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Volumn 3, Issue 4, 2004, Pages 340-351

AMP kinase and malonyl-CoA: Targets for therapy of the metabolic syndrome

Author keywords

[No Author keywords available]

Indexed keywords

2,4 THIAZOLIDINEDIONE DERIVATIVE; 5 AMINO 4 IMIDAZOLECARBOXAMIDE RIBOSIDE; ACETYL COENZYME A CARBOXYLASE; ADENYLATE KINASE; ADIPONECTIN; CARNITINE PALMITOYLTRANSFERASE; CARNITINE PALMITOYLTRANSFERASE INHIBITOR; DIACYLGLYCEROL; FATTY ACID; FATTY ACID SYNTHASE; GLUCOSE; GLUCOSE TRANSPORTER 4; GLYCEROL 3 PHOSPHATE ACYLTRANSFERASE; GLYCEROLIPID; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INSULIN; LEPTIN; LIPID; MALONYL COENZYME A; METFORMIN; NITRIC OXIDE SYNTHASE; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR ALPHA; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE C; STEROL REGULATORY ELEMENT BINDING PROTEIN 1; TROGLITAZONE; TUMOR NECROSIS FACTOR ALPHA; UNINDEXED DRUG; VASCULAR CELL ADHESION MOLECULE 1;

EID: 3843061592     PISSN: 14741776     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrd1344     Document Type: Review
Times cited : (394)

References (165)
  • 1
    • 0024160877 scopus 로고
    • Banting lecture 1988. Role of insulin resistance in human disease
    • Reaven, G. M. Banting lecture 1988. Role of insulin resistance in human disease. Diabetes 37, 1595-1607 (1988).
    • (1988) Diabetes , vol.37 , pp. 1595-1607
    • Reaven, G.M.1
  • 2
    • 0031944785 scopus 로고    scopus 로고
    • The metabolically obese, normal-weight individual revisited
    • Ruderman, N., Chisholm, D., Pi-Sunyer, X. & Schneider, S. The metabolically obese, normal-weight individual revisited. Diabetes 47, 699-713 (1998).
    • (1998) Diabetes , vol.47 , pp. 699-713
    • Ruderman, N.1    Chisholm, D.2    Pi-Sunyer, X.3    Schneider, S.4
  • 3
    • 0037118703 scopus 로고    scopus 로고
    • Metabolic syndrome: Pathophysiology and implications for management of cardiovascular disease
    • Reaven, G. Metabolic syndrome: pathophysiology and implications for management of cardiovascular disease. Circulation 106, 286-288 (2002).
    • (2002) Circulation , vol.106 , pp. 286-288
    • Reaven, G.1
  • 4
    • 0019943007 scopus 로고
    • Relation of body fat distribution to metabolic complications of obesity
    • Kissebah, A. H. et al. Relation of body fat distribution to metabolic complications of obesity. J. Clin. Endocrinol. Metab. 53, 254-260 (1982).
    • (1982) J. Clin. Endocrinol. Metab. , vol.53 , pp. 254-260
    • Kissebah, A.H.1
  • 5
    • 0029944207 scopus 로고    scopus 로고
    • Insulin resistance in relatives of NIDDM patients: The role of physical fitness and muscle metabolism
    • Nyholm, B. et al. Insulin resistance in relatives of NIDDM patients: the role of physical fitness and muscle metabolism. Diabetologia 39, 813-822 (1996).
    • (1996) Diabetologia , vol.39 , pp. 813-822
    • Nyholm, B.1
  • 7
    • 0036092239 scopus 로고    scopus 로고
    • Banting lecture 2001: Dysregulation of fatty acid metabolism in the etiology of type 2 diabetes
    • McGarry, J. D. Banting lecture 2001: Dysregulation of fatty acid metabolism in the etiology of type 2 diabetes. Diabetes 51, 7-18 (2002).
    • (2002) Diabetes , vol.51 , pp. 7-18
    • McGarry, J.D.1
  • 8
    • 0036182137 scopus 로고    scopus 로고
    • Lipotoxic diseases
    • Unger, R. H. Lipotoxic diseases. Annu. Rev. Med. 53, 319-336 (2002).
    • (2002) Annu. Rev. Med. , vol.53 , pp. 319-336
    • Unger, R.H.1
  • 9
    • 0030029605 scopus 로고    scopus 로고
    • Are the β-cell signaling molecules malonyl-CoA and cystolic long-chain acyl-CoA implicated in multiple tissue defects of obesity and NIDDM?
    • Prentki, M. & Corkey, B. E. Are the β-cell signaling molecules malonyl-CoA and cystolic long-chain acyl-CoA implicated in multiple tissue defects of obesity and NIDDM? Diabetes 45, 273-283 (1996).
