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Volumn 296, Issue 4, 2009, Pages

Protein kinase B activity is required for the effects of insulin on lipid metabolism in adipocytes

Author keywords

Acetyl coenzyme A carboxylase; Adenosine 5 monophosphate activated protein kinase; Akt; Lipogenesis; Phosphodiesterase 3B

Indexed keywords

ACETYL COENZYME A CARBOXYLASE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE KINASE; INSULIN; INSULIN RECEPTOR; INSULIN RECEPTOR SUBSTRATE 1; LIPID; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHODIESTERASE III; PROTEIN KINASE B; MITOGEN ACTIVATED PROTEIN KINASE; PDE3B PROTEIN, MOUSE; PROTEIN KINASE INHIBITOR;

EID: 65649091377     PISSN: 01931849     EISSN: 15221555     Source Type: Journal    
DOI: 10.1152/ajpendo.90596.2008     Document Type: Article
Times cited : (102)

References (56)
  • 1
    • 0035970805 scopus 로고    scopus 로고
    • Continuous fatty acid oxidation and reduced fat storage in mice lacking acetyl-coa carboxylase 2
    • DOI 10.1126/science.1056843
    • Abu-Elheiga L, Matzuk MM, Abo-Hashema KA, Wakil SJ. Continuous fatty acid oxidation and reduced fat storage in mice lacking acetyl-CoA carboxylase 2. Science 291: 2613-2616, 2001. (Pubitemid 32249687)
    • (2001) Science , vol.291 , Issue.5513 , pp. 2613-2616
    • Abu-Elheiga, L.1    Matzuk, M.M.2    Abo-Hashema, K.A.H.3    Wakil, S.J.4
  • 2
    • 0034192086 scopus 로고    scopus 로고
    • Cyclic nucleotide phosphodiesterase 3B is a downstream target of protein kinase B and may be involved in regulation of effects of protein kinase B on thymidine incorporation in FDCP2 cells
    • Ahmad F, Cong LN, Stenson Holst L, Wang LM, Rahn Landström T, Pierce JH, Quon MJ, Degerman E, Manganiello VC. Cyclic nucleotide phosphodiesterase 3B is a downstream target of protein kinase B and may be involved in regulation of effects of protein kinase B on thymidine incorporation in FDCP2 cells. J Immunol 164: 4678-4688, 2000. (Pubitemid 30238068)
    • (2000) Journal of Immunology , vol.164 , Issue.9 , pp. 4678-4688
    • Ahmad, F.1    Cong, L.-N.2    Holst, L.S.3    Wang, L.-M.4    Landstrom, T.R.5    Pierce, J.H.6    Quon, M.J.7    Degerman, E.8    Manganiello, V.C.9
  • 3
    • 34249807012 scopus 로고    scopus 로고
    • Insulin-induced formation of macromolecular complexes involved in activation of cyclic nucleotide phosphodiesterase 3B (PDE3B) and its interaction with PKB
    • DOI 10.1042/BJ20060960
    • Ahmad F, Lindh R, Tang Y, Weston M, Degerman E, Manganiello VC. Insulin-induced formation of macromolecular complexes involved in activation of cyclic nucleotide phosphodiesterase 3B (PDE3B) and its interaction with PKB. Biochem J 404: 257-268, 2007. (Pubitemid 46849597)
    • (2007) Biochemical Journal , vol.404 , Issue.2 , pp. 257-268
    • Ahmad, F.1    Lindh, R.2    Tang, Y.3    Weston, M.4    Degerman, E.5    Manganiello, V.C.6
  • 5
    • 0031127305 scopus 로고    scopus 로고
    • Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα
    • Alessi DR, James SR, Downes CP, Holmes AB, Gaffney PR, Reese CB, Cohen P. Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Balpha. Curr Biol 7: 261-269, 1997. (Pubitemid 27176852)
