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Volumn 99, Issue 1, 2005, Pages 71-80

Clenbuterol induces muscle-specific attenuation of atrophy through effects on the ubiquitin-proteasome pathway

Author keywords

Hindlimb unweighting; Insulin like growth factor 1; Protein degradation

Indexed keywords

BETA ADRENERGIC RECEPTOR STIMULATING AGENT; CLENBUTEROL; MUSCLE PROTEIN; PROTEASOME; SOMATOMEDIN C; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME;

EID: 21644478996     PISSN: 87507587     EISSN: None     Source Type: Journal    
DOI: 10.1152/japplphysiol.00448.2004     Document Type: Article
Times cited : (88)

References (52)
  • 1
    • 0031623288 scopus 로고    scopus 로고
    • Role of insulin-like growth factor-I in the regulation of skeletal muscle adaptation to increased load
    • Adams GR. Role of insulin-like growth factor-I in the regulation of skeletal muscle adaptation to increased load. Exerc Sport Sci Rev 26: 31-60, 1998.
    • (1998) Exerc Sport Sci Rev , vol.26 , pp. 31-60
    • Adams, G.R.1
  • 3
    • 0141960862 scopus 로고    scopus 로고
    • Beta adrenoceptor agonist, clenbuterol, and isoproterenol retard denervation atrophy in rat gastrocnemius muscle: Use of 3-methylhistidine as a marker of myofibrillar degeneration
    • Agrawal S, Thakur P, and Katoch S. Beta adrenoceptor agonist, clenbuterol, and isoproterenol retard denervation atrophy in rat gastrocnemius muscle: use of 3-methylhistidine as a marker of myofibrillar degeneration. J Physiol 53: 229-237, 2003.
    • (2003) J Physiol , vol.53 , pp. 229-237
    • Agrawal, S.1    Thakur, P.2    Katoch, S.3
  • 5
    • 0036079364 scopus 로고    scopus 로고
    • Role of IGF-I and IGFBPs in the changes of mass and phenotype induced in rat soleus muscle by clenbuterol
    • Awede BL, Thissen JP, and Lebacq J. Role of IGF-I and IGFBPs in the changes of mass and phenotype induced in rat soleus muscle by clenbuterol. Am J Physiol Endocrinol Metab 282: E31-E37, 2002.
    • (2002) Am J Physiol Endocrinol Metab , vol.282
    • Awede, B.L.1    Thissen, J.P.2    Lebacq, J.3
  • 8
    • 0030661803 scopus 로고    scopus 로고
    • Molecular events underlying skeletal muscle atrophy and the development of effective countermeasures
    • Booth FW and Criswell DS. Molecular events underlying skeletal muscle atrophy and the development of effective countermeasures. Int J Sports Med 18: 256-269, 1997.
    • (1997) Int J Sports Med , vol.18 , pp. 256-269
    • Booth, F.W.1    Criswell, D.S.2
  • 9
    • 0033119577 scopus 로고    scopus 로고
    • Phosphorylation of proteasomes in mammalian cells
    • Bose S, Mason GG, and Rivett A. Phosphorylation of proteasomes in mammalian cells. Mol Biol Rep 26: 11-14, 1999.
    • (1999) Mol Biol Rep , vol.26 , pp. 11-14
    • Bose, S.1    Mason, G.G.2    Rivett, A.3
  • 10
    • 0033305506 scopus 로고    scopus 로고
    • Regulation of components of the ubiquitin system by insulin-like growth factor 1 and growth hormone in skeletal muscle of rats made catabolic with dexamethasone
    • Chrysis D and Underwood LE. Regulation of components of the ubiquitin system by insulin-like growth factor 1 and growth hormone in skeletal muscle of rats made catabolic with dexamethasone. Endocrinology 140: 5635-5641, 1999.
