메뉴 건너뛰기




Volumn 155, Issue 3, 2014, Pages 873-888

AMPK in the small intestine in normal and pathophysiological conditions

Author keywords

[No Author keywords available]

Indexed keywords

5 AMINO 4 IMIDAZOLECARBOXAMIDE RIBOSIDE; ADENYLATE KINASE; AMP KINASE ALPHA1; CARNITINE PALMITOYLTRANSFERASE I; GLUCOSE; GLYCOGEN SYNTHASE KINASE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; INSULIN; METFORMIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE 6; MITOGEN ACTIVATED PROTEIN KINASE P38; PROTEIN KINASE B; UNCLASSIFIED DRUG;

EID: 84896858573     PISSN: 00137227     EISSN: 19457170     Source Type: Journal    
DOI: 10.1210/en.2013-1750     Document Type: Article
Times cited : (42)

References (55)
  • 1
    • 0029989587 scopus 로고    scopus 로고
    • Non-catalyticß- and γ-subunit isoforms of the 5′-AMP-activated protein kinase
    • Gao G, Fernandez CS, Stapleton D, et al. Non-catalyticß- and γ-subunit isoforms of the 5′-AMP-activated protein kinase. J Biol Chem. 1996;271:8675-8681.
    • (1996) J Biol Chem , vol.271 , pp. 8675-8681
    • Gao, G.1    Fernandez, C.S.2    Stapleton, D.3
  • 2
    • 34648828532 scopus 로고    scopus 로고
    • AMP-activated/SNF1 protein kinases: Conserved guardians of cellular energy
    • DOI 10.1038/nrm2249, PII NRM2249
    • Hardie DG. AMP-activated/SNF1 protein kinases: conserved guardians of cellular energy. Nat Rev Mol Cell Biol. 2007;8:774-785. (Pubitemid 47462132)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.10 , pp. 774-785
    • Hardie, D.G.1
  • 4
    • 0036064261 scopus 로고    scopus 로고
    • Glycogen-dependent effects of 5-aminoimidazole-4-carboxamide (AICA)-riboside on AMP-activated protein kinase and glycogen synthase activities in rat skeletal muscle
    • Wojtaszewski JF, Jørgensen SB, Hellsten Y, Hardie DG, Richter EA. Glycogen-dependent effects of 5-aminoimidazole-4-carboxamide (AICA)-riboside on AMP-activated protein kinase and glycogen synthase activities in rat skeletal muscle. Diabetes. 2002;51:284-292. (Pubitemid 34764782)
    • (2002) Diabetes , vol.51 , Issue.2 , pp. 284-292
    • Wojtaszewski, J.F.P.1    Jorgensen, S.B.2    Hellsten, Y.3    Grahame, H.D.4    Richter, E.A.5
  • 5
    • 0031849916 scopus 로고    scopus 로고
    • Evidence for 5'AMP-activated protein kinase mediation of the effect of muscle contraction on glucose transport
    • DOI 10.2337/diabetes.47.8.1369
    • Hayashi T, Hirshman MF, Kurth EJ, Winder WW, Goodyear LJ. Evidence for 5′ AMP-activated protein kinase mediation of the effect of muscle contraction on glucose transport. Diabetes. 1998;47: 1369-1373. (Pubitemid 28357021)
    • (1998) Diabetes , vol.47 , Issue.8 , pp. 1369-1373
    • Hayashi, T.1    Hirshman, M.F.2    Kurth, E.J.3    Winder, W.W.4    Goodyear, L.J.5
  • 6
    • 0024335432 scopus 로고
    • The substrate and sequence specificity of the AMP-activated protein kinase. Phosphorylation of glycogen synthase and phosphorylase kinase
    • DOI 10.1016/0167-4889(89)90014-1
