메뉴 건너뛰기




Volumn 39, Issue 4, 2012, Pages 364-372

Calpastatin overexpression in the skeletal muscle of mice prevents clenbuterol-induced muscle hypertrophy and phenotypic shift

Author keywords

Calpain; Calpastatin; Clenbuterol; Hypertrophy; Mouse; Muscle; Phenotypic shift

Indexed keywords

AMPK PROTEIN; CALPAIN; CALPASTATIN; CAMK2 PROTEIN; CLENBUTEROL; INITIATION FACTOR 4E BINDING PROTEIN 1; MAMMALIAN TARGET OF RAPAMYCIN; PROTEIN; PROTEIN KINASE B; PROTEIN S6; UNCLASSIFIED DRUG;

EID: 84858987556     PISSN: 03051870     EISSN: 14401681     Source Type: Journal    
DOI: 10.1111/j.1440-1681.2012.05677.x     Document Type: Article
Times cited : (11)

References (39)
  • 4
    • 0017101439 scopus 로고
    • 2+-activated protease possibly involved in myofibrillar protein turnover. Purification from porcine muscle
    • 2+-activated protease possibly involved in myofibrillar protein turnover. Purification from porcine muscle. Biochemistry 1976; 15: 2150-8.
    • (1976) Biochemistry , vol.15 , pp. 2150-2158
    • Dayton, W.R.1    Goll, D.E.2    Zeece, M.G.3    Robson, R.M.4    Reville, W.J.5
  • 5
    • 45949101825 scopus 로고    scopus 로고
    • Myofibrillar protein turnover: The proteasome and the calpains
    • Goll DE, Neti G, Mares SW, Thompson VF. Myofibrillar protein turnover: The proteasome and the calpains. J. Anim. Sci. 2008; 86: E19-35.
    • (2008) J. Anim. Sci. , vol.86
    • Goll, D.E.1    Neti, G.2    Mares, S.W.3    Thompson, V.F.4
  • 6
    • 0027205596 scopus 로고
    • Calpastatin has two distinct sites for interaction with calpain: Effect of calpastatin fragments on the binding of calpain to membranes
    • Kawasaki H, Emori Y, Suzuki K. Calpastatin has two distinct sites for interaction with calpain: Effect of calpastatin fragments on the binding of calpain to membranes. Arch. Biochem. Biophys. 1993; 305: 467-72.
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 467-472
    • Kawasaki, H.1    Emori, Y.2    Suzuki, K.3
  • 7
    • 0033825945 scopus 로고    scopus 로고
    • Calpain activity in fast, slow, transforming, and regenerating skeletal muscles of rat
    • Sultan KR, Dittrich BT, Pette D. Calpain activity in fast, slow, transforming, and regenerating skeletal muscles of rat. Am. J. Physiol. Cell Physiol. 2000; 279: C639-47.
    • (2000) Am. J. Physiol. Cell Physiol. , vol.279
    • Sultan, K.R.1    Dittrich, B.T.2    Pette, D.3
  • 8
    • 0029903175 scopus 로고    scopus 로고
    • 2+-activated and ATP-ubiquitin-dependent proteinases in the unweighted rat soleus muscle
    • 2+-activated and ATP-ubiquitin-dependent proteinases in the unweighted rat soleus muscle. Biochem. J 1996; 316: 65-72.
    • (1996) Biochem. J , vol.316 , pp. 65-72
    • Taillandier, D.1    Aurousseau, E.2    Meynial-Denis, D.3
  • 9
    • 34250678518 scopus 로고    scopus 로고
    • Differential localization of autolyzed calpains 1 and 2 in slow and fast skeletal muscles in the early phase of atrophy
    • Vermaelen M, Sirvent P, Raynaud F et al. Differential localization of autolyzed calpains 1 and 2 in slow and fast skeletal muscles in the early phase of atrophy. Am. J. Physiol. Cell Physiol. 2007; 292: C1723-31.
    • (2007) Am. J. Physiol. Cell Physiol. , vol.292
    • Vermaelen, M.1    Sirvent, P.2    Raynaud, F.3
  • 10
    • 2442666398 scopus 로고    scopus 로고
    • Calpain system regulates muscle mass and glucose transporter GLUT4 turnover
    • Otani K, Han DH, Ford EL et al. Calpain system regulates muscle mass and glucose transporter GLUT4 turnover. J. Biol. Chem. 2004; 279: 20.
    • (2004) J. Biol. Chem. , vol.279 , pp. 20
    • Otani, K.1    Han, D.H.2    Ford, E.L.3
  • 11
    • 33748466001 scopus 로고    scopus 로고
    • Inhibition of calpain results in impaired contraction-stimulated GLUT4 translocation in skeletal muscle