    • (1999) Endocrinology , vol.140 , pp. 5635-5641
    • Chrysis, D.1    Underwood, L.E.2
  • 12
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux O, Tanaka K, and Goldberg AL. Structure and functions of the 20S and 26S proteasomes. Annu Rev Biochem 65: 801-847, 1996.
    • (1996) Annu Rev Biochem , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 13
    • 0035072229 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by the 20S proteasome
    • Davies KJ. Degradation of oxidized proteins by the 20S proteasome. Biochemie 83: 301-310, 2001.
    • (2001) Biochemie , vol.83 , pp. 301-310
    • Davies, K.J.1
  • 14
    • 0031626721 scopus 로고    scopus 로고
    • Ubiquitin-proteasome pathway of intracellular protein degradation: Implications for muscle atrophy during unloading
    • Demartino GN and Ordway GA. Ubiquitin-proteasome pathway of intracellular protein degradation: implications for muscle atrophy during unloading. Exerc Sport Sci Rev 26: 219-252, 1998.
    • (1998) Exerc Sport Sci Rev , vol.26 , pp. 219-252
    • Demartino, G.N.1    Ordway, G.A.2
  • 15
    • 0035987612 scopus 로고    scopus 로고
    • Clenbuterol attenuates muscle atrophy and dysfunction in hindlimb-suspended rats
    • Dodd SL and Koesterer TJ. Clenbuterol attenuates muscle atrophy and dysfunction in hindlimb-suspended rats. Aviat Space Environ Med 73: 635-639, 2002.
    • (2002) Aviat Space Environ Med , vol.73 , pp. 635-639
    • Dodd, S.L.1    Koesterer, T.J.2
  • 16
    • 0028202862 scopus 로고
    • Differential tissue regulation of insulin-like growth factor-1 content and binding proteins after endotoxin
    • Fan J, Molina PE, Gelato MC, and Lang CH. Differential tissue regulation of insulin-like growth factor-1 content and binding proteins after endotoxin. Endocrinology 134: 1685-1692, 1994.
    • (1994) Endocrinology , vol.134 , pp. 1685-1692
    • Fan, J.1    Molina, P.E.2    Gelato, M.C.3    Lang, C.H.4
  • 17
    • 0031598822 scopus 로고    scopus 로고
    • The molecular regulation of protein breakdown following burn injury is different in fast- And slow-twitch skeletal muscle
    • Fang CH, Li BG, Tiao G, Wang JJ, Fischer JE, and Hasseigren PO. The molecular regulation of protein breakdown following burn injury is different in fast- and slow-twitch skeletal muscle. Int J Mol Med 1: 163-169, 1998.
    • (1998) Int J Mol Med , vol.1 , pp. 163-169
    • Fang, C.H.1    Li, B.G.2    Tiao, G.3    Wang, J.J.4    Fischer, J.E.5    Hasseigren, P.O.6
  • 18
    • 0033883216 scopus 로고    scopus 로고
    • Physiology of a microgravity environment. Invited review: Microgravity and skeletal muscle
    • Fitts RH, Riley DR, and Widrick JJ. Physiology of a microgravity environment. Invited review: Microgravity and skeletal muscle. J Appl Physiol 89: 823-839, 2000.
    • (2000) J Appl Physiol , vol.89 , pp. 823-839
    • Fitts, R.H.1    Riley, D.R.2    Widrick, J.J.3
  • 19
    • 0029907306 scopus 로고    scopus 로고
    • Growth hormone and the insulin-like growth factor system in myogenesis
    • Florini JR, Ewton DZ, and Coolican SA. Growth hormone and the insulin-like growth factor system in myogenesis. Endocr Rev 17: 481-517, 1996.
    • (1996) Endocr Rev , vol.17 , pp. 481-517
    • Florini, J.R.1    Ewton, D.Z.2    Coolican, S.A.3
  • 21
    • 0032493104 scopus 로고    scopus 로고
    • Examining potential drug therapies for muscle dystrophy utilizing the dy/dy mouse: I. Clenbuterol
    • Hayes A and Williams DA. Examining potential drug therapies for muscle dystrophy utilizing the dy/dy mouse: I. Clenbuterol. J Neurol Sci 157: 122-128, 1998.