    • (1996) Diabetes , vol.45 , pp. 273-283
    • Prentki, M.1    Corkey, B.E.2
  • 10
    • 0342314436 scopus 로고    scopus 로고
    • Hepatic fat content and insulin action on free fatty acids and glucose metabolism rather than insulin absorption are associated with insulin requirements during insulin therapy in type 2 diabetic patients
    • Ryysy, L. et al. Hepatic fat content and insulin action on free fatty acids and glucose metabolism rather than insulin absorption are associated with insulin requirements during insulin therapy in type 2 diabetic patients. Diabetes 49, 749-758 (2000).
    • (2000) Diabetes , vol.49 , pp. 749-758
    • Ryysy, L.1
  • 11
    • 0032934826 scopus 로고    scopus 로고
    • Intramyocellular lipid concentrations are correlated with insulin sensitivity in humans: A 1H NMR spectroscopy study
    • Krssak, M. et al. Intramyocellular lipid concentrations are correlated with insulin sensitivity in humans: a 1H NMR spectroscopy study. Diabetologia 42, 113-116 (1999).
    • (1999) Diabetologia , vol.42 , pp. 113-116
    • Krssak, M.1
  • 12
    • 0032960890 scopus 로고    scopus 로고
    • Association of increased intramyocellular lipid content with insulin resistance in lean nondiabetic offspring of type 2 diabetic subjects
    • Jacob, S. et al. Association of increased intramyocellular lipid content with insulin resistance in lean nondiabetic offspring of type 2 diabetic subjects. Diabetes 48, 1113-1119 (1999).
    • (1999) Diabetes , vol.48 , pp. 1113-1119
    • Jacob, S.1
  • 13
    • 0036312905 scopus 로고    scopus 로고
    • Fat accumulation in the liver is associated with defects in insulin suppression of glucose production and serum free fatty acids independent of obesity in normal men
    • Seppala-Lindroos, A. et al. Fat accumulation in the liver is associated with defects in insulin suppression of glucose production and serum free fatty acids independent of obesity in normal men. J. Clin. Endocrinol. Metab. 87, 3023-3028 (2002).
    • (2002) J. Clin. Endocrinol. Metab. , vol.87 , pp. 3023-3028
    • Seppala-Lindroos, A.1
  • 14
    • 0027947379 scopus 로고
    • β-cell lipotoxicity in the pathogenesis of non-insulin-dependent diabetes mellitus of obese rats: Impairment in adipocyte-β-cell relationships
    • Lee, Y. et al. β-cell lipotoxicity in the pathogenesis of non-insulin-dependent diabetes mellitus of obese rats: impairment in adipocyte-β-cell relationships. Proc. Natl Acad. Sci. USA 91, 10878-10882 (1994).
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10878-10882
    • Lee, Y.1
  • 15
    • 0028833276 scopus 로고
    • Caloric restriction in obese pre-diabetic rats prevents β-cell depletion, loss of β-cell GLUT 2 and glucose incompetence
    • Ohneda, M., Inman, L. R. & Unger, R. H. Caloric restriction in obese pre-diabetic rats prevents β-cell depletion, loss of β -cell GLUT 2 and glucose incompetence. Diabetologia 38, 173-179 (1995).
    • (1995) Diabetologia , vol.38 , pp. 173-179
    • Ohneda, M.1    Inman, L.R.2    Unger, R.H.3
  • 16
    • 0033613181 scopus 로고    scopus 로고
    • Troglitazone prevents mitochondrial alterations, β-cell destruction, and diabetes in obese prediabetic rats
    • Higa, M. et al. Troglitazone prevents mitochondrial alterations, β-cell destruction, and diabetes in obese prediabetic rats. Proc. Natl Acad. Sci. USA 96, 11513-11518 (1999).
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 11513-11518
    • Higa, M.1
  • 17
    • 0035130102 scopus 로고    scopus 로고
    • Diseases of liporegulation: New perspective on obesity and related disorders
    • Unger, R. H. & Orci, L. Diseases of liporegulation: new perspective on obesity and related disorders. FASEB J. 15, 312-321 (2001).
    • (2001) FASEB J. , vol.15 , pp. 312-321
    • Unger, R.H.1    Orci, L.2
  • 18
    • 0037328928 scopus 로고    scopus 로고
    • Malonyl-CoA and AMP-activated protein kinase (AMPK): Possible links between insulin resistance in muscle and early endothelial cell damage in diabetes
    • Ruderman, N. B. et al. Malonyl-CoA and AMP-activated protein kinase (AMPK): possible links between insulin resistance in muscle and early endothelial cell damage in diabetes. Biochem. Soc. Trans. 31, 202-206 (2003).
