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Volumn 14, Issue 3, 2004, Pages 395-403

The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors

Author keywords

[No Author keywords available]

Indexed keywords

GLUCOCORTICOID; MUTANT PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; PROTEIN MAFBX; PROTEIN MURF1; SOMATOMEDIN BINDING PROTEIN; TRANSCRIPTION FACTOR; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 2042425906     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1097-2765(04)00211-4     Document Type: Article
Times cited : (1596)

References (35)
  • 1
    • 0031965872 scopus 로고    scopus 로고
    • Localized infusion of IGF-I results in skeletal muscle hypertrophy in rats
    • Adams G.R., McCue S.A. Localized infusion of IGF-I results in skeletal muscle hypertrophy in rats. J. Appl. Physiol. 84:1998;1716-1722
    • (1998) J. Appl. Physiol. , vol.84 , pp. 1716-1722
    • Adams, G.R.1    McCue, S.A.2
  • 4
    • 0037416153 scopus 로고    scopus 로고
    • FKHR (FOXO1a) is required for myotube fusion of primary mouse myoblasts
    • Bois P.R., Grosveld G.C. FKHR (FOXO1a) is required for myotube fusion of primary mouse myoblasts. EMBO J. 22:2003;1147-1157
    • (2003) EMBO J. , vol.22 , pp. 1147-1157
    • Bois, P.R.1    Grosveld, G.C.2
  • 6
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley L.C. The phosphoinositide 3-kinase pathway. Science. 296:2002;1655-1657
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 7
    • 0036387193 scopus 로고    scopus 로고
    • Forkhead transcription factors: Key players in development and metabolism
    • Carlsson P., Mahlapuu M. Forkhead transcription factors. key players in development and metabolism Dev. Biol. 250:2002;1-23
    • (2002) Dev. Biol. , vol.250 , pp. 1-23
    • Carlsson, P.1    Mahlapuu, M.2
  • 8
    • 0029040848 scopus 로고
    • Myogenic vector expression of insulin-like growth factor I stimulates muscle cell differentiation and myofiber hypertrophy in transgenic mice
    • Coleman M.E., DeMayo F., Yin K.C., Lee H.M., Geske R., Montgomery C., Schwartz R.J. Myogenic vector expression of insulin-like growth factor I stimulates muscle cell differentiation and myofiber hypertrophy in transgenic mice. J. Biol. Chem. 270:1995;12109-12116
    • (1995) J. Biol. Chem. , vol.270 , pp. 12109-12116
    • Coleman, M.E.1    Demayo, F.2    Yin, K.C.3    Lee, H.M.4    Geske, R.5    Montgomery, C.6    Schwartz, R.J.7
  • 9
    • 0029587224 scopus 로고
    • Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B
    • Cross D.A., Alessi D.R., Cohen P., Andjelkovich M., Hemmings B.A. Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B. Nature. 378:1995;785-789
    • (1995) Nature , vol.378 , pp. 785-789
    • Cross, D.A.1    Alessi, D.R.2    Cohen, P.3    Andjelkovich, M.4    Hemmings, B.A.5
  • 10
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three Akts
    • Datta S.R., Brunet A., Greenberg M.E. Cellular survival. a play in three Akts Genes Dev. 13:1999;2905-2927
    • (1999) Genes Dev. , vol.13 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 11
    • 0025362896 scopus 로고
    • Activation of insulin-like growth factor gene expression during work-induced skeletal muscle growth
    • DeVol D.L., Rotwein P., Sadow J.L., Novakofski J., Bechtel P.J. Activation of insulin-like growth factor gene expression during work-induced skeletal muscle growth. Am. J. Physiol. 259:1990;E89-E95