    • (1998) J Neurol Sci , vol.157 , pp. 122-128
    • Hayes, A.1    Williams, D.A.2
  • 22
    • 0028507737 scopus 로고
    • Effects of serum and insulin-like growth factor I on protein degradation and protease gene expression in rat L8 myotubes
    • Hong D and Frosberg NE. Effects of serum and insulin-like growth factor I on protein degradation and protease gene expression in rat L8 myotubes. J Anim Sci 72: 2279-2288, 1994.
    • (1994) J Anim Sci , vol.72 , pp. 2279-2288
    • Hong, D.1    Frosberg, N.E.2
  • 24
    • 0035350530 scopus 로고    scopus 로고
    • What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?
    • Jagoe RT and Goldberg AL. What do we really know about the ubiquitin-proteasome pathway in muscle atrophy? Curr Opin Clin Nutr Metab Care 4: 183-190, 2001.
    • (2001) Curr Opin Clin Nutr Metab Care , vol.4 , pp. 183-190
    • Jagoe, R.T.1    Goldberg, A.L.2
  • 25
    • 0023903166 scopus 로고
    • Effects of immobilization on rat hind limb muscles under non-weight-bearing conditions
    • Jaspers SR, Fagan JM, Satarug S, Cook PH, and Tischler ME. Effects of immobilization on rat hind limb muscles under non-weight-bearing conditions. Muscle Nerve 11: 458-466, 1988.
    • (1988) Muscle Nerve , vol.11 , pp. 458-466
    • Jaspers, S.R.1    Fagan, J.M.2    Satarug, S.3    Cook, P.H.4    Tischler, M.E.5
  • 26
    • 0036893386 scopus 로고    scopus 로고
    • Increased antioxidant capacity does not attenuate muscle atrophy caused by unweighting
    • Koesterer TK, Dodd SL, Powers SK. Increased antioxidant capacity does not attenuate muscle atrophy caused by unweighting. J Appl Physiol 93: 1959-1965, 2002.
    • (2002) J Appl Physiol , vol.93 , pp. 1959-1965
    • Koesterer, T.K.1    Dodd, S.L.2    Powers, S.K.3
  • 27
    • 0035215549 scopus 로고    scopus 로고
    • 2+-dependent and ubiquitin/proteasome-dependent proteolytic pathways in fast-twitch and slow-twitch rat muscle following hyperinsulinaemia
    • 2+-dependent and ubiquitin/proteasome-dependent proteolytic pathways in fast-twitch and slow-twitch rat muscle following hyperinsulinaemia. Clin Sci (Lond) 101: 551-558, 2001.
    • (2001) Clin Sci (Lond) , vol.101 , pp. 551-558
    • Larbaud, D.1    Balage, M.2    Taillandier, D.3    Combaret, L.4    Grizard, J.5    Attaix, D.6
  • 28
    • 0037861856 scopus 로고    scopus 로고
    • Hindlimb unloading increases oxidative stress and disrupts antioxidant capacity in skeletal muscle
    • Lawler JM, Song W, and Demaree SR. Hindlimb unloading increases oxidative stress and disrupts antioxidant capacity in skeletal muscle. Free Radic Biol Med 35: 9-16, 2003.
    • (2003) Free Radic Biol Med , vol.35 , pp. 9-16
    • Lawler, J.M.1    Song, W.2    Demaree, S.R.3
  • 29
    • 1642526416 scopus 로고    scopus 로고
    • Insulin-like growth factor-T blocks dexamethasone-induced protein degradation in cultured myotubes by inhibiting multiple proteolytic pathways
    • Li BG, Hasseigren PO, Fang CH, and Warden GD. Insulin-like growth factor-T blocks dexamethasone-induced protein degradation in cultured myotubes by inhibiting multiple proteolytic pathways. J Burn Care Rehabil 25: 112-118, 2004.
