메뉴 건너뛰기




Volumn 315, Issue 1-2, 2010, Pages 104-112

Involvement of cAMP/Epac/PI3K-dependent pathway in the antiproteolytic effect of epinephrine on rat skeletal muscle

Author keywords

AKT; cAMP; Epac; Foxo3a; PKA; Skeletal muscle proteolysis

Indexed keywords

ADRENALIN; ANTIPORTER; CYCLIC AMP; CYCLIC AMP DEPENDENT PROTEIN KINASE; EXCHANGE PROTEIN DIRECTLY ACTIVATED BY CYCLIC AMP; INSULIN; N [2 (4 BROMOCINNAMYLAMINO)ETHYL] 5 ISOQUINOLINESULFONAMIDE; PHOSPHATIDYLINOSITOL 3 KINASE; TRANSCRIPTION FACTOR FKHRL1; UNCLASSIFIED DRUG; WORTMANNIN;

EID: 71849084153     PISSN: 03037207     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mce.2009.09.028     Document Type: Article
Times cited : (42)

References (44)
  • 3
    • 49449097930 scopus 로고    scopus 로고
    • Chemical sympathectomy further increases muscle protein degradation of acutely diabetic rats
    • Baviera A.M., Zanon N.M., Navegantes L.C., Migliorini R.H., and Kettelhut I.C. Chemical sympathectomy further increases muscle protein degradation of acutely diabetic rats. Muscle Nerve 38 (2008) 1027-1035
    • (2008) Muscle Nerve , vol.38 , pp. 1027-1035
    • Baviera, A.M.1    Zanon, N.M.2    Navegantes, L.C.3    Migliorini, R.H.4    Kettelhut, I.C.5
  • 4
    • 8044257699 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase inhibitors wortmannin and LY294002 inhibit autophagy in isolated rat hepatocytes
    • Blommaart E.F., Krause U., Schellens J.P., Vreeling-Sindelárová H., and Meijer A.J. The phosphatidylinositol 3-kinase inhibitors wortmannin and LY294002 inhibit autophagy in isolated rat hepatocytes. Eur. J. Biochem. 243 (1997) 240-246
    • (1997) Eur. J. Biochem. , vol.243 , pp. 240-246
    • Blommaart, E.F.1    Krause, U.2    Schellens, J.P.3    Vreeling-Sindelárová, H.4    Meijer, A.J.5
  • 5
    • 69249216479 scopus 로고    scopus 로고
    • EPAC proteins transduce diverse cellular actions of cAMP
    • Borland G., Smith B.O., and Yarwood S.J. EPAC proteins transduce diverse cellular actions of cAMP. Br. J. Pharmacol. 158 (2009) 70-86
    • (2009) Br. J. Pharmacol. , vol.158 , pp. 70-86
    • Borland, G.1    Smith, B.O.2    Yarwood, S.J.3
  • 6
    • 24344439701 scopus 로고    scopus 로고
    • Adrenaline potentiates insulin-stimulated PKB activation via cAMP and Epac: implications for cross talk between insulin and adrenaline
    • Brennesvik E.O., Ktori C., Ruzzin J., Jebens E., Shepherd P.R., and Jensen J. Adrenaline potentiates insulin-stimulated PKB activation via cAMP and Epac: implications for cross talk between insulin and adrenaline. Cell. Signal. 17 (2005) 1551-1559
    • (2005) Cell. Signal. , vol.17 , pp. 1551-1559
    • Brennesvik, E.O.1    Ktori, C.2    Ruzzin, J.3    Jebens, E.4    Shepherd, P.R.5    Jensen, J.6
  • 7
    • 47549108691 scopus 로고    scopus 로고
    • Epac and PKA: a tale of two intracellular cAMP receptors
    • Cheng X., Ji Z., Tsalkova T., and Mei F. Epac and PKA: a tale of two intracellular cAMP receptors. Acta Biochim. Biophys. Sin. 40 (2008) 651-662
    • (2008) Acta Biochim. Biophys. Sin. , vol.40 , pp. 651-662
    • Cheng, X.1    Ji, Z.2    Tsalkova, T.3    Mei, F.4
  • 8
    • 0029779604 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase and p70s6 kinase participate in the regulation of protein turnover in skeletal muscle by insulin and insulin-like growth factor I