    • (1990) Am. J. Physiol. , vol.259 , pp. 89-E95
    • Devol, D.L.1    Rotwein, P.2    Sadow, J.L.3    Novakofski, J.4    Bechtel, P.J.5
  • 12
    • 0034733634 scopus 로고    scopus 로고
    • Glucocorticoids induce proteasome C3 subunit expression in L6 muscle cells by opposing the suppression of its transcription by NF-kappa B
    • Du J., Mitch W.E., Wang X., Price S.R. Glucocorticoids induce proteasome C3 subunit expression in L6 muscle cells by opposing the suppression of its transcription by NF-kappa B. J. Biol. Chem. 275:2000;19661-19666
    • (2000) J. Biol. Chem. , vol.275 , pp. 19661-19666
    • Du, J.1    Mitch, W.E.2    Wang, X.3    Price, S.R.4
  • 13
    • 0029907306 scopus 로고    scopus 로고
    • Growth hormone and the insulin-like growth factor system in myogenesis
    • Florini J.R., Ewton D.Z., Coolican S.A. Growth hormone and the insulin-like growth factor system in myogenesis. Endocr. Rev. 17:1996;481-517
    • (1996) Endocr. Rev. , vol.17 , pp. 481-517
    • Florini, J.R.1    Ewton, D.Z.2    Coolican, S.A.3
  • 14
    • 0037318822 scopus 로고    scopus 로고
    • Signalling pathways that mediate skeletal muscle hypertrophy and atrophy
    • Glass D.J. Signalling pathways that mediate skeletal muscle hypertrophy and atrophy. Nat. Cell Biol. 5:2003;87-90
    • (2003) Nat. Cell Biol. , vol.5 , pp. 87-90
    • Glass, D.J.1
  • 15
    • 0020660874 scopus 로고
    • Protein turnover measured in vivo and in vitro in muscles undergoing compensatory growth and subsequent denervation atrophy
    • Goldspink D.F., Garlick P.J., McNurlan M.A. Protein turnover measured in vivo and in vitro in muscles undergoing compensatory growth and subsequent denervation atrophy. Biochem. J. 210:1983;89-98
    • (1983) Biochem. J. , vol.210 , pp. 89-98
    • Goldspink, D.F.1    Garlick, P.J.2    McNurlan, M.A.3
  • 18
    • 0028899142 scopus 로고
    • Effects of dexamethasone on protein degradation and protease gene expression in rat L8 myotube cultures
    • Hong D.H., Forsberg N.E. Effects of dexamethasone on protein degradation and protease gene expression in rat L8 myotube cultures. Mol. Cell. Endocrinol. 108:1995;199-209
    • (1995) Mol. Cell. Endocrinol. , vol.108 , pp. 199-209
    • Hong, D.H.1    Forsberg, N.E.2
  • 19
    • 0042477748 scopus 로고    scopus 로고
    • Regulation of insulin-like growth factor-dependent myoblast differentiation by Foxo forkhead transcription factors
    • Hribal M.L., Nakae J., Kitamura T., Shutter J.R., Accili D. Regulation of insulin-like growth factor-dependent myoblast differentiation by Foxo forkhead transcription factors. J. Cell Biol. 162:2003;535-541
    • (2003) J. Cell Biol. , vol.162 , pp. 535-541
    • Hribal, M.L.1    Nakae, J.2    Kitamura, T.3    Shutter, J.R.4    Accili, D.5
  • 20
    • 0035350530 scopus 로고    scopus 로고
    • What do we really know about the ubiquitin-proteasome pathway in muscle atrophy?
    • Jagoe R.T., Goldberg A.L. What do we really know about the ubiquitin-proteasome pathway in muscle atrophy? Curr. Opin. Clin. Nutr. Metab. Care. 4:2001;183-190
    • (2001) Curr. Opin. Clin. Nutr. Metab. Care , vol.4 , pp. 183-190
    • Jagoe, R.T.1    Goldberg, A.L.2
  • 22
    • 0030593939 scopus 로고    scopus 로고
    • Mechanisms of muscle wasting. The role of the ubiquitin-proteasome pathway
    • Mitch W.E., Goldberg A.L. Mechanisms of muscle wasting. The role of the ubiquitin-proteasome pathway. N. Engl. J. Med. 335:1996;1897-1905