    • (2004) J Burn Care Rehabil , vol.25 , pp. 112-118
    • Li, B.G.1    Hasseigren, P.O.2    Fang, C.H.3    Warden, G.D.4
  • 30
    • 0035984736 scopus 로고    scopus 로고
    • Adverse and beneficial functions of proteolytic enzymes in skeletal muscles: An overview
    • Mantle D and Preedy VR. Adverse and beneficial functions of proteolytic enzymes in skeletal muscles: an overview. Adverse Drug React Toxicol Rev 21: 31-49, 2002.
    • (2002) Adverse Drug React Toxicol Rev , vol.21 , pp. 31-49
    • Mantle, D.1    Preedy, V.R.2
  • 31
    • 0029892643 scopus 로고    scopus 로고
    • Phosphorylation of proteasomes in mammalian cells: Identification of two phosphorylated subunits and the effect of phosphorylation on activity
    • Mason GG, Hendil KB, and Rivett A. Phosphorylation of proteasomes in mammalian cells: identification of two phosphorylated subunits and the effect of phosphorylation on activity. Eur J Biochem 238: 453-462, 1996.
    • (1996) Eur J Biochem , vol.238 , pp. 453-462
    • Mason, G.G.1    Hendil, K.B.2    Rivett, A.3
  • 32
    • 0036092597 scopus 로고    scopus 로고
    • Hindlimb unloading rodent model: Technical aspects
    • Morey-Holton ER and Globus RK. Hindlimb unloading rodent model: technical aspects. J Appl Physiol 92: 1367-1377, 2002.
    • (2002) J Appl Physiol , vol.92 , pp. 1367-1377
    • Morey-Holton, E.R.1    Globus, R.K.2
  • 35
    • 0022456299 scopus 로고
    • Stimulation of muscle growth by clenbuterol: Lack of effect on muscle protein biosynthesis
    • Reeds PJ, Hay SM, Dorwood PM, and Palmer RM. Stimulation of muscle growth by clenbuterol: lack of effect on muscle protein biosynthesis. Br J Nutr 56: 249-258, 1986.
    • (1986) Br J Nutr , vol.56 , pp. 249-258
    • Reeds, P.J.1    Hay, S.M.2    Dorwood, P.M.3    Palmer, R.M.4
  • 37
    • 0028246550 scopus 로고
    • Decreased femoral arterial flow during simulated microgravity in the rat
    • Roer RD and Dillaman RM. Decreased femoral arterial flow during simulated microgravity in the rat. J Appl Physiol 76: 2125-2129, 1994.
    • (1994) J Appl Physiol , vol.76 , pp. 2125-2129
    • Roer, R.D.1    Dillaman, R.M.2
  • 39
    • 0034076016 scopus 로고    scopus 로고
    • Effect of clenbuterol on growth in underfed cattle
    • Sillence MN, Matthews ML, and Badran TW. Effect of clenbuterol on growth in underfed cattle. Aust J Arg Res 51: 401-406, 2000.
    • (2000) Aust J Arg Res , vol.51 , pp. 401-406
    • Sillence, M.N.1    Matthews, M.L.2    Badran, T.W.3
  • 40
    • 0029956781 scopus 로고    scopus 로고
    • Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts
    • Solomon V and Goldberg AL. Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts. J Biochem 271: 26690-26697, 1996.
    • (1996) J Biochem , vol.271 , pp. 26690-26697
    • Solomon, V.1    Goldberg, A.L.2
  • 41
    • 0029886022 scopus 로고    scopus 로고
    • Kinetic characterization of the chymotryptic activity of the 20S proteasome
    • Stein RL, Melabdri F, and Dick L. Kinetic characterization of the chymotryptic activity of the 20S proteasome. Biochemistry 35: 3899-3908, 1996.