    • Otani K, Polonsky KS, Holloszy JO, Han DH. Inhibition of calpain results in impaired contraction-stimulated GLUT4 translocation in skeletal muscle. Am. J. Physiol. Endocrinol. Metab 2006; 291: E544-8.
    • (2006) Am. J. Physiol. Endocrinol. Metab , vol.291
    • Otani, K.1    Polonsky, K.S.2    Holloszy, J.O.3    Han, D.H.4
  • 12
    • 42949139481 scopus 로고    scopus 로고
    • AMPK phosphorylation of raptor mediates a metabolic checkpoint
    • Gwinn DM, Shackelford DB, Egan DF et al. AMPK phosphorylation of raptor mediates a metabolic checkpoint. Mol. Cell 2008; 30: 214-26.
    • (2008) Mol. Cell , vol.30 , pp. 214-226
    • Gwinn, D.M.1    Shackelford, D.B.2    Egan, D.F.3
  • 13
    • 0036713778 scopus 로고    scopus 로고
    • TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling
    • Inoki K, Li Y, Zhu T, Wu J, Guan KL. TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling. Nat. Cell Biol. 2002; 4: 648-57.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 648-657
    • Inoki, K.1    Li, Y.2    Zhu, T.3    Wu, J.4    Guan, K.L.5
  • 14
    • 32044465506 scopus 로고    scopus 로고
    • TOR signaling in growth and metabolism
    • Wullschleger S, Loewith R, Hall MN. TOR signaling in growth and metabolism. Cell 2006; 124: 471-84.
    • (2006) Cell , vol.124 , pp. 471-484
    • Wullschleger, S.1    Loewith, R.2    Hall, M.N.3
  • 15
    • 23044495913 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent kinases in skeletal muscle plasticity
    • 2+/calmodulin-dependent kinases in skeletal muscle plasticity. J. Appl. Physiol. 2005; 99: 414-23.
    • (2005) J. Appl. Physiol. , vol.99 , pp. 414-423
    • Chin, E.R.1
  • 16
    • 2942720949 scopus 로고    scopus 로고
    • The role of calcium and calcium/calmodulin-dependent kinases in skeletal muscle plasticity and mitochondrial biogenesis
    • Chin ER. The role of calcium and calcium/calmodulin-dependent kinases in skeletal muscle plasticity and mitochondrial biogenesis. Proc. Nutr. Soc 2004; 63: 279-86.
    • (2004) Proc. Nutr. Soc , vol.63 , pp. 279-286
    • Chin, E.R.1
  • 17
    • 0029797113 scopus 로고    scopus 로고
    • Effects of beta 2-agonist administration and exercise on contractile activation of skeletal muscle fibers
    • Lynch GS, Hayes A, Campbell SP, Williams DA. Effects of beta 2-agonist administration and exercise on contractile activation of skeletal muscle fibers. J. Appl. Physiol. 1996; 81: 1610-18.
    • (1996) J. Appl. Physiol. , vol.81 , pp. 1610-1618
    • Lynch, G.S.1    Hayes, A.2    Campbell, S.P.3    Williams, D.A.4
  • 18
    • 1542329713 scopus 로고    scopus 로고
    • Beta 2-agonist administration reverses muscle wasting and improves muscle function in aged rats
    • Ryall JG, Plant DR, Gregorevic P, Sillence MN, Lynch GS. Beta 2-agonist administration reverses muscle wasting and improves muscle function in aged rats. J. Physiol. 2004; 555: 175-88.
    • (2004) J. Physiol. , vol.555 , pp. 175-188
    • Ryall, J.G.1    Plant, D.R.2    Gregorevic, P.3    Sillence, M.N.4    Lynch, G.S.5
  • 19
    • 1542344875 scopus 로고    scopus 로고
    • Clenbuterol treatment affects myosin heavy chain isoforms and MyoD content similarly in intact and regenerated soleus muscles
    • Bricout VA, Serrurier BD, Bigard AX. Clenbuterol treatment affects myosin heavy chain isoforms and MyoD content similarly in intact and regenerated soleus muscles. Acta Physiol. Scand. 2004; 180: 271-80.
    • (2004) Acta Physiol. Scand. , vol.180 , pp. 271-280
    • Bricout, V.A.1    Serrurier, B.D.2    Bigard, A.X.3
  • 20
    • 42049097879 scopus 로고    scopus 로고
    • Role of beta-adrenoceptor signaling in skeletal muscle. Implications for muscle wasting and disease
    • Lynch GS, Ryall JG. Role of beta-adrenoceptor signaling in skeletal muscle. Implications for muscle wasting and disease. Physiol. Rev. 2008; 88: 729-67.