    • (1997) Current Biology , vol.7 , Issue.4 , pp. 261-269
    • Alessi, D.R.1    James, S.R.2    Downes, C.P.3    Holmes, A.B.4    Gaffney, P.R.J.5    Reese, C.B.6    Cohen, P.7
  • 6
    • 0032563091 scopus 로고    scopus 로고
    • Protein kinase B/Akt induces resumption of meiosis in Xenopus oocytes
    • DOI 10.1074/jbc.273.30.18705
    • Andersen CB, Roth RA, Conti M. Protein kinase B/Akt induces resumption of meiosis in Xenopus oocytes. J Biol Chem 273: 18705-18708, 1998. (Pubitemid 28366252)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.30 , pp. 18705-18708
    • Andersen, C.B.1    Roth, R.A.2    Conti, M.3
  • 8
    • 0032512587 scopus 로고    scopus 로고
    • Protein kinase C modulates the insulin-stimulated increase in Akt1 and Akt3 activity in 3T3-L1 adipocytes
    • DOI 10.1006/bbrc.1998.8134
    • Barthel A, Nakatani K, Dandekar AA, Roth RA. Protein kinase C modulates the insulin-stimulated increase in Akt1 and Akt3 activity in 3T3L1 adipocytes. Biochem Biophys Res Commun 243: 509-513, 1998. (Pubitemid 28414055)
    • (1998) Biochemical and Biophysical Research Communications , vol.243 , Issue.2 , pp. 509-513
    • Barthel, A.1    Nakatani, K.2    Dandekar, A.A.3    Roth, R.A.4
  • 9
    • 0037072780 scopus 로고    scopus 로고
    • The identification of ATP-citrate lyase as a protein kinase B (Akt) substrate in primary adipocytes
    • Berwick DC, Hers I, Heesom KJ, Moule SK, Tavare JM. The identification of ATP-citrate lyase as a protein kinase B (Akt) substrate in primary adipocytes. J Biol Chem 277: 33895-33900, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 33895-33900
    • Berwick, D.C.1    Hers, I.2    Heesom, K.J.3    Moule, S.K.4    Tavare, J.M.5
  • 10
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254, 1976.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 11
    • 2342565881 scopus 로고    scopus 로고
    • Advances in protein kinase B signalling: AKTion on multiple fronts
    • Brazil DP, Yang ZZ, Hemmings BA. Advances in protein kinase B signalling: AKTion on multiple fronts. Trends Biochem Sci 29: 233-242, 2004.
    • (2004) Trends Biochem Sci , vol.29 , pp. 233-242
    • Brazil, D.P.1    Yang, Z.Z.2    Hemmings, B.A.3
  • 13
    • 0032752063 scopus 로고    scopus 로고
    • Cellular survival: A play in three Akts
    • Datta SR, Brunet A, Greenberg ME. Cellular survival: a play in three Akts. Genes Dev 13: 2905-2927, 1999.
    • (1999) Genes Dev , vol.13 , pp. 2905-2927
    • Datta, S.R.1    Brunet, A.2    Greenberg, M.E.3
  • 14
    • 0025192341 scopus 로고
    • Location and function of three sites phosphorylated on rat acetyl-CoA carboxylase by the AMP-activated protein kinase
    • Davies SP, Sim AT, Hardie DG. Location and function of three sites phosphorylated on rat acetyl-CoA carboxylase by the AMP-activated protein kinase. Eur J Biochem 187: 183-190, 1990.
    • (1990) Eur J Biochem , vol.187 , pp. 183-190
    • Davies, S.P.1    Sim, A.T.2    Hardie, D.G.3
  • 17
    • 0021822478 scopus 로고
    • Antilipolytic action of insulin: Role of cAMP phosphodiesterase activation
    • Elks ML, Manganiello VC. Antilipolytic action of insulin: role of cAMP phosphodiesterase activation. Endocrinology 116: 2119-2121, 1985.
