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Volumn 314, Issue 6, 2008, Pages 1281-1291

Long-term effects of rapamycin treatment on insulin mediated phosphorylation of Akt/PKB and glycogen synthase activity

Author keywords

Akt PKB phosphorylation; Glycogen synthase; HepG2 cells; Insulin; IRS 1; Protein phosphatase 1; Rapamycin

Indexed keywords

GLYCOGEN SYNTHASE; INSULIN; MAMMALIAN TARGET OF RAPAMYCIN; PROTEIN KINASE B; RAPAMYCIN; SERINE;

EID: 40049086403     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2007.12.019     Document Type: Article
Times cited : (7)

References (45)
  • 2
    • 8344281974 scopus 로고    scopus 로고
    • Targeting the molecular target of rapamycin (mTOR)
    • E.K. Rowinsky Targeting the molecular target of rapamycin (mTOR) Curr. Opin. Oncol. 16 2004 564 575
    • (2004) Curr. Opin. Oncol. , vol.16 , pp. 564-575
    • Rowinsky, E.K.1
  • 3
    • 0034644525 scopus 로고    scopus 로고
    • TOR, a central controller of cell growth
    • T. Schmelzle M.N. Hall TOR, a central controller of cell growth Cell 103 2000 253 262
    • (2000) Cell , vol.103 , pp. 253-262
    • Schmelzle, T.1    Hall, M.N.2
  • 4
    • 0033607531 scopus 로고    scopus 로고
    • Immunopurified mammalian target of rapamycin phosphorylates and activates p70 S6 kinase alpha in vitro
    • S. Isotani K. Hara C. Tokunaga H. Inoue J. Avruch K. Yonezawa Immunopurified mammalian target of rapamycin phosphorylates and activates p70 S6 kinase alpha in vitro J. Biol. Chem. 274 1999 34493 34498
    • (1999) J. Biol. Chem. , vol.274 , pp. 34493-34498
    • Isotani, S.1    Hara, K.2    Tokunaga, C.3    Inoue, H.4    Avruch, J.5    Yonezawa, K.6
  • 7
    • 0037623417 scopus 로고    scopus 로고
    • GβL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR
    • D.H. Kim D.D. Sarbassov S.M. Ali R.R. Latek K.V. Guntur H. Erdjument-Bromage P. Tempst D.M. Sabatini GβL, a positive regulator of the rapamycin-sensitive pathway required for the nutrient-sensitive interaction between raptor and mTOR Mol. Cell 11 2003 895 904
    • (2003) Mol. Cell , vol.11 , pp. 895-904
    • Kim, D.H.1    Sarbassov, D.D.2    Ali, S.M.3    Latek, R.R.4    Guntur, K.V.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabatini, D.M.8
  • 10
    • 3342895823 scopus 로고    scopus 로고
    • Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton
    • D.D. Sarbassov S.M. Ali D.H. Kim D.A. Guertin R.R. Latek H. Erdjument-Bromage P. Tempst D.M. Sabatini Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton Curr. Biol. 14 2004 1296 1302
    • (2004) Curr. Biol. , vol.14 , pp. 1296-1302
    • Sarbassov, D.D.1    Ali, S.M.2    Kim, D.H.3    Guertin, D.A.4    Latek, R.R.5    Erdjument-Bromage, H.6    Tempst, P.7    Sabatini, D.M.8
  • 11
    • 33751079895 scopus 로고    scopus 로고
    • Identification of Sin1 as an essential TORC2 component required for complex formation and kinase activity
    • Q. Yang K. Inoki T. Ikenoue K.L. Guan Identification of Sin1 as an essential TORC2 component required for complex formation and kinase activity Genes Dev. 20 2006 2820 2832
    • (2006) Genes Dev. , vol.20 , pp. 2820-2832
    • Yang, Q.1    Inoki, K.2    Ikenoue, T.3    Guan, K.L.4
  • 12
    • 33947330747 scopus 로고    scopus 로고
