메뉴 건너뛰기




Volumn 6, Issue , 2016, Pages

The phosphatidylethanolamine derivative diDCP-LA-PE mimics intracellular insulin signaling

Author keywords

[No Author keywords available]

Indexed keywords

1,2-O-BIS(8-(2-(2-PENTYLCYCLOPROPYLMETHYL)CYCLOPROPYL)OCTANOYL)-SN-GLYCERO-3-PHOSPHATIDYLETHANOLAMINE; GLUCOSE; INSULIN; PHOSPHATIDYLETHANOLAMINE; PROTEIN KINASE C; PROTEIN KINASE C EPSILON; PROTEIN KINASE C ZETA; PROTEIN TYROSINE PHOSPHATASE 1B; PTPN1 PROTEIN, MOUSE;

EID: 84973299487     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep27267     Document Type: Article
Times cited : (3)

References (21)
  • 1
    • 84890284142 scopus 로고    scopus 로고
    • PI3 kinase directly phosphorylates Akt1/2 at Ser473/474 in the insulin signal transduction pathway
    • Tsuchiya, A., Kanno, T. & Nishizaki, T. PI3 kinase directly phosphorylates Akt1/2 at Ser473/474 in the insulin signal transduction pathway. J Endocrinol 220, 49-59, doi: 10.1530/JOE-13-0172 (2013).
    • (2013) J Endocrinol , vol.220 , pp. 49-59
    • Tsuchiya, A.1    Kanno, T.2    Nishizaki, T.3
  • 2
    • 84876077384 scopus 로고    scopus 로고
    • Effects of newly synthesized DCP-LA-phospholipids on protein kinase C and protein phosphatases
    • Kanno, T. et al. Effects of newly synthesized DCP-LA-phospholipids on protein kinase C and protein phosphatases. Cell Physiol Biochem 31, 555-564, doi: 10.1159/000350076 (2013).
    • (2013) Cell Physiol Biochem , vol.31 , pp. 555-564
    • Kanno, T.1
  • 3
    • 33746983981 scopus 로고    scopus 로고
    • Specific protein kinase C isoforms as transducers and modulators of insulin signaling
    • Sampsona, S. R. & Cooper D. R. Specific protein kinase C isoforms as transducers and modulators of insulin signaling. Mol Genet Metab 89, 32-47 (2006)
    • (2006) Mol Genet Metab , vol.89 , pp. 32-47
    • Sampsona, S.R.1    Cooper, D.R.2
  • 4
    • 0031038052 scopus 로고    scopus 로고
    • Activation of protein kinase C (α, β, and ζ ) by insulin in 3T3/L1 cells. Transfection studies suggest A role for PKC-ζ in glucose transport
    • Bandyopadhyay, G. et al. Activation of protein kinase C (α, β, and ζ ) by insulin in 3T3/L1 cells. Transfection studies suggest A role for PKC-ζ in glucose transport. J Biol Chem 272, 2551-2558 (1997).
    • (1997) J Biol Chem , vol.272 , pp. 2551-2558
    • Bandyopadhyay, G.1
  • 5
    • 0032883639 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of specific protein kinase C isoenzymes participates in insulin stimulation of glucose transport in primary cultures of rat skeletal muscle
    • Braiman, L. et al. Tyrosine phosphorylation of specific protein kinase C isoenzymes participates in insulin stimulation of glucose transport in primary cultures of rat skeletal muscle. Diabetes 48, 1922-1929 (1999).
    • (1999) Diabetes , vol.48 , pp. 1922-1929
    • Braiman, L.1
  • 6
    • 0033529546 scopus 로고    scopus 로고
    • In vivo adenoviral delivery of recombinant human protein kinase C-ζ stimulates glucose transport activity in rat skeletal muscle
    • Etgen, G. J. et al. In vivo adenoviral delivery of recombinant human protein kinase C-ζ stimulates glucose transport activity in rat skeletal muscle. J Biol Chem 274, 22139-22142 (1999).
    • (1999) J Biol Chem , vol.274 , pp. 22139-22142
    • Etgen, G.J.1
  • 7