    • Carling D, Hardie DG. The substrate and sequence specificity of the AMP-activated protein kinase. Phosphorylation of glycogen synthase and phosphorylase kinase. Biochim Biophys Acta. 1989;1012: 81-86. (Pubitemid 19154923)
    • (1989) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1012 , Issue.1 , pp. 81-86
    • Carling, D.1    Hardie, D.G.2
  • 7
    • 33744804815 scopus 로고    scopus 로고
    • Inhibition of lipid synthesis through activation of AMP kinase: An additional mechanism for the hypolipidemic effects of berberine
    • DOI 10.1194/jlr.M600020-JLR200
    • Brusq JM, Ancellin N, Grondin P, et al. Inhibition of lipid synthesis through activation of AMP kinase: an additional mechanism for the hypolipidemic effects of berberine. J Lipid Res. 2006;47:1281-1288. (Pubitemid 43830720)
    • (2006) Journal of Lipid Research , vol.47 , Issue.6 , pp. 1281-1288
    • Brusq, J.-M.1    Ancellin, N.2    Grondin, P.3    Guillard, R.4    Martin, S.5    Saintillan, Y.6    Issandou, M.7
  • 11
    • 33749349202 scopus 로고    scopus 로고
    • Polyphenols stimulate AMP-activated protein kinase, lower lipids, and inhibit accelerated atherosclerosis in diabetic LDL receptor-deficient mice
    • DOI 10.2337/db05-1188
    • Zang M, Xu S, Maitland-Toolan KA, et al. Polyphenols stimulate AMP-activated protein kinase, lower lipids, and inhibit accelerated atherosclerosis in diabetic LDL receptor-deficient mice. Diabetes. 2006;55:2180-2191. (Pubitemid 44743614)
    • (2006) Diabetes , vol.55 , Issue.8 , pp. 2180-2191
    • Zang, M.1    Xu, S.2    Maitland-Toolan, K.A.3    Zuccollo, A.4    Hou, X.5    Jiang, B.6    Wierzbicki, M.7    Verbeuren, T.J.8    Cohen, R.A.9
  • 12
    • 20844451123 scopus 로고    scopus 로고
    • AMP-activated protein kinase: Ancient energy gauge provides clues to modern understanding of metabolism
    • DOI 10.1016/j.cmet.2004.12.003, PII S1550413104000099
    • Kahn BB, Alquier T, Carling D, Hardie DG. AMP-activated protein kinase: ancient energy gauge provides clues to modern understanding of metabolism. Cell Metab. 2005;1:15-25. (Pubitemid 43960587)
    • (2005) Cell Metabolism , vol.1 , Issue.1 , pp. 15-25
    • Kahn, B.B.1    Alquier, T.2    Carling, D.3    Hardie, D.G.4
  • 13
    • 0345374578 scopus 로고    scopus 로고
    • Minireview: Malonyl CoA, AMP-Activated Protein Kinase, and Adiposity
    • DOI 10.1210/en.2003-0849
    • Ruderman NB, Saha AK, Kraegen EW. Minireview: malonyl CoA, AMP-activated protein kinase, and adiposity. Endocrinology. 2003; 144:5166-5171. (Pubitemid 37476042)
    • (2003) Endocrinology , vol.144 , Issue.12 , pp. 5166-5171
    • Ruderman, N.B.1    Saha, A.K.2    Kraegen, E.W.3
  • 15
    • 50449097852 scopus 로고    scopus 로고
    • Postprandial dyslipidemia in insulin resistance: Mechanisms and role of intestinal insulin sensitivity 1
    • Hsieh J, Hayashi AA, Webb J, Adeli K. Postprandial dyslipidemia in insulin resistance: mechanisms and role of intestinal insulin sensitivity 1. Atheroscler Suppl. 2008;9:7-13.