    • Re-evaluating AKT regulation: role of TOR complex 2 in tissue growth
    • V. Hietakangas S.M. Cohen Re-evaluating AKT regulation: role of TOR complex 2 in tissue growth Genes Dev. 21 2007 632 637
    • (2007) Genes Dev. , vol.21 , pp. 632-637
    • Hietakangas, V.1    Cohen, S.M.2
  • 13
    • 33749076673 scopus 로고    scopus 로고
    • SIN1/MIP1 maintains rictor–mTOR complex integrity and regulates Akt phosphorylation and substrate specificity
    • E. Jacinto V. Facchinetti D. Liu N. Soto S. Wei S.Y. Jung Q. Huang J. Qin B. Su SIN1/MIP1 maintains rictor–mTOR complex integrity and regulates Akt phosphorylation and substrate specificity Cell 127 2006 125 137
    • (2006) Cell , vol.127 , pp. 125-137
    • Jacinto, E.1    Facchinetti, V.2    Liu, D.3    Soto, N.4    Wei, S.5    Jung, S.Y.6    Huang, Q.7    Qin, J.8    Su, B.9
  • 14
    • 13844312400 scopus 로고    scopus 로고
    • Phosphorylation and regulation of Akt/PKB by the rictor–mTOR complex
    • D.D. Sarbassov D.A. Guertin S.M. Ali D.M. Sabatini Phosphorylation and regulation of Akt/PKB by the rictor–mTOR complex Science 307 2005 1098 1101
    • (2005) Science , vol.307 , pp. 1098-1101
    • Sarbassov, D.D.1    Guertin, D.A.2    Ali, S.M.3    Sabatini, D.M.4
  • 15
    • 0031127305 scopus 로고    scopus 로고
    • Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha
    • D.R. Alessi S.R. James C.P. Downes A.B. Holmes P.R. Gaffney C.B. Reese P. Cohen Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha Curr. Biol. 7 1997 261 269
    • (1997) Curr. Biol. , vol.7 , pp. 261-269
    • Alessi, D.R.1    James, S.R.2    Downes, C.P.3    Holmes, A.B.4    Gaffney, P.R.5    Reese, C.B.6    Cohen, P.7
  • 16
    • 14244256097 scopus 로고    scopus 로고
    • Increased activation of the mammalian target of rapamycin pathway in liver and skeletal muscle of obese rats: possible involvement in obesity-linked insulin resistance
    • L. Khamzina A. Veilleux S. Bergeron A. Marette Increased activation of the mammalian target of rapamycin pathway in liver and skeletal muscle of obese rats: possible involvement in obesity-linked insulin resistance Endocrinology 146 2005 1473 1481
    • (2005) Endocrinology , vol.146 , pp. 1473-1481
    • Khamzina, L.1    Veilleux, A.2    Bergeron, S.3    Marette, A.4
  • 17
    • 0032560521 scopus 로고    scopus 로고
    • Evidence of insulin-stimulated phosphorylation and activation of the mammalian target of rapamycin mediated by a protein kinase B signaling pathway
    • P.H. Scott G.J. Brunn A.D. Kohn R.A. Roth J.C. Lawrence Jr. Evidence of insulin-stimulated phosphorylation and activation of the mammalian target of rapamycin mediated by a protein kinase B signaling pathway Proc. Natl. Acad. Sci. 95 1998 7772 7777
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 7772-7777
    • Scott, P.H.1    Brunn, G.J.2    Kohn, A.D.3    Roth, R.A.4    Lawrence, J.C.5
  • 18
    • 0034644523 scopus 로고    scopus 로고
    • Cellular signaling: pivoting around PDK-1
    • A. Toker A.C. Newton Cellular signaling: pivoting around PDK-1 Cell 103 2000 185 188
    • (2000) Cell , vol.103 , pp. 185-188
    • Toker, A.1    Newton, A.C.2
  • 20
    • 0035815649 scopus 로고    scopus 로고
    • Elevated AKT activity protects the prostate cancer cell line LNCaP from TRAIL-induced apoptosis
