharmacological relevance. Curr Opin Pharmacol 7, 310 315.
    • (2007) Curr Opin Pharmacol , vol.7 , pp. 310-315
    • Joulia-Ekaza, D.1    Cabello, G.2
  • 17
    • 16244382549 scopus 로고    scopus 로고
    • Muscle-specific signaling mechanism that links actin dynamics to serum response factor
    • Kuwahara, K., Barrientos, T., Pipes, G.C., Li, S. Olson, E.N. 2005. Muscle-specific signaling mechanism that links actin dynamics to serum response factor. Mol Cell Biol 25, 3173 3181.
    • (2005) Mol Cell Biol , vol.25 , pp. 3173-3181
    • Kuwahara, K.1    Barrientos, T.2    Pipes, G.C.3    Li, S.4    Olson, E.N.5
  • 19
    • 0037147210 scopus 로고    scopus 로고
    • Myostatin inhibits myoblast differentiation by downregulating MyoD expression
    • Langley, B., Thomas, M., Bishop, A., Sharma, M., Gilmour, S. Kambadur, R. 2002. Myostatin inhibits myoblast differentiation by downregulating MyoD expression. J Biol Chem 277, 49831 49840.
    • (2002) J Biol Chem , vol.277 , pp. 49831-49840
    • Langley, B.1    Thomas, M.2    Bishop, A.3    Sharma, M.4    Gilmour, S.5    Kambadur, R.6
  • 20
    • 13244298415 scopus 로고    scopus 로고
    • Insulin-like growth factor-1 (IGF-1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway
    • Latres, E., Amini, A.R., Amini, A.A., Griffiths, J., Martin, F.J., Wei, Y., Lin, H.C., Yancopoulos, G.D. Glass, D.J. 2005. Insulin-like growth factor-1 (IGF-1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway. J Biol Chem 280, 2737 2744.
    • (2005) J Biol Chem , vol.280 , pp. 2737-2744
    • Latres, E.1    Amini, A.R.2    Amini, A.A.3    Griffiths, J.4    Martin, F.J.5    Wei, Y.6    Lin, H.C.7    Yancopoulos, G.D.8    Glass, D.J.9
  • 21
    • 0035979253 scopus 로고    scopus 로고
    • Regulation of myostatin activity and muscle growth
    • Lee, S.J. McPherron, A.C. 2001. Regulation of myostatin activity and muscle growth. Proc Natl Acad Sci USA 98, 9306 9311.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 9306-9311
    • Lee, S.J.1    McPherron, A.C.2
  • 23
    • 0035491028 scopus 로고    scopus 로고
    • Therapies for improving muscle function in neuromuscular disorders
    • Lynch, G.S. 2001. Therapies for improving muscle function in neuromuscular disorders. Exerc Sport Sci Rev 29, 141 148.
    • (2001) Exerc Sport Sci Rev , vol.29 , pp. 141-148
    • Lynch, G.S.1
  • 24
    • 38349043742 scopus 로고    scopus 로고
    • Repeated resistance exercise training induces different changes in mRNA expression of MAFbx and MuRF-1 in human skeletal muscle
    • Mascher, H., Tannerstedt, J., Elfegoun, T., Ekblom, B.T., Gustafsson, T. Blomstrand, E. 2008. Repeated resistance exercise training induces different changes in mRNA expression of MAFbx and MuRF-1 in human skeletal muscle. Am J Physiol Endocrinol Metab 294, E43 E51.
    • (2008) Am J Physiol Endocrinol Metab , vol.294
    • Mascher, H.1    Tannerstedt, J.2    Elfegoun, T.3    Ekblom, B.T.4    Gustafsson, T.5    Blomstrand, E.6
  • 25
    • 1642372983 scopus 로고    scopus 로고
    • RhoA expression during recovery from skeletal muscle disuse
    • McClung, J.M., Thompson, R.W., Lowe, L.L. Carson, J.A. 2004. RhoA expression during recovery from skeletal muscle disuse. J Appl Physiol 96, 1341 1348.
    • (2004) J Appl Physiol , vol.96 , pp. 1341-1348
    • McClung, J.M.1    Thompson, R.W.2    Lowe, L.L.3    Carson, J.A.4
  • 26
    • 0030840359 scopus 로고    scopus 로고
    • Double muscling in cattle due to mutations in the myostatin gene
    • McPherron, A.C. Lee, S.J. 1997b. Double muscling in cattle due to mutations in the myostatin gene. Proc Natl Acad Sci USA 94, 12457 12461.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12457-12461
    • McPherron, A.C.1    Lee, S.J.2
  • 27
    • 0031010050 scopus 로고    scopus 로고
    • Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member
    • McPherron, A.C., Lawler, A.M. Lee, S.J. 1997a. Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member. Nature 38, 783 790.