    • Dardevet D., Sornet C., Vary T., and Grizard J. Phosphatidylinositol 3-kinase and p70s6 kinase participate in the regulation of protein turnover in skeletal muscle by insulin and insulin-like growth factor I. Endocrinology 137 (1996) 4087-4094
    • (1996) Endocrinology , vol.137 , pp. 4087-4094
    • Dardevet, D.1    Sornet, C.2    Vary, T.3    Grizard, J.4
  • 11
    • 22144453941 scopus 로고    scopus 로고
    • Protein breakdown in muscle from burned rats is blocked by insulin-like growth factor I and glycogen synthase kinase-3beta inhibitors
    • Fang C.H., Li B.G., James J.H., King J.K., Evenson A.R., Warden G.D., and Hasselgren P.O. Protein breakdown in muscle from burned rats is blocked by insulin-like growth factor I and glycogen synthase kinase-3beta inhibitors. Endocrinology 146 (2005) 3141-3149
    • (2005) Endocrinology , vol.146 , pp. 3141-3149
    • Fang, C.H.1    Li, B.G.2    James, J.H.3    King, J.K.4    Evenson, A.R.5    Warden, G.D.6    Hasselgren, P.O.7
  • 12
    • 34447644976 scopus 로고    scopus 로고
    • Protein kinase B/Akt: a nexus of growth factor and cytokine signaling in determining muscle mass
    • Frost R.A., and Lang C.H. Protein kinase B/Akt: a nexus of growth factor and cytokine signaling in determining muscle mass. J. Appl. Physiol. 103 (2007) 378-387
    • (2007) J. Appl. Physiol. , vol.103 , pp. 378-387
    • Frost, R.A.1    Lang, C.H.2
  • 14
    • 45649084226 scopus 로고    scopus 로고
    • Adrenaline potentiates insulin-stimulated PKB activation in the rat fast-twitch epitrochlearis muscle without affecting IRS-1-associated PI 3-kinase activity
    • Jensen J., Grønning-Wang L.M., Jebens E., Whitehead J.P., Zorec R., and Shepherd P.R. Adrenaline potentiates insulin-stimulated PKB activation in the rat fast-twitch epitrochlearis muscle without affecting IRS-1-associated PI 3-kinase activity. Pflugers Arch. 456 (2008) 969-978
    • (2008) Pflugers Arch. , vol.456 , pp. 969-978
    • Jensen, J.1    Grønning-Wang, L.M.2    Jebens, E.3    Whitehead, J.P.4    Zorec, R.5    Shepherd, P.R.6
  • 16
    • 33846885682 scopus 로고    scopus 로고
    • Rapamycin inhibits the growth and muscle-sparing effects of clenbuterol
    • Kline W.O., Panaro F.J., Yang H., and Bodine S.C. Rapamycin inhibits the growth and muscle-sparing effects of clenbuterol. J. Appl. Physiol. 102 (2007) 740-747
    • (2007) J. Appl. Physiol. , vol.102 , pp. 740-747
    • Kline, W.O.1    Panaro, F.J.2    Yang, H.3    Bodine, S.C.4
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 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 (2001) 551-558
    • (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
  • 20
    • 42049097879 scopus 로고    scopus 로고
    • Role of beta-adrenoceptor signaling in skeletal muscle: implications for muscle wasting and disease
    • Lynch G.S., and Ryall J.G. Role of beta-adrenoceptor signaling in skeletal muscle: implications for muscle wasting and disease. Physiol. Rev. 88 (2008) 729-767
    • (2008) Physiol. Rev. , vol.88 , pp. 729-767
    • Lynch, G.S.1    Ryall, J.G.2
  • 22
    • 0037192820 scopus 로고    scopus 로고
    • Differential signaling of cyclic AMP: opposing effects of exchange protein directly activated by cyclic AMP and cAMP-dependent protein kinase on protein kinase B activation