    • (1985) Endocrinology , vol.116 , pp. 2119-2121
    • Elks, M.L.1    Manganiello, V.C.2
  • 19
    • 0034988819 scopus 로고    scopus 로고
    • 632 in human insulin receptor substrate-1 are important for full activation of insulin-stimulated phosphatidylinositol 3-kinase activity and translocation of GLUT4 in adipose cells
    • DOI 10.1210/en.142.7.2833
    • Esposito DL, Li Y, Cama A, Quon MJ. Tyr612 and Tyr632 in human insulin receptor substrate-1 are important for full activation of insulin-stimulated phosphatidylinositol 3-kinase activity and translocation of GLUT4 in adipose cells. Endocrinology 142: 2833-2840, 2001. (Pubitemid 32575518)
    • (2001) Endocrinology , vol.142 , Issue.7 , pp. 2833-2840
    • Esposito, D.L.1    Li, Y.2    Cama, A.3    Quon, M.J.4
  • 20
    • 33748752150 scopus 로고    scopus 로고
    • 5-Aminoimidazole-4-carboxamide-1-β-D-ribofuranoside-induced AMP-activated protein kinase phosphorylation inhibits basal and insulin-stimulated glucose uptake, lipid synthesis, and fatty acid oxidation in isolated rat adipocytes
    • DOI 10.1074/jbc.M602992200
    • Gaidhu MP, Fediuc S, Ceddia RB. 5-Aminoimidazole-4-carboxamide-1-beta-D- ribofuranoside-induced AMP-activated protein kinase phosphorylation inhibits basal and insulin-stimulated glucose uptake, lipid synthesis, and fatty acid oxidation in isolated rat adipocytes. J Biol Chem 281: 25956-25964, 2006. (Pubitemid 44401801)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.36 , pp. 25956-25964
    • Gaidhu, M.P.1    Fediuc, S.2    Ceddia, R.B.3
  • 21
    • 47749085114 scopus 로고    scopus 로고
    • AMP-activated protein kinase is activated as a consequence of lipolysis in the adipocyte: Potential mechanism and physiological relevance
    • Gauthier MS, Miyoshi H, Souza SC, Cacicedo JM, Saha AK, Greenberg AS, Ruderman NB. AMP-activated protein kinase is activated as a consequence of lipolysis in the adipocyte: potential mechanism and physiological relevance. J Biol Chem 283: 16514-16524, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 16514-16524
    • Gauthier, M.S.1    Miyoshi, H.2    Souza, S.C.3    Cacicedo, J.M.4    Saha, A.K.5    Greenberg, A.S.6    Ruderman, N.B.7
  • 22
    • 33749489511 scopus 로고    scopus 로고
    • Insulin signaling diverges into Akt-dependent and -independent signals to regulate the recruitment/docking and the fusion of GLUT4 vesicles to the plasma membrane
    • DOI 10.1091/mbc.E06-07-0585
    • Gonzalez E, McGraw TE. Insulin signaling diverges into Akt-dependent and -independent signals to regulate the recruitment/docking and the fusion of GLUT4 vesicles to the plasma membrane. Mol Biol Cell 17: 4484-4493, 2006. (Pubitemid 44522065)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.10 , pp. 4484-4493
    • Gonzalez, E.1    McGraw, T.E.2
  • 23
    • 55549088220 scopus 로고    scopus 로고
    • Use of Akt inhibitor and a drug-resistant mutant validates a critical role for protein kinase B/Akt in the insulin-dependent regulation of glucose and system a amino acid uptake
    • Green CJ, Goransson O, Kular GS, Leslie NR, Gray A, Alessi DR, Sakamoto K, Hundal HS. Use of Akt inhibitor and a drug-resistant mutant validates a critical role for protein kinase B/Akt in the insulin-dependent regulation of glucose and system A amino acid uptake. J Biol Chem 283: 27653-27667, 2008.
    • (2008) J Biol Chem , vol.283 , pp. 27653-27667
    • Green, C.J.1    Goransson, O.2    Kular, G.S.3    Leslie, N.R.4    Gray, A.5    Alessi, D.R.6    Sakamoto, K.7    Hundal, H.S.8
  • 25
    • 0015594233 scopus 로고
    • Insulin and the regulation of adipose tissue acetyl-coenzyme a carboxylase
    • Halestrap AP, Denton RM. Insulin and the regulation of adipose tissue acetyl-coenzyme A carboxylase. Biochem J 132: 509-517, 1973.
    • (1973) Biochem J , vol.132 , pp. 509-517
    • Halestrap, A.P.1    Denton, R.M.2
  • 26
    • 0023712662 scopus 로고
    • Analysis of sites phosphorylated on acetyl-CoA carboxylase in response to insulin in isolated adipocytes. Comparison with sites phosphorylated by casein kinase-2 and the calmodulin-dependent multiprotein kinase
    • Haystead TA, Campbell DG, Hardie DG. Analysis of sites phosphorylated on acetyl-CoA carboxylase in response to insulin in isolated adipocytes. Comparison with sites phosphorylated by casein kinase-2 and the calmodulin-dependent multiprotein kinase. Eur J Biochem 175: 347-354, 1988.