    • (2008) Atheroscler Suppl , vol.9 , pp. 7-13
    • Hsieh, J.1    Hayashi, A.A.2    Webb, J.3    Adeli, K.4
  • 16
    • 43249119219 scopus 로고    scopus 로고
    • Intestinal lipoprotein overproduction in insulin-resistant states
    • DOI 10.1097/MOL.0b013e3282ffaf82, PII 0004143320080600000002
    • Adeli K, Lewis GF. Intestinal lipoprotein overproduction in insulin-resistant states. Curr Opin Lipidol. 2008;19:221-228. (Pubitemid 351653558)
    • (2008) Current Opinion in Lipidology , vol.19 , Issue.3 , pp. 221-228
    • Adeli, K.1    Lewis, G.F.2
  • 19
    • 33745802004 scopus 로고    scopus 로고
    • Overproduction of intestinal lipoprotein containing apolipoprotein B-48 in Psammomys obesus: Impact of dietary n-3 fatty acids
    • DOI 10.1007/s00125-006-0315-3
    • Levy E, Spahis S, Ziv E, et al. Overproduction of intestinal lipoprotein containing apolipoprotein B-48 in Psammomys obesus: impact of dietary n-3 fatty acids. Diabetologia. 2006;49:1937-1945. (Pubitemid 44025049)
    • (2006) Diabetologia , vol.49 , Issue.8 , pp. 1937-1945
    • Levy, E.1    Spahis, S.2    Ziv, E.3    Marette, A.4    Elchebly, M.5    Lambert, M.6    Delvin, E.7
  • 20
    • 77149134008 scopus 로고    scopus 로고
    • Intestinal and hepatic cholesterol carriers in diabetic Psammomys obesus
    • Levy E, Lalonde G, Delvin E, et al. Intestinal and hepatic cholesterol carriers in diabetic Psammomys obesus. Endocrinology. 2010;151: 958-970.
    • (2010) Endocrinology , vol.151 , pp. 958-970
    • Levy, E.1    Lalonde, G.2    Delvin, E.3
  • 21
    • 0034966455 scopus 로고    scopus 로고
    • Circulating lipoproteins and hepatic sterol metabolism in Psammomys obesus prone to obesity, hyperglycemia and hyperinsulinemia
    • DOI 10.1016/S0021-9150(00)00711-5, PII S0021915000007115
    • Zoltowska M, Ziv E, Delvin E, et al. Circulating lipoproteins and hepatic sterol metabolism in Psammomys obesus prone to obesity, hyperglycemia and hyperinsulinemia. Atherosclerosis. 2001;157: 85-96. (Pubitemid 32539357)
    • (2001) Atherosclerosis , vol.157 , Issue.1 , pp. 85-96
    • Zoltowska, M.1    Ziv, E.2    Delvin, E.3    Stan, S.4    Bar-On, H.5    Kalman, R.6    Levy, E.7
  • 22
    • 0141755321 scopus 로고    scopus 로고
    • Cellular aspects of intestinal lipoprotein assembly in Psammomys obesus: A model of insulin resistance and type 2 diabetes
    • DOI 10.2337/diabetes.52.10.2539
    • Zoltowska M, Ziv E, Delvin E, et al. Cellular aspects of intestinal lipoprotein assembly in Psammomys obesus: a model of insulin resistance and type 2 diabetes. Diabetes. 2003;52:2539-2545. (Pubitemid 37210543)
    • (2003) Diabetes , vol.52 , Issue.10 , pp. 2539-2545
    • Zoltowska, M.1    Ziv, E.2    Delvin, E.3    Sinnett, D.4    Kalman, R.5    Garofalo, C.6    Seidman, E.7    Levy, E.8
  • 23
    • 0346492596 scopus 로고    scopus 로고
    • Both Insulin Resistance and Diabetes in Psammomys obesus Upregulate the Hepatic Machinery Involved in Intracellular VLDL Assembly
    • DOI 10.1161/01.ATV.0000105901.18785.99
    • Zoltowska M, Ziv E, Delvin E, Lambert M, Seidman E, Levy E. Both insulin resistance and diabetes in Psammomys obesus upregulate the hepatic machinery involved in intracellular VLDL assembly. Arterioscler Thromb Vasc Biol. 2004;24:118-123. (Pubitemid 38082421)
    • (2004) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.24 , Issue.1 , pp. 118-123
    • Zoltowska, M.1    Ziv, E.2    Delvin, E.3    Lambert, M.4    Seidman, E.5    Levy, E.6
  • 24
    • 0026458439 scopus 로고
    • Intestinal lipids and lipoproteins in the human fetus: Modulation by epidermal growth factor
    • Levy E, Thibault L, Ménard D. Intestinal lipids and lipoproteins in the human fetus: modulation by epidermal growth factor. J Lipid Res. 1992;33:1607-1617.