    • A. Nesterov X. Lu M. Johnson G.J. Miller Y. Ivashchenko A.S. Kraft Elevated AKT activity protects the prostate cancer cell line LNCaP from TRAIL-induced apoptosis J. Biol. Chem. 276 2001 10767 10774
    • (2001) J. Biol. Chem. , vol.276 , pp. 10767-10774
    • Nesterov, A.1    Lu, X.2    Johnson, M.3    Miller, G.J.4    Ivashchenko, Y.5    Kraft, A.S.6
  • 21
    • 0032558822 scopus 로고    scopus 로고
    • Protein kinase B (PKB/Akt) activity is elevated in glioblastoma cells due to mutation of the tumor suppressor PTEN/MMAC
    • D. Haas-Kogan N. Shalev M. Wong G. Mills G. Yount D. Stokoe Protein kinase B (PKB/Akt) activity is elevated in glioblastoma cells due to mutation of the tumor suppressor PTEN/MMAC Curr. Biol. 8 1998 1195 1198
    • (1998) Curr. Biol. , vol.8 , pp. 1195-1198
    • Haas-Kogan, D.1    Shalev, N.2    Wong, M.3    Mills, G.4    Yount, G.5    Stokoe, D.6
  • 22
    • 28644435769 scopus 로고    scopus 로고
    • Elevated phosphorylation and activation of PDK-1/AKT pathway in human breast cancer
    • H.J. Lin F.C. Hsieh H. Song J. Lin Elevated phosphorylation and activation of PDK-1/AKT pathway in human breast cancer Br. J. Cancer 93 2005 1372 1381
    • (2005) Br. J. Cancer , vol.93 , pp. 1372-1381
    • Lin, H.J.1    Hsieh, F.C.2    Song, H.3    Lin, J.4
  • 23
    • 12444279265 scopus 로고
    • On the origin of cancer cells
    • O. Warburg On the origin of cancer cells Science 123 1956 309 314
    • (1956) Science , vol.123 , pp. 309-314
    • Warburg, O.1
  • 24
    • 16644393866 scopus 로고    scopus 로고
    • Effect of overexpression and nuclear translocation of constitutively active PKB-α on cellular survival and proliferation in HepG2 cells
    • D. Gupta N.A. Syed W.J. Roesler R.L. Khandelwal Effect of overexpression and nuclear translocation of constitutively active PKB-α on cellular survival and proliferation in HepG2 cells J. Cell. Biochem. 93 2004 513 525
    • (2004) J. Cell. Biochem. , vol.93 , pp. 513-525
    • Gupta, D.1    Syed, N.A.2    Roesler, W.J.3    Khandelwal, R.L.4
  • 25
    • 0034714239 scopus 로고    scopus 로고
    • Glycogen synthase association with the striated muscle glycogen-targeting subunit of protein phosphatase-1. Synthase activation involves scaffolding regulated by β-adrenergic signaling
    • J. Liu D.L. Brautigan Glycogen synthase association with the striated muscle glycogen-targeting subunit of protein phosphatase-1. Synthase activation involves scaffolding regulated by β-adrenergic signaling J. Biol. Chem. 275 2000 26074 26081
    • (2000) J. Biol. Chem. , vol.275 , pp. 26074-26081
    • Liu, J.1    Brautigan, D.L.2
  • 26
    • 0025877838 scopus 로고
    • Inhibitory effect of okadaic acid on the p-nitrophenyl phosphate phosphatase activity of protein phosphatases
    • A. Takai G. Mieskes Inhibitory effect of okadaic acid on the p -nitrophenyl phosphate phosphatase activity of protein phosphatases Biochem. J. 275 Pt 1 1991 233 239
    • (1991) Biochem. J. , vol.275 , Issue.Pt 1 , pp. 233-239
    • Takai, A.1    Mieskes, G.2
  • 27
    • 85120250102 scopus 로고    scopus 로고
    • H. Towbin, T. Staehelin, J. Gordon, Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. 1979, Biotechnology 24 (1992) 145–149.