    • (1988) Eur J Biochem , vol.175 , pp. 347-354
    • Haystead, T.A.1    Campbell, D.G.2    Hardie, D.G.3
  • 27
    • 0033826850 scopus 로고    scopus 로고
    • Molecular mechanisms regulating hormone-sensitive lipase and lipolysis
    • Holm C, Osterlund T, Laurell H, Contreras JA. Molecular mechanisms regulating hormone-sensitive lipase and lipolysis. Annu Rev Nutr 20: 365-393, 2000.
    • (2000) Annu Rev Nutr , vol.20 , pp. 365-393
    • Holm, C.1    Osterlund, T.2    Laurell, H.3    Contreras, J.A.4
  • 29
    • 28844434558 scopus 로고    scopus 로고
    • 473 kinase for Akt/protein kinase B in 3T3-L1 adipocytes
    • DOI 10.1074/jbc.M508361200
    • Hresko RC, Mueckler M. mTOR RICTOR is the Ser473 kinase for Akt/protein kinase B in 3T3L1 adipocytes. J Biol Chem 280: 40406-40416, 2005. (Pubitemid 41780527)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.49 , pp. 40406-40416
    • Hresko, R.C.1    Mueckler, M.2
  • 30
    • 34547959389 scopus 로고    scopus 로고
    • PI3Kγ is required for PDE4, not PDE3, activity in subcellular microdomains containing the sarcoplasmic reticular calcium ATPase in cardiomyocytes
    • DOI 10.1161/CIRCRESAHA.107.156422, PII 0000301220070817000012
    • Kerfant BG, Zhao D, Lorenzen-Schmidt I, Wilson LS, Cai S, Chen SR, Maurice DH, Backx PH. PI3Kgamma is required for PDE4, not PDE3, activity in subcellular microdomains containing the sarcoplasmic reticular calcium ATPase in cardiomyocytes. Circ Res 101: 400-408, 2007. (Pubitemid 47267708)
    • (2007) Circulation Research , vol.101 , Issue.4 , pp. 400-408
    • Kerfant, B.-G.1    Zhao, D.2    Lorenzen-Schmidt, I.3    Wilson, L.S.4    Cai, S.5    Chen, S.R.W.6    Maurice, D.H.7    Backx, P.H.8
  • 31
    • 0030795278 scopus 로고    scopus 로고
    • Regulation of mammalian acetyl-coenzyme a carboxylase
    • Kim KH. Regulation of mammalian acetyl-coenzyme A carboxylase. Annu Rev Nutr 17: 77-99, 1997.
    • (1997) Annu Rev Nutr , vol.17 , pp. 77-99
    • Kim, K.H.1
  • 33
    • 0029908016 scopus 로고    scopus 로고
    • Expression of a constitutively active Akt Ser/Thr kinase in 3T3L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation
    • Kohn AD, Summers SA, Birnbaum MJ, Roth RA. Expression of a constitutively active Akt Ser/Thr kinase in 3T3L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation. J Biol Chem 271: 31372-31378, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 31372-31378
    • Kohn, A.D.1    Summers, S.A.2    Birnbaum, M.J.3    Roth, R.A.4
  • 34
    • 0028799420 scopus 로고
    • Molecular cloning and characterization of a new member of the RAC protein kinase family: Association of the pleckstrin homology domain of three types of RAC protein kinase with protein kinase C subspecies and beta gamma subunits of G proteins
    • Konishi H, Kuroda S, Tanaka M, Matsuzaki H, Ono Y, Kameyama K, Haga T, Kikkawa U. Molecular cloning and characterization of a new member of the RAC protein kinase family: association of the pleckstrin homology domain of three types of RAC protein kinase with protein kinase C subspecies and beta gamma subunits of G proteins. Biochem Biophys Res Commun 216: 526-534, 1995.
    • (1995) Biochem Biophys Res Commun , vol.216 , pp. 526-534
    • Konishi, H.1    Kuroda, S.2    Tanaka, M.3    Matsuzaki, H.4    Ono, Y.5    Kameyama, K.6    Haga, T.7    Kikkawa, U.8
  • 35
  • 36
    • 0022412012 scopus 로고
    • Effect of insulin on association of acetyl CoA carboxylase phosphatase and acetyl CoA carboxylase
    • Krakower GR, Kim KH. Effect of insulin on association of acetyl CoA carboxylase phosphatase and acetyl CoA carboxylase. Biochem Biophys Res Commun 130: 814-820, 1985.