    • Mei F.C., Qiao J., Tsygankova O.M., Meinkoth J.L., Quilliam L.A., and Cheng X. Differential signaling of cyclic AMP: opposing effects of exchange protein directly activated by cyclic AMP and cAMP-dependent protein kinase on protein kinase B activation. J. Biol. Chem. 277 (2002) 11497-11504
    • (2002) J. Biol. Chem. , vol.277 , pp. 11497-11504
    • Mei, F.C.1    Qiao, J.2    Tsygankova, O.M.3    Meinkoth, J.L.4    Quilliam, L.A.5    Cheng, X.6
  • 23
    • 0031607382 scopus 로고    scopus 로고
    • Overview of the effects of beta-adrenergic receptor agonists on animal growth including mechanisms of action
    • Mersmann H.J. Overview of the effects of beta-adrenergic receptor agonists on animal growth including mechanisms of action. J. Anim. Sci. 76 (1998) 160-172
    • (1998) J. Anim. Sci. , vol.76 , pp. 160-172
    • Mersmann, H.J.1
  • 25
    • 33644688682 scopus 로고    scopus 로고
    • Coordinate regulation of forskolin-induced cellular proliferation in macrophages by PKA-CREB and Epac1-Rap1 signaling: effects of silencing CREB gene expression on AKT activation
    • Misra U.K., and Pizzo S.V. Coordinate regulation of forskolin-induced cellular proliferation in macrophages by PKA-CREB and Epac1-Rap1 signaling: effects of silencing CREB gene expression on AKT activation. J. Biol. Chem. 280 (2005) 38276-38289
    • (2005) J. Biol. Chem. , vol.280 , pp. 38276-38289
    • Misra, U.K.1    Pizzo, S.V.2
  • 26
    • 0033060435 scopus 로고    scopus 로고
    • Evaluation of signals activating ubiquitin-proteasome proteolysis in a model of muscle wasting
    • Mitch W.E., Bailey J.L., Wang X., Jurkovitz C., Newby D., and Price S.R. Evaluation of signals activating ubiquitin-proteasome proteolysis in a model of muscle wasting. Am. J. Physiol. 276 (1999) C1132-C1138
    • (1999) Am. J. Physiol. , vol.276
    • Mitch, W.E.1    Bailey, J.L.2    Wang, X.3    Jurkovitz, C.4    Newby, D.5    Price, S.R.6
  • 27
    • 23944480371 scopus 로고    scopus 로고
    • Molecular determinants of skeletal muscle mass: getting the "AKT" together
    • Nader G.A. Molecular determinants of skeletal muscle mass: getting the "AKT" together. Int. J. Biochem. Cell Biol. 37 (2005) 1985-1996
    • (2005) Int. J. Biochem. Cell Biol. , vol.37 , pp. 1985-1996
    • Nader, G.A.1
  • 31
    • 0032756854 scopus 로고    scopus 로고
    • Effect of guanethidine-induced adrenergic blockade on the different proteolytic systems in rat skeletal muscle
    • Navegantes L.C., Resano N.M., Migliorini R.H., and Kettelhut I.C. Effect of guanethidine-induced adrenergic blockade on the different proteolytic systems in rat skeletal muscle. Am. J. Physiol. Endocrinol. Metab. 277 (1999) E883-E889
    • (1999) Am. J. Physiol. Endocrinol. Metab. , vol.277
    • Navegantes, L.C.1    Resano, N.M.2    Migliorini, R.H.3    Kettelhut, I.C.4
  • 32
  • 33
    • 0034652203 scopus 로고    scopus 로고
    • Effects of epinephrine infusion on expression of calpastatin in porcine cardiac and skeletal muscle
    • Parr T., Sensky P.L., Arnold M.K., Bardsley R.G., and Buttery P.J. Effects of epinephrine infusion on expression of calpastatin in porcine cardiac and skeletal muscle. Arch. Biochem. Biophys. 374 (2000) 299-305
    • (2000) Arch. Biochem. Biophys. , vol.374 , pp. 299-305
    • Parr, T.1    Sensky, P.L.2    Arnold, M.K.3    Bardsley, R.G.4    Buttery, P.J.5