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 202-206
    • Ruderman, N.B.1
  • 19
    • 0036896505 scopus 로고    scopus 로고
    • Malonyl-CoA Signaling, Lipid Partitioning, and Glucolipotoxicity: Role in β-cell adaptation and failure in the etiology of diabetes
    • Prentki M, J. E., El-Assaad W, Roduit R. Malonyl-CoA Signaling, Lipid Partitioning, and Glucolipotoxicity: Role in β-cell adaptation and failure in the etiology of diabetes. Diabetes 51, S405-S413 (2002).
    • (2002) Diabetes , vol.51
    • Prentki, M.J.E.1    El-Assaad, W.2    Roduit, R.3
  • 20
    • 0037453056 scopus 로고    scopus 로고
    • Triglyceride accumulation protects against fatty acid-induced lipotoxicity
    • Listenberger, L. L. et al. Triglyceride accumulation protects against fatty acid-induced lipotoxicity. Proc. Natl Acad. Sci. USA 100, 3077-3082 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3077-3082
    • Listenberger, L.L.1
  • 21
    • 0031043030 scopus 로고    scopus 로고
    • The mitochondrial carnitine palmitoyltransferase system. From concept to molecular analysis
    • McGarry, J. D. & Brown, N. F. The mitochondrial carnitine palmitoyltransferase system. From concept to molecular analysis. Eur. J. Biochem. 244, 11-14 (1997).
    • (1997) Eur. J. Biochem. , vol.244 , pp. 11-14
    • McGarry, J.D.1    Brown, N.F.2
  • 22
    • 0023525741 scopus 로고
    • Ca2+, cAMP, and phospholipid-derived messengers in coupling mechanisms of insulin secretion
    • Prentki, M. & Matschinsky, F. M. Ca2+, cAMP, and phospholipid-derived messengers in coupling mechanisms of insulin secretion. Physiol. Rev. 67, 1185-1248 (1987).
    • (1987) Physiol. Rev. , vol.67 , pp. 1185-1248
    • Prentki, M.1    Matschinsky, F.M.2
  • 23
    • 0024791536 scopus 로고
    • A role for malonyl-CoA in glucose-stimulated insulin secretion from clonal pancreatic β-cells
    • Corkey, B. E. et al. A role for malonyl-CoA in glucose-stimulated insulin secretion from clonal pancreatic β -cells. J. Biol. Chem. 264, 21608-21612 (1989).
    • (1989) J. Biol. Chem. , vol.264 , pp. 21608-21612
    • Corkey, B.E.1
  • 24
    • 0026733643 scopus 로고
    • Malony-CoA and long chain acyl-CoA esters as metabolic coupling factors in nutrient-induced insulin secretion
    • Prentki, M. et al. Malony-CoA and long chain acyl-CoA esters as metabolic coupling factors in nutrient-induced insulin secretion. J. Biol. Chem. 267, 5802-6810 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 5802-6810
    • Prentki, M.1
  • 25
    • 0028817443 scopus 로고
    • A malonyl-CoA fuel-sensing mechanism in muscle: Effects of insulin, glucose, and denervation
    • Saha, A. K., Kurowski, T. G. & Ruderman, N. B. A malonyl-CoA fuel-sensing mechanism in muscle: effects of insulin, glucose, and denervation. Am. J. Physiol. 269, E283-E289 (1995).
    • (1995) Am. J. Physiol. , vol.269
    • Saha, A.K.1    Kurowski, T.G.2    Ruderman, N.B.3
  • 26
    • 0028200530 scopus 로고
    • Lipid abnormalities in tissues of the KKAy mouse: Effects of pioglitazone on malonyl-CoA and diacyglycerol
    • Saha, A. K., Kurowski, T. G., Colca, J. R. & Ruderman, N. B. Lipid abnormalities in tissues of the KKAy mouse: effects of pioglitazone on malonyl-CoA and diacyglycerol. Am. J. Physiol. 267, E95-E101 (1994).
    • (1994) Am. J. Physiol. , vol.267
    • Saha, A.K.1    Kurowski, T.G.2    Colca, J.R.3    Ruderman, N.B.4
  • 27
    • 0242300121 scopus 로고    scopus 로고
    • Hypothalamic malonyl-CoA as a mediator of feeding behavior
    • Hu, Z., Cha, S. H., Chohnan, S. & Lane, M. D. Hypothalamic malonyl-CoA as a mediator of feeding behavior. Proc. Natl Acad. Sci. USA 100, 12624-12629 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12624-12629
    • Hu, Z.1    Cha, S.H.2    Chohnan, S.3    Lane, M.D.4
  • 28
    • 0031007065 scopus 로고    scopus 로고
    • The AMP-activated protein kinase - Fuel gauge of the mammalian cell?