    • (1985) Biochem Biophys Res Commun , vol.130 , pp. 814-820
    • Krakower, G.R.1    Kim, K.H.2
  • 38
    • 34548453703 scopus 로고    scopus 로고
    • Characterization of a protein kinase B inhibitor in vitro and in insulin-treated liver cells
    • DOI 10.2337/db07-0343
    • Logie L, Ruiz-Alcaraz AJ, Keane M, Woods YL, Bain J, Marquez R, Alessi DR, Sutherland C. Characterization of a protein kinase B inhibitor in vitro and in insulin-treated liver cells. Diabetes 56: 2218-2227, 2007. (Pubitemid 47358228)
    • (2007) Diabetes , vol.56 , Issue.9 , pp. 2218-2227
    • Logie, L.1    Ruiz-Alcaraz, A.J.2    Keane, M.3    Woods, Y.L.4    Bain, J.5    Marquez, R.6    Alessi, D.R.7    Sutherland, C.8
  • 40
    • 0025237826 scopus 로고
    • Acute hormonal control of acetyl-CoA carboxylase. The roles of insulin, glucagon, and epinephrine
    • Mabrouk GM, Helmy IM, Thampy KG, Wakil SJ. Acute hormonal control of acetyl-CoA carboxylase. The roles of insulin, glucagon, and epinephrine. J Biol Chem 265: 6330-6338, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 6330-6338
    • Mabrouk, G.M.1    Helmy, I.M.2    Thampy, K.G.3    Wakil, S.J.4
  • 41
    • 0015217665 scopus 로고
    • Effects of lipolytic and antilipolytic agents on cyclic 3′,5′-adenosine monophosphate in fat cells
    • Manganiello VC, Murad F, Vaughan M. Effects of lipolytic and antilipolytic agents on cyclic 3′,5′-adenosine monophosphate in fat cells. J Biol Chem 246: 2195-2202, 1971.
    • (1971) J Biol Chem , vol.246 , pp. 2195-2202
    • Manganiello, V.C.1    Murad, F.2    Vaughan, M.3
  • 44
    • 0031731021 scopus 로고    scopus 로고
    • The activation of p38 MAPK by the beta-adrenergic agonist isoproterenol in rat epididymal fat cells
    • Moule SK, Denton RM. The activation of p38 MAPK by the beta-adrenergic agonist isoproterenol in rat epididymal fat cells. FEBS Lett 439: 287-290, 1998.
    • (1998) FEBS Lett , vol.439 , pp. 287-290
    • Moule, S.K.1    Denton, R.M.2
  • 45
    • 0023789884 scopus 로고
    • Identification by amino acid sequencing of three major regulatory phosphorylation sites on rat acetyl-CoA carboxylase
    • DOI 10.1111/j.1432-1033.1988.tb14201.x
    • Munday MR, Campbell DG, Carling D, Hardie DG. Identification by amino acid sequencing of three major regulatory phosphorylation sites on rat acetyl-CoA carboxylase. Eur J Biochem 175: 331-338, 1988. (Pubitemid 18190131)
    • (1988) European Journal of Biochemistry , vol.175 , Issue.2 , pp. 331-338
    • Munday, M.R.1    Campbell, D.G.2    Carling, D.3    Hardie, D.G.4
  • 46
    • 78651166782 scopus 로고
    • Metabolism of isolated fat cells
    • Rodbell M. Metabolism of isolated fat cells. J Biol Chem 239: 375-380, 1964.