    • (1992) J Lipid Res , vol.33 , pp. 1607-1617
    • Levy, E.1    Thibault, L.2    Ménard, D.3
  • 25
    • 0035955652 scopus 로고    scopus 로고
    • The polymorphism at codon 54 of the FABP2 gene increases fat absorption in human intestinal explants
    • Levy E, Ménard D, Delvin E, et al. The polymorphism at codon 54 of the FABP2 gene increases fat absorption in human intestinal explants. J Biol Chem. 2001;276:39679-39684.
    • (2001) J Biol Chem , vol.276 , pp. 39679-39684
    • Levy, E.1    Ménard, D.2    Delvin, E.3
  • 27
    • 50049083108 scopus 로고    scopus 로고
    • Intestinal fatty acid binding protein regulates mitochondrion β-oxidation and cholesterol uptake
    • Montoudis A, Seidman E, Boudreau F, et al. Intestinal fatty acid binding protein regulates mitochondrion β-oxidation and cholesterol uptake. J Lipid Res. 2008;49:961-972.
    • (2008) J Lipid Res , vol.49 , pp. 961-972
    • Montoudis, A.1    Seidman, E.2    Boudreau, F.3
  • 28
    • 70350034157 scopus 로고    scopus 로고
    • Increased hepatic lipogenesis in insulin resistance and type 2 diabetes is associated with AMPK signalling pathway up-regulation in Psammomys obesus
    • Ben Djoudi Ouadda A, Levy E, Ziv E, et al. Increased hepatic lipogenesis in insulin resistance and type 2 diabetes is associated with AMPK signalling pathway up-regulation in Psammomys obesus. Biosci Rep. 2009;29:283-292.
    • (2009) Biosci Rep , vol.29 , pp. 283-292
    • Ben Djoudi Ouadda, A.1    Levy, E.2    Ziv, E.3
  • 29
    • 0035710746 scopus 로고    scopus 로고
    • -ΔΔCT method
    • DOI 10.1006/meth.2001.1262
    • Livak KJ, Schmittgen TD. Analysis of relative gene expression data using real-time quantitative PCR and the 2(-ΔΔ C(T)) method. Methods. 2001;25:402-408. (Pubitemid 34164012)
    • (2001) Methods , vol.25 , Issue.4 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 31
    • 0018087734 scopus 로고
    • Malonyl-CoA decarboxylase from the uropygial gland of waterfowl: Purification, properties, immunological comparison, and role in regulating the synthesis of multimethyl-branched fatty acids
    • Kim YS, Kolattukudy PE. Malonyl-CoA decarboxylase from the uropygial gland of waterfowl: purification, properties, immunological comparison, and role in regulating the synthesis of multimethyl-branched fatty acids. Arch Biochem Biophys. 1978;190:585-597. (Pubitemid 9037850)
    • (1978) Archives of Biochemistry and Biophysics , vol.190 , Issue.2 , pp. 585-597
    • Kim, Y.S.1    Kolattukudy, P.E.2
  • 33
    • 21244466801 scopus 로고    scopus 로고
    • Role of the PDK1-PKB-GSK3 pathway in regulating glycogen synthase and glucose uptake in the heart
    • DOI 10.1016/j.febslet.2005.05.040, PII S0014579305006587
    • Mora A, Sakamoto K, McManus EJ, Alessi DR. Role of the PDK1-PKB-GSK3 pathway in regulating glycogen synthase and glucose uptake in the heart. FEBS Lett. 2005;579:3632-3638. (Pubitemid 40897703)