    • Hardie, D. G. & Carling, D. The AMP-activated protein kinase - fuel gauge of the mammalian cell? Eur. J. Biochem. 246, 259-273 (1997).
    • (1997) Eur. J. Biochem. , vol.246 , pp. 259-273
    • Hardie, D.G.1    Carling, D.2
  • 29
    • 0037323971 scopus 로고    scopus 로고
    • AMP-activated protein kinase, super metabolic regulator
    • Kemp, B. E. et al. AMP-activated protein kinase, super metabolic regulator. Biochem. Soc. Trans. 31, 162-168 (2003).
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 162-168
    • Kemp, B.E.1
  • 30
    • 0035933369 scopus 로고    scopus 로고
    • Acute regulation of fatty acid oxidation and AMP-activated protein kinase in human umbilical vein endothelial cells
    • Dagher, Z., Ruderman, N., Tornheim, K. & Ido, Y. Acute regulation of fatty acid oxidation and AMP-activated protein kinase in human umbilical vein endothelial cells. Circ. Res. 88, 1276-1282 (2001).
    • (2001) Circ. Res. , vol.88 , pp. 1276-1282
    • Dagher, Z.1    Ruderman, N.2    Tornheim, K.3    Ido, Y.4
  • 31
    • 0038015693 scopus 로고    scopus 로고
    • Glucose autoregulates its uptake in skeletal muscle: Involvement of AMP-activated protein kinase
    • Itani, S. I. et al. Glucose autoregulates its uptake in skeletal muscle: involvement of AMP-activated protein kinase. Diabetes 52, 1635-1640 (2003).
    • (2003) Diabetes , vol.52 , pp. 1635-1640
    • Itani, S.I.1
  • 32
    • 0037067666 scopus 로고    scopus 로고
    • The Anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct signaling pathways
    • Fryer, L. G., Parbu-Patel, A. & Carling, D. The Anti-diabetic drugs rosiglitazone and metformin stimulate AMP-activated protein kinase through distinct signaling pathways. J. Biol. Chem. 277, 25226-25232 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 25226-25232
    • Fryer, L.G.1    Parbu-Patel, A.2    Carling, D.3
  • 33
    • 0036324142 scopus 로고    scopus 로고
    • The antidiabetic drug metformin activates the AMP-activated protein kinase cascade via an adenine nucleotide-independent mechanism
    • Hawley, S. A., Gadalla, A. E., Olsen, G. S. & Hardie, D. G. The antidiabetic drug metformin activates the AMP-activated protein kinase cascade via an adenine nucleotide-independent mechanism. Diabetes 51, 2420-2425 (2002).
    • (2002) Diabetes , vol.51 , pp. 2420-2425
    • Hawley, S.A.1    Gadalla, A.E.2    Olsen, G.S.3    Hardie, D.G.4
  • 34
    • 10744230065 scopus 로고    scopus 로고
    • LKB1 is the upstream kinase in the AMP-activated protein kinase cascade
    • Woods, A. et al. LKB1 is the upstream kinase in the AMP-activated protein kinase cascade. Curr Biol 13, 2004-2008 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 2004-2008
    • Woods, A.1
  • 35
    • 0034637538 scopus 로고    scopus 로고
    • Activation of malonyl-CoA decarboxylase in rat skeletal muscle by contraction and the AMP-activated protein kinase activator 5-aminoimidazole-4-carboxamide-1-β-D-ribofuranoside
    • Saha, A. K. et al. Activation of malonyl-CoA decarboxylase in rat skeletal muscle by contraction and the AMP-activated protein kinase activator 5-aminoimidazole-4-carboxamide-1-β-D-ribofuranoside. J. Biol. Chem. 275, 24279-24283 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 24279-24283
    • Saha, A.K.1
  • 36
    • 0033559856 scopus 로고    scopus 로고
    • AMP-activated knees reciprocally regulates triacylglycerol synthesis and fatty and oxidation in liver and muscle: Evidence that sn-glycerol-3-phosphate acyltransferase is a novel target
    • Muoio, D. M., Seefeld, K., Witters, L. A. & Coleman, R. A. AMP-activated knees reciprocally regulates triacylglycerol synthesis and fatty and oxidation in liver and muscle: evidence that sn-glycerol-3-phosphate acyltransferase is a novel target. Biochem. J. 338, 783-791 (1999).
    • (1999) Biochem. J. , vol.338 , pp. 783-791
    • Muoio, D.M.1    Seefeld, K.2    Witters, L.A.3    Coleman, R.A.4
  • 37
    • 0037323828 scopus 로고    scopus 로고
    • AMP-activated protein kinase and hepatic genes involved in glucose metabolism
    • Ferre, P., Azzout-Marniche, D. & Foufelle, F. AMP-activated protein kinase and hepatic genes involved in glucose metabolism. Biochem. Soc. Trans. 31, 220-223 (2003).