    • (1997) Nature , vol.38 , pp. 783-790
    • McPherron, A.C.1    Lawler, A.M.2    Lee, S.J.3
  • 29
    • 0032718056 scopus 로고    scopus 로고
    • Signal transduction pathways that regulate eukaryotic protein synthesis
    • Rhoads, R.E. 1999. Signal transduction pathways that regulate eukaryotic protein synthesis. J Biol Chem 274, 30337 30340.
    • (1999) J Biol Chem , vol.274 , pp. 30337-30340
    • Rhoads, R.E.1
  • 30
    • 34548349311 scopus 로고    scopus 로고
    • 2+ calmodulin-dependent protein kinase II expression and signalling in skeletal muscle of humans
    • 2+ calmodulin-dependent protein kinase II expression and signalling in skeletal muscle of humans. J Physiol 583 (Pt 2 785 795.
    • (2007) J Physiol , vol.583 , Issue.PART 2 , pp. 785-795
    • Rose, A.J.1    Frøsig, C.2    Kiens, B.3    Wojtaszewski, J.F.4    Richter, E.A.5
  • 31
    • 33846015010 scopus 로고    scopus 로고
    • Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases
    • Sacheck, J.M., Hyatt, J.P., Raffaello, A., Jagoe, R.T., Roy, R.R., Edgerton, V.R., Lecker, S.H. Goldberg, A.L. 2007. Rapid disuse and denervation atrophy involve transcriptional changes similar to those of muscle wasting during systemic diseases. FASEB J 21, 140 155.
    • (2007) FASEB J , vol.21 , pp. 140-155
    • Sacheck, J.M.1    Hyatt, J.P.2    Raffaello, A.3    Jagoe, R.T.4    Roy, R.R.5    Edgerton, V.R.6    Lecker, S.H.7    Goldberg, A.L.8
  • 32
    • 0034595910 scopus 로고    scopus 로고
    • Differential adaptation of growth and differentiation factor 8/myostatin, fibroblast growth factor 6 and leukemia inhibitory factor in overloaded, regenerating and denervated rat muscles
    • Sakuma, K., Watanabe, K., Sano, M., Uramoto, I. Totsuka, T. 2000. Differential adaptation of growth and differentiation factor 8/myostatin, fibroblast growth factor 6 and leukemia inhibitory factor in overloaded, regenerating and denervated rat muscles. Biochim Biophys Acta Mol Cell Res 1497, 77 88.
    • (2000) Biochim Biophys Acta Mol Cell Res , vol.1497 , pp. 77-88
    • Sakuma, K.1    Watanabe, K.2    Sano, M.3    Uramoto, I.4    Totsuka, T.5
  • 33
    • 0037294936 scopus 로고    scopus 로고
    • Serum response factor plays an important role in the mechanically overloaded plantaris muscle of rats
    • Sakuma, K., Nishikawa, J., Nakao, R., Nakano, H., Sano, M. Yasuhara, M. 2003. Serum response factor plays an important role in the mechanically overloaded plantaris muscle of rats. Histochem Cell Biol 119, 149 160.
    • (2003) Histochem Cell Biol , vol.119 , pp. 149-160
    • Sakuma, K.1    Nishikawa, J.2    Nakao, R.3    Nakano, H.4    Sano, M.5    Yasuhara, M.6
  • 34
    • 33744529770 scopus 로고    scopus 로고
    • Normal distribution of presenilin-1 and nicastrin in skeletal muscle and the differential responses of these proteins after denervation
    • Sakuma, K., Nakao, R., Yamasa, Y. Yasuhara, M. 2006. Normal distribution of presenilin-1 and nicastrin in skeletal muscle and the differential responses of these proteins after denervation. Biochim Biophys Acta Gen Subj 1760, 980 987.
    • (2006) Biochim Biophys Acta Gen Subj , vol.1760 , pp. 980-987
    • Sakuma, K.1    Nakao, R.2    Yamasa, Y.3    Yasuhara, M.4
  • 35
    • 49649097995 scopus 로고    scopus 로고
    • Age-related reductions in expression of serum response factor and myocardin-related transcription factor A in mouse skeletal muscles
    • Sakuma, K., Akiho, M., Nakashima, H., Akima, H. Yasuhara, M. 2008. Age-related reductions in expression of serum response factor and myocardin-related transcription factor A in mouse skeletal muscles. Biochim Biophys Acta Mol Basis Dis 1782, 453 461.