    • (1964) J Biol Chem , vol.239 , pp. 375-380
    • Rodbell, M.1
  • 47
    • 0034673376 scopus 로고    scopus 로고
    • PKB inhibition prevents the stimulatory effect of insulin on glucose transport and protein translocation but not the antilipolytic effect in rat adipocytes
    • DOI 10.1006/bbrc.2000.2145
    • Smith U, Carvalho E, Mosialou E, Beguinot F, Formisano P, Rondinone C. PKB inhibition prevents the stimulatory effect of insulin on glucose transport and protein translocation but not the antilipolytic effect in rat adipocytes. Biochem Biophys Res Commun 268: 315-320, 2000. (Pubitemid 30119619)
    • (2000) Biochemical and Biophysical Research Communications , vol.268 , Issue.2 , pp. 315-320
    • Smith, U.1    Carvalho, E.2    Mosialou, E.3    Beguinot, F.4    Formisano, P.5    Rondinone, C.6
  • 48
  • 49
    • 0032055131 scopus 로고    scopus 로고
    • Activation of protein kinase B β and γ isoforms by insulin in vivo and by 3-phosphoinositide dependent protein kinase-1 in vitro: Comparison with protein kinase B α
    • Walker KS, Deak M, Paterson A, Hudson K, Cohen P, Alessi DR. 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 Balpha. Biochem J 331: 299-308, 1998. (Pubitemid 28163988)
    • (1998) Biochemical Journal , vol.331 , Issue.1 , pp. 299-308
    • Walker, K.S.1    Deak, M.2    Paterson, A.3    Hudson, K.4    Cohen, P.5    Alessi, D.R.6
  • 51
    • 0037600600 scopus 로고    scopus 로고
    • Role of Akt/protein kinase B in metabolism
    • DOI 10.1016/S1043-2760(02)00662-8, PII S1043276002006628
    • Whiteman EL, Cho H, Birnbaum MJ. Role of Akt/protein kinase B in metabolism. Trends Endocrinol Metab 13: 444-451, 2002. (Pubitemid 36733939)
    • (2002) Trends in Endocrinology and Metabolism , vol.13 , Issue.10 , pp. 444-451
    • Whiteman, E.L.1    Cho, H.2    Birnbaum, M.J.3
  • 52
    • 70449170621 scopus 로고
    • Enzymic method for the determination of glycerin
    • Wieland O. [Enzymic method for the determination of glycerin]. Biochem Z 329: 313-319, 1957.
    • (1957) Biochem Z , vol.329 , pp. 313-319
    • Wieland, O.1
  • 53
    • 0011057557 scopus 로고
    • Insulin stimulates the dephosphorylation and activation of acetyl-CoA carboxylase
    • Witters LA, Watts TD, Daniels DL, Evans JL. Insulin stimulates the dephosphorylation and activation of acetyl-CoA carboxylase. Proc Natl Acad Sci USA 85: 5473-5477, 1988.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 5473-5477
    • Witters, L.A.1    Watts, T.D.2    Daniels, D.L.3    Evans, J.L.4
  • 54
    • 0242384915 scopus 로고    scopus 로고
    • Role of AMP-activated Protein Kinase in Cyclic AMP-dependent Lipolysis in 3T3-L1 Adipocytes
    • DOI 10.1074/jbc.M308484200
    • Yin W, Mu J, Birnbaum MJ. Role of AMP-activated protein kinase in cyclic AMP-dependent lipolysis in 3T3L1 adipocytes. J Biol Chem 278: 43074-43080, 2003. (Pubitemid 37345923)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.44 , pp. 43074-43080
    • Yin, W.1    Mu, J.2    Birnbaum, M.J.3
  • 55
    • 33845460303 scopus 로고    scopus 로고
    • Novel mechanisms of the regulation of protein kinase B in adipocytes; implications for protein kinase A, Epac, phosphodiesterases 3 and 4
    • Zmuda-Trzebiatowska E, Manganiello V, Degerman E. Novel mechanisms of the regulation of protein kinase B in adipocytes; implications for protein kinase A, Epac, phosphodiesterases 3 and 4. Cell Signal 19: 81-86, 2007.
    • (2007) Cell Signal , vol.19 , pp. 81-86
    • Zmuda-Trzebiatowska, E.1    Manganiello, V.2    Degerman, E.3
  • 56
    • 27844585184 scopus 로고    scopus 로고
    • Role of PDE3B in insulin-induced glucose uptake, GLUT-4 translocation and lipogenesis in primary rat adipocytes
    • DOI 10.1016/j.cellsig.2005.05.007, PII S0898656805001051
    • Zmuda-Trzebiatowska E, Oknianska A, Manganiello V, Degerman E. Role of PDE3B in insulin-induced glucose uptake, GLUT-4 translocation and lipogenesis in primary rat adipocytes. Cell Signal 18: 382-390, 2006. (Pubitemid 41661353)
    • (2006) Cellular Signalling , vol.18 , Issue.3 , pp. 382-390
    • Zmuda-Trzebiatowska, E.1    Oknianska, A.2    Manganiello, V.3    Degerman, E.4


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