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 220-223
    • Ferre, P.1    Azzout-Marniche, D.2    Foufelle, F.3
  • 38
    • 0033949848 scopus 로고    scopus 로고
    • Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle
    • Winder, W. W. et al. Activation of AMP-activated protein kinase increases mitochondrial enzymes in skeletal muscle. J. Appl. Physiol. 88, 2219-2226 (2000).
    • (2000) J. Appl. Physiol. , vol.88 , pp. 2219-2226
    • Winder, W.W.1
  • 39
    • 0141905919 scopus 로고    scopus 로고
    • Roles of 5′AMP-activated protein kinase in mammalian glucose homeostasis
    • Rutter, G. A., DaSilvaXavier, G. & Leclerc, I. Roles of 5′AMP-activated protein kinase in mammalian glucose homeostasis. Biochem. J. 375, 1-16 (2003).
    • (2003) Biochem. J. , vol.375 , pp. 1-16
    • Rutter, G.A.1    DaSilvaXavier, G.2    Leclerc, I.3
  • 40
    • 0033830770 scopus 로고    scopus 로고
    • UCP-3 expression in skeletal muscle: Effects of exercise, hypoxia, and AMP-activated protein kinase
    • Zhou, M., Lin, B. Z., Coughlin, S., Vallega, G. & Pilch, P. F. UCP-3 expression in skeletal muscle: effects of exercise, hypoxia, and AMP-activated protein kinase. Am. J. Physiol. Endocrinol. Metab. 279, E622-E629 (2000).
    • (2000) Am. J. Physiol. Endocrinol. Metab. , vol.279
    • Zhou, M.1    Lin, B.Z.2    Coughlin, S.3    Vallega, G.4    Pilch, P.F.5
  • 41
    • 0034800518 scopus 로고    scopus 로고
    • Insulin and contraction directly stimulate UCP2 and UCP3 mRNA expression in rat skeletal muscle in vitro
    • Pedersen, S. B., Lund, S., Buhl, E. S. & Richelsen, B. Insulin and contraction directly stimulate UCP2 and UCP3 mRNA expression in rat skeletal muscle in vitro. Biochem. Biophys. Res. Commun. 283, 19-25 (2001).
    • (2001) Biochem. Biophys. Res. Commun. , vol.283 , pp. 19-25
    • Pedersen, S.B.1    Lund, S.2    Buhl, E.S.3    Richelsen, B.4
  • 42
    • 0034863102 scopus 로고    scopus 로고
    • Regulation of muscle GLUT-4 transcription by AMP-activated protein kinase
    • Zheng, D. et al. Regulation of muscle GLUT-4 transcription by AMP-activated protein kinase. J. Appl. Physiol. 91, 1073-1083 (2001).
    • (2001) J. Appl. Physiol. , vol.91 , pp. 1073-1083
    • Zheng, D.1
  • 43
    • 0037329494 scopus 로고    scopus 로고
    • AMP-activated protein kinase regulates gene expression by direct phosphorylation of nuclear proteins
    • Leff, T. AMP-activated protein kinase regulates gene expression by direct phosphorylation of nuclear proteins. Biochem. Soc. Trans. 31, 224-247 (2003).
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 224-247
    • Leff, T.1
  • 44
    • 0036320801 scopus 로고    scopus 로고
    • Regulation of the forkhead transcription factor FKHR (FOXO1a) by glucose starvation and AICAR, an activator of AMP-activated protein kinase
    • Barthels, A., Schmoll, D., Kruger, K. D., Roth, R. A. & Joost, H. G. Regulation of the forkhead transcription factor FKHR (FOXO1a) by glucose starvation and AICAR, an activator of AMP-activated protein kinase. Endocrinology 143, 3183-3186 (2002).
    • (2002) Endocrinology , vol.143 , pp. 3183-3186
    • Barthels, A.1    Schmoll, D.2    Kruger, K.D.3    Roth, R.A.4    Joost, H.G.5
  • 45
    • 0035406121 scopus 로고    scopus 로고
    • Hepatocyte nuclear factor-4α involved in type 1 maturity-onset diabetes of the young is a novel target of AMP-activated protein kinase
    • Leclerc, I. et al. Hepatocyte nuclear factor-4α involved in type 1 maturity-onset diabetes of the young is a novel target of AMP-activated protein kinase. Diabetes 50, 1515-1521 (2001).