    • (2008) Biochim Biophys Acta Mol Basis Dis , vol.1782 , pp. 453-461
    • Sakuma, K.1    Akiho, M.2    Nakashima, H.3    Akima, H.4    Yasuhara, M.5
  • 39
    • 1642343601 scopus 로고    scopus 로고
    • Hypertrophy of chronically unloaded muscle subjected to resistance exercise
    • Tesch, P.A., Trieschmann, J.T. Ekberg, A. 2004. Hypertrophy of chronically unloaded muscle subjected to resistance exercise. J Appl Physiol 96, 1451 1458.
    • (2004) J Appl Physiol , vol.96 , pp. 1451-1458
    • Tesch, P.A.1    Trieschmann, J.T.2    Ekberg, A.3
  • 40
    • 0034704106 scopus 로고    scopus 로고
    • Myostatin, a negative regulator of muscle growth, functions by inhibiting myoblast proliferation
    • Thomas, M., Langley, B., Berry, C., Sharma, M., Kirk, S., Bass, J. Kambadur, R. 2000. Myostatin, a negative regulator of muscle growth, functions by inhibiting myoblast proliferation. J Biol Chem 275, 40235 40243.
    • (2000) J Biol Chem , vol.275 , pp. 40235-40243
    • Thomas, M.1    Langley, B.2    Berry, C.3    Sharma, M.4    Kirk, S.5    Bass, J.6    Kambadur, R.7
  • 41
    • 20744447058 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway as a therapeutic target for muscle wasting
    • Tisdale, M.J. 2005. The ubiquitin-proteasome pathway as a therapeutic target for muscle wasting. J Support Oncol 3, 209 217.
    • (2005) J Support Oncol , vol.3 , pp. 209-217
    • Tisdale, M.J.1
  • 43
    • 0033971745 scopus 로고    scopus 로고
    • Modulation of myostatin expression during modified muscle use
    • Wehling, M., Cai, B. Tidball, J.G. 2000. Modulation of myostatin expression during modified muscle use. FASEB J 14, 103 110.
    • (2000) FASEB J , vol.14 , pp. 103-110
    • Wehling, M.1    Cai, B.2    Tidball, J.G.3
  • 44
    • 0033918680 scopus 로고    scopus 로고
    • β1-Integrin and PI 3-kinase regulate RhoA-dependent activation of skeletal α-actin promoter in myoblasts
    • Wei, L., Zhou, W., Wang, L. Schwartz, R.J. 2000. β1-Integrin and PI 3-kinase regulate RhoA-dependent activation of skeletal α-actin promoter in myoblasts. Am J Physiol Heart Circ Physiol 278, H1736 H1743.
    • (2000) Am J Physiol Heart Circ Physiol , vol.278
    • Wei, L.1    Zhou, W.2    Wang, L.3    Schwartz, R.J.4
  • 45
    • 1842610095 scopus 로고    scopus 로고
    • Effects of heavy resistance training on myostatin mRNA and protein expression
    • Willoughby, D.S. 2004. Effects of heavy resistance training on myostatin mRNA and protein expression. Med Sci Sports Exerc 36, 574 582.
    • (2004) Med Sci Sports Exerc , vol.36 , pp. 574-582
    • Willoughby, D.S.1
  • 46
    • 2942536234 scopus 로고    scopus 로고
    • Myostatin signaling through Smad2, Smad3 and Smad4 is regulated by the inhibitory Smad7 by a negative feedback mechanism
    • Zhu, X., Topouzis, S., Liang, L.F. Stotish, R.L. 2004. Myostatin signaling through Smad2, Smad3 and Smad4 is regulated by the inhibitory Smad7 by a negative feedback mechanism. Cytokine 26, 262 272.
    • (2004) Cytokine , vol.26 , pp. 262-272
    • Zhu, X.1    Topouzis, S.2    Liang, L.F.3    Stotish, R.L.4
  • 47
    • 1842844177 scopus 로고    scopus 로고
    • Exercise treatment to counteract protein wasting of chronic diseases
    • Zinna, E.M. Yarasheski, K.E. 2003. Exercise treatment to counteract protein wasting of chronic diseases. Curr Opin Clin Nutr Metab Care 6, 87 93.
    • (2003) Curr Opin Clin Nutr Metab Care , vol.6 , pp. 87-93
    • Zinna, E.M.1    Yarasheski, K.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.