  • 28
    • 0015921129 scopus 로고
    • Specificity of activation of glycogen synthase I from skeletal muscle and heart
    • J.A. Thomas K.K. Schlender J. Larner Specificity of activation of glycogen synthase I from skeletal muscle and heart Biochim. Biophys. Acta 293 1973 84 93
    • (1973) Biochim. Biophys. Acta , vol.293 , pp. 84-93
    • Thomas, J.A.1    Schlender, K.K.2    Larner, J.3
  • 29
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein–dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein–dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 30
    • 33845426904 scopus 로고    scopus 로고
    • Effects of rapamycin on cell proliferation and phosphorylation of mTOR and p70(S6K) in HepG2 and HepG2 cells overexpressing constitutively active Akt/PKB
    • S. Varma R.L. Khandelwal Effects of rapamycin on cell proliferation and phosphorylation of mTOR and p70(S6K) in HepG2 and HepG2 cells overexpressing constitutively active Akt/PKB Biochim. Biophys. Acta 1770 2007 71 78
    • (2007) Biochim. Biophys. Acta , vol.1770 , pp. 71-78
    • Varma, S.1    Khandelwal, R.L.2
  • 31
    • 0030951346 scopus 로고    scopus 로고
    • Insulin activates protein kinase B, inhibits glycogen synthase kinase-3 and activates glycogen synthase by rapamycin-insensitive pathways in skeletal muscle and adipose tissue
    • D.A. Cross P.W. Watt M. Shaw J. van der Kaay C.P. Downes J.C. Holder P. Cohen Insulin activates protein kinase B, inhibits glycogen synthase kinase-3 and activates glycogen synthase by rapamycin-insensitive pathways in skeletal muscle and adipose tissue FEBS Lett. 406 1997 211 215
    • (1997) FEBS Lett. , vol.406 , pp. 211-215
    • Cross, D.A.1    Watt, P.W.2    Shaw, M.3    van der Kaay, J.4    Downes, C.P.5    Holder, J.C.6    Cohen, P.7
  • 32
    • 0030721534 scopus 로고    scopus 로고
    • The regulation of glycogen synthase by protein phosphatase 1 in 3T3-L1 adipocytes. Evidence for a potential role for DARPP-32 in insulin action
    • M.J. Brady A.C. Nairn A.R. Saltiel The regulation of glycogen synthase by protein phosphatase 1 in 3T3-L1 adipocytes. Evidence for a potential role for DARPP-32 in insulin action J. Biol. Chem. 272 1997 29698 29703
    • (1997) J. Biol. Chem. , vol.272 , pp. 29698-29703
    • Brady, M.J.1    Nairn, A.C.2    Saltiel, A.R.3
  • 33
    • 0028926498 scopus 로고
    • Stimulation of protein phosphatase-1 activity by insulin in rat adipocytes. Evaluation of the role of mitogen-activated protein kinase pathway
    • N. Begum Stimulation of protein phosphatase-1 activity by insulin in rat adipocytes. Evaluation of the role of mitogen-activated protein kinase pathway J. Biol. Chem. 270 1995 709 714
    • (1995) J. Biol. Chem. , vol.270 , pp. 709-714
    • Begum, N.1
  • 35
    • 23844438209 scopus 로고    scopus 로고
    • Activation of Akt and eIF4E survival pathways by rapamycin-mediated mammalian target of rapamycin inhibition
    • S.Y. Sun L.M. Rosenberg X. Wang Z. Zhou P. Yue H. Fu F.R. Khuri Activation of Akt and eIF4E survival pathways by rapamycin-mediated mammalian target of rapamycin inhibition Cancer Res. 65 2005 7052 7058
    • (2005) Cancer Res. , vol.65 , pp. 7052-7058
    • Sun, S.Y.1    Rosenberg, L.M.2    Wang, X.3    Zhou, Z.4    Yue, P.5    Fu, H.6    Khuri, F.R.7
  • 36
    • 33749040235 scopus 로고    scopus 로고
    • Human cytomegalovirus infection alters the substrate specificities and rapamycin sensitivities of raptor- and rictor-containing complexes
    • S.B. Kudchodkar Y. Yu T.G. Maguire J.C. Alwine Human cytomegalovirus infection alters the substrate specificities and rapamycin sensitivities of raptor- and rictor-containing complexes Proc. Natl. Acad. Sci. U. S. A. 103 2006 14182 14187
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 14182-14187
    • Kudchodkar, S.B.1    Yu, Y.2    Maguire, T.G.3    Alwine, J.C.4
  • 38
    • 34548509880 scopus 로고    scopus 로고
    • PRR5, a novel component of mTOR complex 2, regulates platelet-derived growth factor receptor β expression and signaling