    • (2001) Diabetes , vol.50 , pp. 1515-1521
    • Leclerc, I.1
  • 46
    • 0036386911 scopus 로고    scopus 로고
    • Effects of low-intensity prolonged exercise on PGC-1 mRNA expression in rat epitrochlearis muscle
    • Terada, S. et al. Effects of low-intensity prolonged exercise on PGC-1 mRNA expression in rat epitrochlearis muscle. Biochem. Biophys. Res. Commun. 296, 350-354 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.296 , pp. 350-354
    • Terada, S.1
  • 47
    • 0042423598 scopus 로고    scopus 로고
    • Effects of chronic AICAR treatment on fiber composition, enzyme activity, UCP3, and PGC-1 in rat muscles
    • Suwa, M., Nakano, H. & Kumagai, S. Effects of chronic AICAR treatment on fiber composition, enzyme activity, UCP3, and PGC-1 in rat muscles. J. Appl. Physiol. 95, 960-968 (2003).
    • (2003) J. Appl. Physiol. , vol.95 , pp. 960-968
    • Suwa, M.1    Nakano, H.2    Kumagai, S.3
  • 48
    • 50549202600 scopus 로고
    • The glucose fatty-acid cycyel its role in insulin sensitivity and the metabolic disturbance of diabetes mellitus
    • Randle, P., Garland, P. B., Hales, C. N. & Newsholme, E. A. The glucose fatty-acid cycyel its role in insulin sensitivity and the metabolic disturbance of diabetes mellitus. Lancet 1, 785-789 (1963).
    • (1963) Lancet , vol.1 , pp. 785-789
    • Randle, P.1    Garland, P.B.2    Hales, C.N.3    Newsholme, E.A.4
  • 49
    • 0032452225 scopus 로고    scopus 로고
    • Regulatory interactions between lipids and carbohydrates: The glucose fatty acid cycle after 35 years
    • Randle, P. J. Regulatory interactions between lipids and carbohydrates: the glucose fatty acid cycle after 35 years. Diabetes Metab. Rev. 14, 263-283 (1998).
    • (1998) Diabetes Metab. Rev. , vol.14 , pp. 263-283
    • Randle, P.J.1
  • 50
    • 0026002683 scopus 로고
    • Effects of fat on insulin-stimulated carbohydrate metabolism in normal men
    • Boden, G. et al. Effects of fat on insulin-stimulated carbohydrate metabolism in normal men. J. Clin. Invest. 88, 960-966 (1991).
    • (1991) J. Clin. Invest. , vol.88 , pp. 960-966
    • Boden, G.1
  • 51
    • 0026334132 scopus 로고
    • Enhanced stimulation of diacylglycerol and lipid synthesis by insulin in denervated muscle. Altered protein kinase C activity and possible link to insulin resistance
    • Heydrick, S. J., Ruderman, N. B., Kurowski, T. G., Adams, H. B. & Chen, K. S. Enhanced stimulation of diacylglycerol and lipid synthesis by insulin in denervated muscle. Altered protein kinase C activity and possible link to insulin resistance. Diabetes 40, 1707-1711 (1991).
    • (1991) Diabetes , vol.40 , pp. 1707-1711
    • Heydrick, S.J.1    Ruderman, N.B.2    Kurowski, T.G.3    Adams, H.B.4    Chen, K.S.5
  • 52
    • 0036320696 scopus 로고    scopus 로고
    • Alterations of nPKC distribution, but normal Akt/PKB activation in denervated rat soleus muscle
    • Lin, Y. et al. Alterations of nPKC distribution, but normal Akt/PKB activation in denervated rat soleus muscle. Am. J. Physiol. Endocrinol. Metab. 283, E318-E325 (2002).
    • (2002) Am. J. Physiol. Endocrinol. Metab. , vol.283
    • Lin, Y.1
  • 53
    • 0029055746 scopus 로고
    • Protein kinase C is increased in the liver of humans and rats with non-insulin-dependent diabetes mellitus: An alteration not due to hyperglycemia
    • Considine, R. V. et al. Protein kinase C is increased in the liver of humans and rats with non-insulin-dependent diabetes mellitus: an alteration not due to hyperglycemia. J. Clin. Invest. 95, 2938-2944 (1995).
    • (1995) J. Clin. Invest. , vol.95 , pp. 2938-2944
    • Considine, R.V.1
  • 54
    • 0036300538 scopus 로고    scopus 로고
    • Lipid-induced insulin resistance in human muscle is associated with changes in diacylglycerol, protein kinase C, and Iκ Bα
    • Itani, S. I., Ruderman, N. B., Schmieder, F. & Boden, G. Lipid-induced insulin resistance in human muscle is associated with changes in diacylglycerol, protein kinase C, and IκBα. Diabetes 51, 2005-2011 (2002).