  • 34
  • 38
    • 33750598324 scopus 로고    scopus 로고
    • Effect of anabolic agents on calpastatin promoters in porcine skeletal muscle and their responsiveness to cyclic adenosine monophosphate- and calcium-related stimuli
    • Sensky P.L., Jewell K.K., Ryan K.J., Parr T., Bardsley R.G., and Buttery P.J. Effect of anabolic agents on calpastatin promoters in porcine skeletal muscle and their responsiveness to cyclic adenosine monophosphate- and calcium-related stimuli. J. Anim. Sci. 84 (2006) 2973-2982
    • (2006) J. Anim. Sci. , vol.84 , pp. 2973-2982
    • Sensky, P.L.1    Jewell, K.K.2    Ryan, K.J.3    Parr, T.4    Bardsley, R.G.5    Buttery, P.J.6
  • 39
    • 2042425906 scopus 로고    scopus 로고
    • The IGF-1/PI3K/AKT pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting Foxo transcription factors
    • Stitt T.N., Drujan D., Clarke B.A., Panaro F., Timofeyva Y., Kline W.O., Gonzalez M., Yancopoulos G.D., and Glass D.J. The IGF-1/PI3K/AKT pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting Foxo transcription factors. Mol. Cell 14 (2004) 395-403
    • (2004) Mol. Cell , vol.14 , pp. 395-403
    • Stitt, T.N.1    Drujan, D.2    Clarke, B.A.3    Panaro, F.4    Timofeyva, Y.5    Kline, W.O.6    Gonzalez, M.7    Yancopoulos, G.D.8    Glass, D.J.9
  • 40
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. 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
  • 41
    • 0000569087 scopus 로고
    • A fluorimetric method for the estimation of tyrosine in plasma and tissues
    • Waalkes T.P., and Udenfriend S. A fluorimetric method for the estimation of tyrosine in plasma and tissues. J. Lab. Clin. Med. 50 (1957) 733-736
    • (1957) J. Lab. Clin. Med. , vol.50 , pp. 733-736
    • Waalkes, T.P.1    Udenfriend, S.2
  • 42
    • 0032055131 scopus 로고    scopus 로고
    • Activation of protein kinase B beta and gamma isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro: comparison with protein kinase B alpha
    • Walker K.S., Deak M., Paterson A., Hudson K., Cohen P., and Alessi D.R. Activation of protein kinase B beta and gamma isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro: comparison with protein kinase B alpha. Biochem. J. 331 (1998) 299-308
    • (1998) Biochem. J. , vol.331 , pp. 299-308
    • Walker, K.S.1    Deak, M.2    Paterson, A.3    Hudson, K.4    Cohen, P.5    Alessi, D.R.6
  • 43
    • 33747619854 scopus 로고    scopus 로고
    • Insulin resistance accelerates muscle protein degradation: activation of the ubiquitin-proteasome pathway by defects in muscle cell signaling
    • Wang X., Hu Z., Hu J., Du J., and Mitch W.E. Insulin resistance accelerates muscle protein degradation: activation of the ubiquitin-proteasome pathway by defects in muscle cell signaling. Endocrinology 147 (2006) 4160-4168
    • (2006) Endocrinology , vol.147 , pp. 4160-4168
    • Wang, X.1    Hu, Z.2    Hu, J.3    Du, J.4    Mitch, W.E.5
  • 44
    • 21644478996 scopus 로고    scopus 로고
    • Clenbuterol induces muscle-specific attenuation of atrophy through effects on the ubiquitin-proteasome pathway
    • Yimlamai T., Dodd S.L., Borst S.E., and Park S. Clenbuterol induces muscle-specific attenuation of atrophy through effects on the ubiquitin-proteasome pathway. J. Appl. Physiol. 99 (2005) 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.