    • (1996) N. Engl. J. Med. , vol.335 , pp. 1897-1905
    • Mitch, W.E.1    Goldberg, A.L.2
  • 25
    • 0033429554 scopus 로고    scopus 로고
    • Mammalian target of rapamycin is a direct target for protein kinase B: Identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation
    • Nave B.T., Ouwens M., Withers D.J., Alessi D.R., Shepherd P.R. Mammalian target of rapamycin is a direct target for protein kinase B. identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation Biochem. J. 344:1999;427-431
    • (1999) Biochem. J. , vol.344 , pp. 427-431
    • Nave, B.T.1    Ouwens, M.2    Withers, D.J.3    Alessi, D.R.4    Shepherd, P.R.5
  • 26
    • 0037047098 scopus 로고    scopus 로고
    • A protein kinase B-dependent and rapamycin-sensitive pathway controls skeletal muscle growth but not fiber type specification
    • Pallafacchina G., Calabria E., Serrano A.L., Kalhovde J.M., Schiaffino S. A protein kinase B-dependent and rapamycin-sensitive pathway controls skeletal muscle growth but not fiber type specification. Proc. Natl. Acad. Sci. USA. 99:2002;9213-9218
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9213-9218
    • Pallafacchina, G.1    Calabria, E.2    Serrano, A.L.3    Kalhovde, J.M.4    Schiaffino, S.5
  • 27
    • 0037123438 scopus 로고    scopus 로고
    • Control of Ser2448 phosphorylation in the mammalian target of rapamycin by insulin and skeletal muscle load
    • Reynolds T.H. 4th, Bodine S.C., Lawrence J.C. Jr. Control of Ser2448 phosphorylation in the mammalian target of rapamycin by insulin and skeletal muscle load. J. Biol. Chem. 277:2002;17657-17662
    • (2002) J. Biol. Chem. , vol.277 , pp. 17657-17662
    • Reynolds IV, T.H.1    Bodine, S.C.2    Lawrence Jr., J.C.3
  • 31
    • 0032545408 scopus 로고    scopus 로고
    • Attenuation of mammalian target of rapamycin activity by increased cAMP in 3T3-L1 adipocytes
    • Scott P.H., Lawrence J.C. Jr. Attenuation of mammalian target of rapamycin activity by increased cAMP in 3T3-L1 adipocytes. J. Biol. Chem. 273:1998;34496-34501
    • (1998) J. Biol. Chem. , vol.273 , pp. 34496-34501
    • Scott, P.H.1    Lawrence Jr., J.C.2
  • 33
    • 0036632368 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase AKT pathway in human cancer
    • Vivanco I., Sawyers C.L. The phosphatidylinositol 3-kinase AKT pathway in human cancer. Nat. Rev. Cancer. 2:2002;489-501
    • (2002) Nat. Rev. Cancer , vol.2 , pp. 489-501
    • Vivanco, I.1    Sawyers, C.L.2
  • 34
    • 0032185015 scopus 로고    scopus 로고
    • Dexamethasone stimulates proteasome- and calcium-dependent proteolysis in cultured L6 myotubes
    • Wang L., Luo G.J., Wang J.J., Hasselgren P.O. Dexamethasone stimulates proteasome- and calcium-dependent proteolysis in cultured L6 myotubes. Shock. 10:1998;298-306
    • (1998) Shock , vol.10 , pp. 298-306
    • Wang, L.1    Luo, G.J.2    Wang, J.J.3    Hasselgren, P.O.4
  • 35
    • 0037401683 scopus 로고    scopus 로고
    • Sepsis upregulates the gene expression of multiple ubiquitin ligases in skeletal muscle
    • Wray C.J., Mammen J.M., Hershko D.D., Hasselgren P.O. Sepsis upregulates the gene expression of multiple ubiquitin ligases in skeletal muscle. Int. J. Biochem. Cell Biol. 35:2003;698-705
    • (2003) Int. J. Biochem. Cell Biol. , vol.35 , pp. 698-705
    • Wray, C.J.1    Mammen, J.M.2    Hershko, D.D.3    Hasselgren, P.O.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.