    • (2002) Diabetes , vol.51 , pp. 2005-2011
    • Itani, S.I.1    Ruderman, N.B.2    Schmieder, F.3    Boden, G.4
  • 55
    • 0033927667 scopus 로고    scopus 로고
    • Cellular mechanisms of insulin resistance
    • Shulman, G. I. Cellular mechanisms of insulin resistance. J. Clin. Invest. 106, 171-176 (2000).
    • (2000) J. Clin. Invest. , vol.106 , pp. 171-176
    • Shulman, G.I.1
  • 56
    • 0035979775 scopus 로고    scopus 로고
    • Reversal of obesity- and diet-induced insulin resistance with salicylates or targeted disruption of IKKβ
    • Yuan, M. et al. Reversal of obesity- and diet-induced insulin resistance with salicylates or targeted disruption of IKKβ. Science 293, 1673-1677 (2001).
    • (2001) Science , vol.293 , pp. 1673-1677
    • Yuan, M.1
  • 57
    • 0036099857 scopus 로고    scopus 로고
    • Mechanism by which high-dose aspirin improves glucose metabolism in type 2 diabetes
    • Hundal, R. S. et al. Mechanism by which high-dose aspirin improves glucose metabolism in type 2 diabetes. J. Clin. Invest. 109, 1321-1326 (2002).
    • (2002) J. Clin. Invest. , vol.109 , pp. 1321-1326
    • Hundal, R.S.1
  • 58
    • 0035217707 scopus 로고    scopus 로고
    • Skeletal muscle lipid content and insulin resistance: Evidence for a paradox in endurance-trained athletes
    • Goodpaster, B. H., He, J., Watkins, S. & Kelley, D. E. Skeletal muscle lipid content and insulin resistance: evidence for a paradox in endurance-trained athletes. J. Clin. Endocrinol. Metab. 86, 5755-5761 (2001).
    • (2001) J. Clin. Endocrinol. Metab. , vol.86 , pp. 5755-5761
    • Goodpaster, B.H.1    He, J.2    Watkins, S.3    Kelley, D.E.4
  • 59
    • 12144273598 scopus 로고    scopus 로고
    • Insulin resistance induced by glucose infusion is associated temporally with reduced muscle and liver AMPK activty
    • Kraegen, E. W. et al. Insulin resistance induced by glucose infusion is associated temporally with reduced muscle and liver AMPK activty. Diabetes 52, A330 (2003).
    • (2003) Diabetes , vol.52
    • Kraegen, E.W.1
  • 60
    • 0033399406 scopus 로고    scopus 로고
    • Muscle lipid accumulation and protein kinase C activation in the insulin-resisant chronically glucose-infused rat
    • Laybutt, D. R. et al. Muscle lipid accumulation and protein kinase C activation in the insulin-resisant chronically glucose-infused rat. Am. J. Physiol. 277, E1070-E1076 (1999).
    • (1999) Am. J. Physiol. , vol.277
    • Laybutt, D.R.1
  • 61
    • 0036788292 scopus 로고    scopus 로고
    • AICAR administration causes an apparent enhancement of muscle and liver insulin action in insulin-resistant high-fat-fed rats
    • Iglesias, M. A. et al. AICAR administration causes an apparent enhancement of muscle and liver insulin action in insulin-resistant high-fat-fed rats. Diabetes 51, 2886-2894 (2002).
    • (2002) Diabetes , vol.51 , pp. 2886-2894
    • Iglesias, M.A.1
  • 62
    • 0030784947 scopus 로고    scopus 로고
    • Diet-induced muscle insulin resistance in rats is ameliorated by acute dietary lipid withdrawal or a single bout of exercise: Parallel relationship between insulin stimulation of glucose uptake and suppression of long-chain fatty acyl-CoA
    • Oakes, N. D. et al. Diet-induced muscle insulin resistance in rats is ameliorated by acute dietary lipid withdrawal or a single bout of exercise: parallel relationship between insulin stimulation of glucose uptake and suppression of long-chain fatty acyl-CoA. Diabetes 46, 2022-2028 (1997).
    • (1997) Diabetes , vol.46 , pp. 2022-2028
    • Oakes, N.D.1
  • 63
    • 0035947235 scopus 로고    scopus 로고
    • A role for AMP-activated protein kinase in contraction- and hypoxia-regulated glucose transport in skeletal muscle
    • Mu, J., Brozinick, J. T., Jr., Valladares, O., Bucan, M. & Birnbaum, M. J. A role for AMP-activated protein kinase in contraction- and hypoxia-regulated glucose transport in skeletal muscle. Mol. Cell 7, 1085-1094 (2001).