    • (2005) FEBS Letters , vol.579 , Issue.17 , pp. 3632-3638
    • Mora, A.1    Sakamoto, K.2    McManus, E.J.3    Alessi, D.R.4
  • 34
    • 18444399216 scopus 로고    scopus 로고
    • Role that phosphorylation of GSK3 plays in insulin and Wnt signalling defined by knockin analysis
    • DOI 10.1038/sj.emboj.7600633
    • McManus EJ, Sakamoto K, Armit LJ, et al. Role that phosphorylation of GSK3 plays in insulin and Wnt signalling defined by knockin analysis. EMBO J. 2005;24:1571-1583. (Pubitemid 40646447)
    • (2005) EMBO Journal , vol.24 , Issue.8 , pp. 1571-1583
    • McManus, E.J.1    Sakamoto, K.2    Armit, L.J.3    Ronaldson, L.4    Shpiro, N.5    Marquez, R.6    Alessi, D.R.7
  • 35
    • 33845332346 scopus 로고    scopus 로고
    • Predominant alpha2/β2/γ3 AMPK activation during exercise in human skeletal muscle
    • DOI 10.1113/jphysiol.2006.120972
    • Birk JB, Wojtaszewski JF. Predominant α2/β2/γ3 AMPK activation during exercise in human skeletal muscle. J Physiol. 2006;577: 1021-1032. (Pubitemid 44873663)
    • (2006) Journal of Physiology , vol.577 , Issue.3 , pp. 1021-1032
    • Birk, J.B.1    Wojtaszewski, J.F.P.2
  • 37
    • 0034654362 scopus 로고    scopus 로고
    • Characterization of AMP-activated protein kinase γ-subunit isoforms and their role in AMP binding
    • DOI 10.1042/0264-6021:3460659
    • Cheung PC, Salt IP, Davies SP, Hardie DG, Carling D. Characterization of AMP-activated protein kinase γ-subunit isoforms and their role in AMP binding. Biochem J. 2000;346(Pt. 3):659-669. (Pubitemid 30171026)
    • (2000) Biochemical Journal , vol.346 , Issue.3 , pp. 659-669
    • Cheung, P.C.F.1    Salt, I.P.2    Davies, S.P.3    Hardie, D.G.4    Carling, D.5
  • 38
    • 79951963800 scopus 로고    scopus 로고
    • Metabolic functions of AMPK: Aspects of structure and of natural mutations in the regulatory γ subunits
    • Moffat C, Ellen Harper M. Metabolic functions of AMPK: aspects of structure and of natural mutations in the regulatory γ subunits. IUBMB Life. 2010;62:739-745.
    • (2010) IUBMB Life , vol.62 , pp. 739-745
    • Moffat, C.1    Ellen Harper, M.2
  • 39
    • 0032529139 scopus 로고    scopus 로고
    • AMP-activated protein kinase: Greater AMP dependence, and preferential nuclear localization, of complexes containing the alpha2 isoform
    • Salt I, Celler JW, Hawley SA, et al. AMP-activated protein kinase: greater AMP dependence, and preferential nuclear localization, of complexes containing the alpha2 isoform. Biochem J. 1998;334 (Pt 1):177-187. (Pubitemid 28420987)
    • (1998) Biochemical Journal , vol.334 , Issue.1 , pp. 177-187
    • Salt, I.1    Celler, J.W.2    Hawley, S.A.3    Prescott, A.4    Woods, A.5    Carling, D.6    Hardie, D.G.7
  • 40
    • 0020044788 scopus 로고