    • (2008) Physiol. Rev. , vol.88 , pp. 729-767
    • Lynch, G.S.1    Ryall, J.G.2
  • 21
    • 0026587025 scopus 로고
    • Effect of beta-agonists on expression of calpain and calpastatin activity in skeletal muscle
    • Bardsley RG, Allcock SM, Dawson JM et al. Effect of beta-agonists on expression of calpain and calpastatin activity in skeletal muscle. Biochimie 1992; 74: 267-73.
    • (1992) Biochimie , vol.74 , pp. 267-273
    • Bardsley, R.G.1    Allcock, S.M.2    Dawson, J.M.3
  • 22
    • 0026673878 scopus 로고
    • Changes in calpain and calpastatin mRNA induced by beta-adrenergic stimulation of bovine skeletal muscle
    • Parr T, Bardsley RG, Gilmour RS, Buttery PJ. Changes in calpain and calpastatin mRNA induced by beta-adrenergic stimulation of bovine skeletal muscle. Eur. J. Biochem. 1992; 208: 333-9.
    • (1992) Eur. J. Biochem. , vol.208 , pp. 333-339
    • Parr, T.1    Bardsley, R.G.2    Gilmour, R.S.3    Buttery, P.J.4
  • 23
    • 79953080689 scopus 로고    scopus 로고
    • Time course in calpain activity and autolysis in slow and fast skeletal muscle during clenbuterol treatment
    • Douillard A, Galbes O, Rossano B et al. Time course in calpain activity and autolysis in slow and fast skeletal muscle during clenbuterol treatment. Can. J. Physiol. Pharmacol. 2011; 89: 117-25.
    • (2011) Can. J. Physiol. Pharmacol. , vol.89 , pp. 117-125
    • Douillard, A.1    Galbes, O.2    Rossano, B.3
  • 24
    • 0031775691 scopus 로고    scopus 로고
    • Effect of clenbuterol on sarcoplasmic reticulum function in single skinned mammalian skeletal muscle fibers
    • Bakker AJ, Head SI, Wareham AC, Stephenson DG. Effect of clenbuterol on sarcoplasmic reticulum function in single skinned mammalian skeletal muscle fibers. Am. J. Physiol. 1998; 274: C1718-26.
    • (1998) Am. J. Physiol. , vol.274
    • Bakker, A.J.1    Head, S.I.2    Wareham, A.C.3    Stephenson, D.G.4
  • 26
    • 0037318822 scopus 로고    scopus 로고
    • Signalling pathways that mediate skeletal muscle hypertrophy and atrophy
    • Glass DJ. Signalling pathways that mediate skeletal muscle hypertrophy and atrophy. Nat. Cell Biol. 2003; 5: 87-90.
    • (2003) Nat. Cell Biol. , vol.5 , pp. 87-90
    • Glass, D.J.1
  • 27
    • 33846885682 scopus 로고    scopus 로고
    • Rapamycin inhibits the growth and muscle-sparing effects of clenbuterol
    • Kline WO, Panaro FJ, Yang H, Bodine SC. Rapamycin inhibits the growth and muscle-sparing effects of clenbuterol. J. Appl. Physiol. 2007; 102: 740-7.
    • (2007) J. Appl. Physiol. , vol.102 , pp. 740-747
    • Kline, W.O.1    Panaro, F.J.2    Yang, H.3    Bodine, S.C.4
  • 28
    • 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, 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 2002; 282: E31-7.
    • (2002) Am. J. Physiol. Endocrinol. Metab , vol.282
    • Awede, B.L.1    Thissen, J.P.2    Lebacq, J.3
  • 29
    • 21644478996 scopus 로고    scopus 로고
    • Clenbuterol induces muscle-specific attenuation of atrophy through effects on the ubiquitin-proteasome pathway
    • Yimlamai T, Dodd SL, Borst SE, Park S. Clenbuterol induces muscle-specific attenuation of atrophy through effects on the ubiquitin-proteasome pathway. J. Appl. Physiol. 2005; 99: 71-80.
    • (2005) J. Appl. Physiol. , vol.99 , pp. 71-80
    • Yimlamai, T.1    Dodd, S.L.2    Borst, S.E.3    Park, S.4
  • 30
    • 15444370210 scopus 로고    scopus 로고
    • beta2-Adrenergic receptor stimulation in vivo induces apoptosis in the rat heart and soleus muscle
    • Burniston JG, Tan LB, Goldspink DF. beta2-Adrenergic receptor stimulation in vivo induces apoptosis in the rat heart and soleus muscle. J. Appl. Physiol. 2005; 98: 1379.86.
    • (2005) J. Appl. Physiol. , vol.98 , pp. 1379-1386