    • S.Y. Woo D.H. Kim C.B. Jun Y.M. Kim E.V. Haar S.I. Lee J.W. Hegg S. Bandhakavi T.J. Griffin PRR5, a novel component of mTOR complex 2, regulates platelet-derived growth factor receptor β expression and signaling J. Biol. Chem. 282 2007 25604 25612
    • (2007) J. Biol. Chem. , vol.282 , pp. 25604-25612
    • Woo, S.Y.1    Kim, D.H.2    Jun, C.B.3    Kim, Y.M.4    Haar, E.V.5    Lee, S.I.6    Hegg, J.W.7    Bandhakavi, S.8    Griffin, T.J.9
  • 39
    • 33845968034 scopus 로고    scopus 로고
    • Functional studies of Akt isoform specificity in skeletal muscle in vivo; maintained insulin sensitivity despite reduced insulin receptor substrate-1 expression
    • M.E. Cleasby T.A. Reinten G.J. Cooney D.E. James E.W. Kraegen Functional studies of Akt isoform specificity in skeletal muscle in vivo ; maintained insulin sensitivity despite reduced insulin receptor substrate-1 expression Mol. Endocrinol. 21 2007 215 228
    • (2007) Mol. Endocrinol. , vol.21 , pp. 215-228
    • Cleasby, M.E.1    Reinten, T.A.2    Cooney, G.J.3    James, D.E.4    Kraegen, E.W.5
  • 40
    • 0016238505 scopus 로고
    • Regulation of rat liver glycogen synthetase. Evidence for a lysyl residue essential for glucose 6-phosphate activation
    • M.J. Ernest K.H. Kim Regulation of rat liver glycogen synthetase. Evidence for a lysyl residue essential for glucose 6-phosphate activation J. Biol. Chem. 249 1974 6770 6778
    • (1974) J. Biol. Chem. , vol.249 , pp. 6770-6778
    • Ernest, M.J.1    Kim, K.H.2
  • 41
    • 0017115658 scopus 로고
    • Evidence for the coordinate control of activity of liver glycogen synthase and phosphorylase by a single protein phosphatase
    • S.D. Killilea H. Brandt E.Y. Lee W.J. Whelan Evidence for the coordinate control of activity of liver glycogen synthase and phosphorylase by a single protein phosphatase J. Biol. Chem. 251 1976 2363 2368
    • (1976) J. Biol. Chem. , vol.251 , pp. 2363-2368
    • Killilea, S.D.1    Brandt, H.2    Lee, E.Y.3    Whelan, W.J.4
  • 43
    • 0038521284 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase-mediated reduction of insulin receptor substrate-1/2 protein expression via different mechanisms contributes to the insulin-induced desensitization of its signaling pathways in L6 muscle cells
    • L. Pirola S. Bonnafous A.M. Johnston C. Chaussade F. Portis E. Van Obberghen Phosphoinositide 3-kinase-mediated reduction of insulin receptor substrate-1/2 protein expression via different mechanisms contributes to the insulin-induced desensitization of its signaling pathways in L6 muscle cells J. Biol. Chem. 278 2003 15641 15651
    • (2003) J. Biol. Chem. , vol.278 , pp. 15641-15651
    • Pirola, L.1    Bonnafous, S.2    Johnston, A.M.3    Chaussade, C.4    Portis, F.5    Van Obberghen, E.6
  • 44
    • 33947684764 scopus 로고    scopus 로고
    • Rapamycin induces feedback activation of Akt signaling through an IGF-1R-dependent mechanism
    • X. Wan B. Harkavy N. Shen P. Grohar L.J. Helman Rapamycin induces feedback activation of Akt signaling through an IGF-1R-dependent mechanism Oncogene 2006
    • (2006) Oncogene
    • Wan, X.1    Harkavy, B.2    Shen, N.3    Grohar, P.4    Helman, L.J.5
  • 45
    • 27644534999 scopus 로고    scopus 로고
    • Mammalian target of rapamycin inhibitors activate the AKT kinase in multiple myeloma cells by up-regulating the insulin-like growth factor receptor/insulin receptor substrate-1/phosphatidylinositol 3-kinase cascade
    • Y. Shi H. Yan P. Frost J. Gera A. Lichtenstein Mammalian target of rapamycin inhibitors activate the AKT kinase in multiple myeloma cells by up-regulating the insulin-like growth factor receptor/insulin receptor substrate-1/phosphatidylinositol 3-kinase cascade Mol. Cancer Ther. 4 2005 1533 1540
    • (2005) Mol. Cancer Ther. , vol.4 , pp. 1533-1540
    • Shi, Y.1    Yan, H.2    Frost, P.3    Gera, J.4    Lichtenstein, A.5


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