    • 3-Hydroxy-3-methylglutaryl coenzyme A reductase from rat intestine: Subcellular localization and in vitro regulation
    • Field FJ, Erickson SK, Shrewsbury MA, Cooper AD. 3-Hydroxy-3- methylglutaryl coenzyme A reductase from rat intestine: subcellular localization and in vitro regulation. J Lipid Res. 1982;23:105-113. (Pubitemid 12112618)
    • (1982) Journal of Lipid Research , vol.23 , Issue.1 , pp. 105-113
    • Field, F.J.1    Erickson, S.K.2    Shrewsbury, M.A.3    Cooper, A.D.4
  • 41
    • 0021357666 scopus 로고
    • Reversible inactivation-reactivation of 3-hydroxy-3-methylglutaryl coenzyme A reductase of rat intestine
    • Oku H, Ide T, Sugano M. Reversible inactivation-reactivation of 3-hydroxy-3-methylglutaryl coenzyme A reductase of rat intestine. J Lipid Res. 1984;25:254-261. (Pubitemid 14165025)
    • (1984) Journal of Lipid Research , vol.25 , Issue.3 , pp. 254-261
    • Oku, H.1    Ide, T.2    Sugano, M.3
  • 43
    • 79959209371 scopus 로고    scopus 로고
    • Apelin stimulates glucose uptake through the PI3K/Akt pathway and improves insulin resistance in 3T3-L1 adipocytes
    • Zhu S, Sun F, Li W, et al. Apelin stimulates glucose uptake through the PI3K/Akt pathway and improves insulin resistance in 3T3-L1 adipocytes. Mol Cell Biochem. 2011;353:305-313.
    • (2011) Mol Cell Biochem , vol.353 , pp. 305-313
    • Zhu, S.1    Sun, F.2    Li, W.3
  • 44
    • 27144450970 scopus 로고    scopus 로고
    • Insulin-sensitive protein kinases (atypical protein kinase C and protein kinase B/Akt): Actions and defects in obesity and type II diabetes
    • Farese RV, Sajan MP, Standaert ML. Insulin-sensitive protein kinases (atypical protein kinase C and protein kinase B/Akt): actions and defects in obesity and type II diabetes. Exp Biol Med (Maywood). 2005;230:593-605. (Pubitemid 41506854)
    • (2005) Experimental Biology and Medicine , vol.230 , Issue.9 , pp. 593-605
    • Farese, R.V.1    Sajan, M.P.2    Standaert, M.L.3
  • 45
    • 63749119765 scopus 로고    scopus 로고
    • PIKKing on PKB: Regulation of PKB activity by phosphorylation
    • Bozulic L, Hemmings BA. PIKKing on PKB: regulation of PKB activity by phosphorylation. Curr Opin Cell Biol. 2009;21:256-261.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 256-261
    • Bozulic, L.1    Hemmings, B.A.2
  • 46
    • 0344305782 scopus 로고    scopus 로고
    • Insulin Signaling in Health and Disease
    • DOI 10.1126/science.1092952
    • White MF. Insulin signaling in health and disease. Science. 2003; 302:1710-1711. (Pubitemid 37505726)
    • (2003) Science , vol.302 , Issue.5651 , pp. 1710-1711
    • White, M.F.1
  • 48
    • 67349091737 scopus 로고    scopus 로고
    • Oxidative stress and metabolic syndrome
    • Roberts CK, Sindhu KK. Oxidative stress and metabolic syndrome. Life Sci. 2009;84:705-712.