    • 0036288402 scopus 로고    scopus 로고
    • Function and dysfunction of aPKC isoforms for glucose transport in insulin-sensitive and insulin-resistant states
    • Farese, R. V. Function and dysfunction of aPKC isoforms for glucose transport in insulin-sensitive and insulin-resistant states. Am J Physiol Endocrinol Metab 283, E1-E11 (2002).
    • (2002) Am J Physiol Endocrinol Metab , vol.283 , pp. E1-E11
    • Farese, R.V.1
  • 8
    • 34547663520 scopus 로고    scopus 로고
    • Muscle-specific knockout of PKC-λ impairs glucose transport and induces metabolic and diabetic syndromes
    • Farese, R. V. et al. Muscle-specific knockout of PKC-λ impairs glucose transport and induces metabolic and diabetic syndromes. J Clin Invest 117, 2289-2301 (2007).
    • (2007) J Clin Invest , vol.117 , pp. 2289-2301
    • Farese, R.V.1
  • 9
    • 0033233463 scopus 로고    scopus 로고
    • Protein kinase Cδ mediates insulin-induced glucose transport in primary cultures of rat skeletal muscle
    • Braiman, L. et al. Protein kinase Cδ mediates insulin-induced glucose transport in primary cultures of rat skeletal muscle. Mol Endocrinol 13, 2002-2012 (1999).
    • (1999) Mol Endocrinol , vol.13 , pp. 2002-2012
    • Braiman, L.1
  • 10
    • 0036263641 scopus 로고    scopus 로고
    • Differential effects of tumor necrosis factor-α on protein kinase C isoforms α and δ mediate inhibition of insulin receptor signaling
    • Rosenzweig, T. et al. Differential effects of tumor necrosis factor-α on protein kinase C isoforms α and δ mediate inhibition of insulin receptor signaling. Diabetes 51, 1921-1930 (2002).
    • (2002) Diabetes , vol.51 , pp. 1921-1930
    • Rosenzweig, T.1
  • 11
    • 84880839466 scopus 로고    scopus 로고
    • Diacylglycerol promotes GLUT4 translocation to the cell surface in A PKCϵ-dependent and PKCλ/i and-ζ-independent manner
    • Tsuchiya, A. Kanno, T. & Nishizaki, T. Diacylglycerol promotes GLUT4 translocation to the cell surface in A PKCϵ-dependent and PKCλ/i and-ζ-independent manner. Life Sci 93, 240-246, doi: 10.1016/j.lfs.2013.06.014 (2013).
    • (2013) Life Sci , vol.93 , pp. 240-246
    • Tsuchiya Kanno A, T.1    Nishizaki, T.2
  • 12
    • 33744828259 scopus 로고    scopus 로고
    • The linoleic acid derivative DCP-LA selectively activates PKC-ϵ, possibly binding to the phosphatidylserine binding site
    • Kanno, T. et al. The linoleic acid derivative DCP-LA selectively activates PKC-ϵ, possibly binding to the phosphatidylserine binding site. J Lipid Res 47, 1146-1156 (2006).
    • (2006) J Lipid Res , vol.47 , pp. 1146-1156
    • Kanno, T.1
  • 13
    • 84906609299 scopus 로고    scopus 로고
    • Dipalmitoleoylphosphoethanolamine as A PP2A enhancer obstructs insulin signaling by promoting Ser/Thr dephosphorylation of Akt
    • Tsuchiya, A., Kanno, T. & Nishizaki, T. Dipalmitoleoylphosphoethanolamine as A PP2A enhancer obstructs insulin signaling by promoting Ser/Thr dephosphorylation of Akt. Cell Physiol Biochem 34, 617-627, doi: 10.1159/000363027 (2014).
    • (2014) Cell Physiol Biochem , vol.34 , pp. 617-627
    • Tsuchiya, A.1    Kanno, T.2    Nishizaki, T.3
  • 14
    • 84920818024 scopus 로고    scopus 로고
    • Oleic acid stimulates glucose uptake into adipocytes by enhancing insulin receptor signaling