    • Burniston, J.G.1    Tan, L.B.2    Goldspink, D.F.3
  • 31
    • 0036436160 scopus 로고    scopus 로고
    • Interleukin-10 expression after intramuscular DNA electrotransfer: Kinetic studies
    • Deleuze V, Scherman D, Bureau MF. Interleukin-10 expression after intramuscular DNA electrotransfer: Kinetic studies. Biochem. Biophys. Res. Commun. 2002; 299: 29-34.
    • (2002) Biochem. Biophys. Res. Commun. , vol.299 , pp. 29-34
    • Deleuze, V.1    Scherman, D.2    Bureau, M.F.3
  • 32
    • 0034307653 scopus 로고    scopus 로고
    • A double-injection DNA electroporation protocol to enhance in vivo gene delivery in skeletal muscle
    • Hoover F, Magne Kalhovde J. A double-injection DNA electroporation protocol to enhance in vivo gene delivery in skeletal muscle. Anal. Biochem. 2000; 285: 175-8.
    • (2000) Anal. Biochem. , vol.285 , pp. 175-178
    • Hoover, F.1    Magne Kalhovde, J.2
  • 33
    • 0029149244 scopus 로고
    • The role of cysteine proteases in hypoxia-induced rat renal proximal tubular injury
    • Edelstein CL, Wieder ED, Yaqoob MM et al. The role of cysteine proteases in hypoxia-induced rat renal proximal tubular injury. Proc. Natl Acad. Sci. USA 1995; 92: 7662-6.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 7662-7666
    • Edelstein, C.L.1    Wieder, E.D.2    Yaqoob, M.M.3
  • 34
    • 33644897573 scopus 로고    scopus 로고
    • Calpain inhibition: A therapeutic strategy targeting multiple disease states
    • Carragher NO. Calpain inhibition: A therapeutic strategy targeting multiple disease states. Curr. Pharm. Des. 2006; 12: 615-38.
    • (2006) Curr. Pharm. Des. , vol.12 , pp. 615-638
    • Carragher, N.O.1
  • 35
    • 25844488169 scopus 로고    scopus 로고
    • Kinetics of transgene expression after electrotransfer into skeletal muscle: Importance of promoter origin/strength
    • Durieux AC, Bonnefoy R, Freyssenet D. Kinetics of transgene expression after electrotransfer into skeletal muscle: Importance of promoter origin/strength. Biochim. Biophys. Acta 2005; 1725: 403-9.
    • (2005) Biochim. Biophys. Acta , vol.1725 , pp. 403-409
    • Durieux, A.C.1    Bonnefoy, R.2    Freyssenet, D.3
  • 36
    • 77956623574 scopus 로고    scopus 로고
    • Coordinated maintenance of muscle cell size control by AMP-activated protein kinase
    • Lantier L, Mounier R, Leclerc J, Pende M, Foretz M, Viollet B. Coordinated maintenance of muscle cell size control by AMP-activated protein kinase. FASEB J 2010; 24: 3555-61.
    • (2010) FASEB J , vol.24 , pp. 3555-3561
    • Lantier, L.1    Mounier, R.2    Leclerc, J.3    Pende, M.4    Foretz, M.5    Viollet, B.6
  • 37
    • 68549106237 scopus 로고    scopus 로고
    • Important role for AMPKalpha1 in limiting skeletal muscle cell hypertrophy
    • Mounier R, Lantier L, Leclerc J et al. Important role for AMPKalpha1 in limiting skeletal muscle cell hypertrophy. FASEB J 2009; 23: 2264-73.
    • (2009) FASEB J , vol.23 , pp. 2264-2273
    • Mounier, R.1    Lantier, L.2    Leclerc, J.3
  • 38
    • 0024333198 scopus 로고
    • Multiple actions of beta-adrenergic agonists on skeletal muscle and adipose tissue
    • Yang YT, McElligott MA. Multiple actions of beta-adrenergic agonists on skeletal muscle and adipose tissue. Biochem. J 1989; 261: 1-10.
    • (1989) Biochem. J , vol.261 , pp. 1-10
    • Yang, Y.T.1    McElligott, M.A.2
  • 39
    • 0023931913 scopus 로고
    • Slow to fast alterations in skeletal muscle fibers caused by clenbuterol, a beta 2-receptor agonist
    • Zeman RJ, Ludemann R, Easton TG, Etlinger JD. Slow to fast alterations in skeletal muscle fibers caused by clenbuterol, a beta 2-receptor agonist. Am. J. Physiol. 1988; 254: E726-32.
    • (1988) Am. J. Physiol. , vol.254
    • Zeman, R.J.1    Ludemann, R.2    Easton, T.G.3    Etlinger, J.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.