    • (2009) Life Sci , vol.84 , pp. 705-712
    • Roberts, C.K.1    Sindhu, K.K.2
  • 49
    • 0038064504 scopus 로고    scopus 로고
    • Effect of metformin and sulfonylurea on C-reactive protein level in well-controlled type 2 diabetics with metabolic syndrome
    • DOI 10.1385/ENDO:20:3:215
    • Akbar DH. Effect of metformin and sulfonylurea on C-reactive protein level in well-controlled type 2 diabetics with metabolic syndrome. Endocrine. 2003;20:215-218. (Pubitemid 36571021)
    • (2003) Endocrine , vol.20 , Issue.3 , pp. 215-218
    • Akbar, D.H.1
  • 50
    • 6344247712 scopus 로고    scopus 로고
    • Increased plasma concentration of macrophage Migration Inhibitory Factor (MIF) and MIF mRNA in mononuclear cells in the obese and the suppressive action of metformin
    • DOI 10.1210/jc.2004-0436
    • Dandona P, Aljada A, Ghanim H, et al. Increased plasma concentration of macrophage migration inhibitory factor (MIF) and MIF mRNA in mononuclear cells in the obese and the suppressive action of metformin. J Clin Endocrinol Metab. 2004;89:5043-5047. (Pubitemid 39391446)
    • (2004) Journal of Clinical Endocrinology and Metabolism , vol.89 , Issue.10 , pp. 5043-5047
    • Dandona, P.1    Aljada, A.2    Ghanim, H.3    Mohanty, P.4    Tripathy, C.5    Hofmeyer, D.6    Chaudhuri, A.7
  • 51
    • 78650964142 scopus 로고    scopus 로고
    • Decreased AMP-activated protein kinase activity is associated with increased inflammation in visceral adipose tissue and with whole-body insulin resistance in morbidly obese humans
    • Gauthier MS, O'Brien EL, Bigornia S, et al. Decreased AMP-activated protein kinase activity is associated with increased inflammation in visceral adipose tissue and with whole-body insulin resistance in morbidly obese humans. Biochem Biophys Res Commun. 2011; 404:382-387.
    • (2011) Biochem Biophys Res Commun , vol.404 , pp. 382-387
    • Gauthier, M.S.1    O'Brien, E.L.2    Bigornia, S.3
  • 52
    • 77953517927 scopus 로고    scopus 로고
    • Macrophage α1 AMP-activated protein kinase (α1AMPK) antagonizes fatty acid-induced inflammation through SIRT1
    • Yang Z, Kahn BB, Shi H, Xue BZ. Macrophage α1 AMP-activated protein kinase (α1AMPK) antagonizes fatty acid-induced inflammation through SIRT1. J Biol Chem. 2010;285:19051-19059.
    • (2010) J Biol Chem , vol.285 , pp. 19051-19059
    • Yang, Z.1    Kahn, B.B.2    Shi, H.3    Xue, B.Z.4
  • 53
    • 77957913650 scopus 로고    scopus 로고
    • AMPK agonist downregulates innate and adaptive immune responses in TNBS-induced murine acute and relapsing colitis
    • Bai A, Ma AG, Yong M, et al. AMPK agonist downregulates innate and adaptive immune responses in TNBS-induced murine acute and relapsing colitis. Biochem Pharmacol. 2010;80:1708-1717.
    • (2010) Biochem Pharmacol , vol.80 , pp. 1708-1717
    • Bai, A.1    Ma, A.G.2    Yong, M.3
  • 54
    • 37149046482 scopus 로고    scopus 로고
    • Adiponectin suppresses IκB kinase activation induced by tumor necrosis factor-alpha or high glucose in endothelial cells: Role of cAMP and AMP kinase signaling
    • DOI 10.1152/ajpendo.00115.2007
    • Wu X, Mahadev K, Fuchsel L, Ouedraogo R, Xu SQ, Goldstein BJ. Adiponectin suppresses IκB kinase activation induced by tumor necrosis factor-α or high glucose in endothelial cells: role of cAMP and AMP kinase signaling. Am J Physiol Endocrinol Metab. 2007;293: E1836-E1844. (Pubitemid 350258452)
    • (2007) American Journal of Physiology - Endocrinology and Metabolism , vol.293 , Issue.6
    • Wu, X.1    Mahadev, K.2    Fuchsel, L.3    Ouedraogo, R.4    Xu, S.-Q.5    Goldstein, B.J.6
  • 55
    • 47649116203 scopus 로고    scopus 로고
    • Effect of fasting on PPARγ and AMPK activity in adipocytes
    • Kajita K, Mune T, Ikeda T, et al. Effect of fasting on PPARγ and AMPK activity in adipocytes. Diabetes Res Clin Pract. 2008;81: 144-149.
    • (2008) Diabetes Res Clin Pract , vol.81 , pp. 144-149
    • Kajita, K.1    Mune, T.2    Ikeda, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.