    • (1996) Biochemistry , vol.35 , pp. 3899-3908
    • Stein, R.L.1    Melabdri, F.2    Dick, L.3
  • 42
    • 0033715778 scopus 로고    scopus 로고
    • Effects of unweighting and clenbuterol on myosin light and heavy chains in fast and slow muscles of rat
    • Stevens L, Firinga C, Gohlsch B, Bastide B, Meunier Y, and Pette D. Effects of unweighting and clenbuterol on myosin light and heavy chains in fast and slow muscles of rat. Am J Physiol Cell Physiol 279: C1558-C1563, 2000.
    • (2000) Am J Physiol Cell Physiol , vol.279
    • Stevens, L.1    Firinga, C.2    Gohlsch, B.3    Bastide, B.4    Meunier, Y.5    Pette, D.6
  • 43
    • 0034997402 scopus 로고    scopus 로고
    • Fiber type-specific expression of major proteolytic enzyme system in fast- to slow-transforming rabbit muscle
    • Sultan KR, Dittrich BT, Leisner E, Paul N, and Pette D. Fiber type-specific expression of major proteolytic enzyme system in fast- to slow-transforming rabbit muscle. Am J Physiol Cell Physiol 280: C239-C247, 2001.
    • (2001) Am J Physiol Cell Physiol , vol.280
    • Sultan, K.R.1    Dittrich, B.T.2    Leisner, E.3    Paul, N.4    Pette, D.5
  • 45
    • 0025019455 scopus 로고
    • Atrophy of the soleus muscle by hindlimb unweighting
    • Thomason DB and Booth FW. Atrophy of the soleus muscle by hindlimb unweighting. J Appl Physiol 68: 1-12, 1990.
    • (1990) J Appl Physiol , vol.68 , pp. 1-12
    • Thomason, D.B.1    Booth, F.W.2
  • 47
    • 0000569087 scopus 로고
    • A fluorometric method for the estimation of tyrosine in plasma and tissues
    • Waalkes TP and Udenfriend S. A fluorometric method for the estimation of tyrosine in plasma and tissues. J Lab Clin Med 50: 733-736, 1957.
    • (1957) J Lab Clin Med , vol.50 , pp. 733-736
    • Waalkes, T.P.1    Udenfriend, S.2
  • 48
    • 0029806222 scopus 로고    scopus 로고
    • Insulin-like growth factor I stimulates degradation of an mRNA transcript encoding the 14kDa ubiquitin-conjugating enzyme
    • Wing SS and Bedard N. Insulin-like growth factor I stimulates degradation of an mRNA transcript encoding the 14kDa ubiquitin-conjugating enzyme. Biochem J 319: 455-461, 1996.
    • (1996) Biochem J , vol.319 , pp. 455-461
    • Wing, S.S.1    Bedard, N.2
  • 49
    • 0029022262 scopus 로고
    • Increase in ubiquitin-protein conjugates concomitant with the increase in proteolysis in rat skeletal muscle during starvation and atrophy denervation
    • Wing SS, Hass AL, and Goldberg AL. Increase in ubiquitin-protein conjugates concomitant with the increase in proteolysis in rat skeletal muscle during starvation and atrophy denervation. Biochem J 307: 639-645, 1995.
    • (1995) Biochem J , vol.307 , pp. 639-645
    • Wing, S.S.1    Hass, A.L.2    Goldberg, A.L.3
  • 50
    • 0024333198 scopus 로고
    • Multiple actions of β-adrenergic agonists on skeletal muscle and adipose tissue
    • Yang YT and McElligott MA. Multiple actions of β-adrenergic agonists on skeletal muscle and adipose tissue. Biochem J 261: 1-10, 1989.
    • (1989) Biochem J , vol.261 , pp. 1-10
    • Yang, Y.T.1    McElligott, M.A.2


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