    • Tsuchiya, A. et al. Oleic acid stimulates glucose uptake into adipocytes by enhancing insulin receptor signaling. J Pharmacol Sci 126, 337-343, doi: 10.1254/jphs.14182FP (2014).
    • (2014) J Pharmacol Sci , vol.126 , pp. 337-343
    • Tsuchiya, A.1
  • 15
    • 80053319859 scopus 로고    scopus 로고
    • Current understanding of increased insulin sensitivity after exercise-emerging candidates
    • Maarbjerg, S. J., Sylow, L. & Richter, E. A. Current understanding of increased insulin sensitivity after exercise-emerging candidates. Acta Physiol (Oxf) 202, 323-335, doi: 10.1111/j.1748-1716.2011.02267.x (2011).
    • (2011) Acta Physiol (Oxf) , vol.202 , pp. 323-335
    • Maarbjerg, S.J.1    Sylow, L.2    Richter, E.A.3
  • 16
    • 36148932174 scopus 로고    scopus 로고
    • The interaction of Akt with APPL1 is required for insulin-stimulated Glut4 translocation
    • Saito, T. et al. The interaction of Akt with APPL1 is required for insulin-stimulated Glut4 translocation. J Biol Chem 282, 32280-32287 (2007).
    • (2007) J Biol Chem , vol.282 , pp. 32280-32287
    • Saito, T.1
  • 17
    • 17044393948 scopus 로고    scopus 로고
    • Regulation of Akt/PKB Ser473 phosphorylation
    • Bayascas, J. R. & Alessi, D. R. Regulation of Akt/PKB Ser473 phosphorylation, Mol Cell 18, 143-145 (2005).
    • (2005) Mol Cell , vol.18 , pp. 143-145
    • Bayascas, J.R.1    Alessi, D.R.2
  • 18
    • 15944406764 scopus 로고    scopus 로고
    • PHLPP: A phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth
    • Gao, T., Furnari, F. & Newton, A. C. PHLPP: A phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth. Mol Cell 18, 13-24 (2005).
    • (2005) Mol Cell , vol.18 , pp. 13-24
    • Gao, T.1    Furnari, F.2    Newton, A.C.3
  • 19
    • 84890303026 scopus 로고    scopus 로고
    • Platelet-derived growth factor-induced Akt phosphorylation requires mTOR/Rictor and phospholipase C-γ 1, whereas S6 phosphorylation depends on mTOR/Raptor and phospholipase D
    • Razmara, M., Heldin, C. H. & Lennartsson, J. Platelet-derived growth factor-induced Akt phosphorylation requires mTOR/Rictor and phospholipase C-γ 1, whereas S6 phosphorylation depends on mTOR/Raptor and phospholipase D. Cell Commun Signal 11, 3, doi: 10.1186/1478-811X-11-3 (2013).
    • (2013) Cell Commun Signal , vol.11 , pp. 3
    • Razmara, M.1    Heldin, C.H.2    Lennartsson, J.3
  • 20
    • 38949200283 scopus 로고    scopus 로고
    • Regulation of Akt/PKB activity by P21-activated kinase in cardiomyocytes
    • Mao, K. et al. Regulation of Akt/PKB activity by P21-activated kinase in cardiomyocytes. J Mol Cell Cardiol 44, 429-434 (2008).
    • (2008) J Mol Cell Cardiol , vol.44 , pp. 429-434
    • Mao, K.1
  • 21
    • 80054804471 scopus 로고    scopus 로고
    • IKBKE protein activates Akt independent of phosphatidylinositol 3-kinase/PDK1/mTORC2 and the pleckstrin homology domain to sustain malignant transformation
    • Guo, J. P., Coppola, D. & Cheng, J. Q. IKBKE protein activates Akt independent of phosphatidylinositol 3-kinase/PDK1/mTORC2 and the pleckstrin homology domain to sustain malignant transformation. J Biol Chem 286, 37389-37398, doi: 10.1074/jbc. M111.287433 (2011).
    • (2011) J Biol Chem , vol.286 , pp. 37389-37398
    • Guo, J.P.1    Coppola, D.2    Cheng, J.Q.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.