    • (2001) Mol. Cell , vol.7 , pp. 1085-1094
    • Mu, J.1    Brozinick Jr., J.T.2    Valladares, O.3    Bucan, M.4    Birnbaum, M.J.5
  • 64
    • 0037251455 scopus 로고    scopus 로고
    • The AMP-activated protein kinase α2 catalytic subunit controls whole-body insulin sensitivity
    • Viollet, B. et al. The AMP-activated protein kinase α2 catalytic subunit controls whole-body insulin sensitivity. J. Clin. Invest. 111, 91-98 (2003).
    • (2003) J. Clin. Invest. , vol.111 , pp. 91-98
    • Viollet, B.1
  • 65
    • 0036319371 scopus 로고    scopus 로고
    • Pancreatic β-cell growth and survival - A role in obesity-linked type 2 diabetes?
    • Lingohr, M. K., Buettner, R. & Rhodes, C. J. Pancreatic β-cell growth and survival - a role in obesity-linked type 2 diabetes? Trends Mol. Med. 8, 375-384 (2002).
    • (2002) Trends Mol. Med. , vol.8 , pp. 375-384
    • Lingohr, M.K.1    Buettner, R.2    Rhodes, C.J.3
  • 66
    • 0036153256 scopus 로고    scopus 로고
    • Minireview: Secondary β-cell failure in type 2 diabetes - A convergence of glucotoxicity and lipotoxicity
    • Poitout, V. & Robertson, R. P. Minireview: Secondary β-cell failure in type 2 diabetes - a convergence of glucotoxicity and lipotoxicity. Endocrinology 143, 339-342 (2002).
    • (2002) Endocrinology , vol.143 , pp. 339-342
    • Poitout, V.1    Robertson, R.P.2
  • 67
    • 0026110135 scopus 로고
    • Banting lecture 1990. β-cells in type II diabetes mellitus
    • Porte, D., Jr. Banting lecture 1990. β-cells in type II diabetes mellitus. Diabetes 40, 166-180 (1991).
    • (1991) Diabetes , vol.40 , pp. 166-180
    • Porte Jr., D.1
  • 68
    • 0031913829 scopus 로고    scopus 로고
    • Role of apoptosis in failure of β-cell mass compensation for insulin resistance and β-cell defects in the male Zucker diabetic fatty rat
    • Pick, A. et al. Role of apoptosis in failure of β-cell mass compensation for insulin resistance and β-cell defects in the male Zucker diabetic fatty rat. Diabetes 47, 358-364 (1998).
    • (1998) Diabetes , vol.47 , pp. 358-364
    • Pick, A.1
  • 69
    • 0037219411 scopus 로고    scopus 로고
    • β-cell deficit and increased β-cell apoptosis in humans with type 2 diabetes
    • Butler, A. E. et al. β-cell deficit and increased β-cell apoptosis in humans with type 2 diabetes. Diabetes 52, 102-110 (2003).
    • (2003) Diabetes , vol.52 , pp. 102-110
    • Butler, A.E.1
  • 70
    • 0028236988 scopus 로고
    • More direct evidence for a malonyl-CoA-carnitine palmitoyltransferase I interaction as a key event in pancreatic β -cell signaling
    • Chen, S. et al. More direct evidence for a malonyl-CoA-carnitine palmitoyltransferase I interaction as a key event in pancreatic β-cell signaling. Diabetes 43, 878-883 (1994).
    • (1994) Diabetes , vol.43 , pp. 878-883
    • Chen, S.1
  • 71
    • 0035794185 scopus 로고    scopus 로고
    • Overexpression of a modified human malonyl-CoA decarboxylase blocks the glucose-induced increase in malonyl-CoA level but has no impact on insulin secretion in INS-1-derived (832/13) β-cells
    • Mulder, H. et al. Overexpression of a modified human malonyl-CoA decarboxylase blocks the glucose-induced increase in malonyl-CoA level but has no impact on insulin secretion in INS-1-derived (832/13) β-cells. J. Biol. Chem. 276, 6479-6484 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 6479-6484
    • Mulder, H.1
  • 72
    • 0034680797 scopus 로고    scopus 로고
    • Glucose down-regulates the expression of the peroxisome proliferator-activated receptor-α gene in the pancreatic β -cell
    • Roduit, R. et al. Glucose down-regulates the expression of the peroxisome proliferator-activated receptor-α gene in the pancreatic β-cell. J. Biol. Chem. 275, 35799-35806 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 35799-35806
    • Roduit, R.1
  • 73
    • 0030810982 scopus 로고    scopus 로고
    • Metabolic fate of glucose in purified islet cells. Glucose-regulated anaplerosis in β-cells
    • Schuit, F. et al. Metabolic fate of glucose in purified islet cells. Glucose-regulated anaplerosis in β-cells. J. Biol. Chem. 272, 18572-18579 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 18572-18579
    • Schuit, F.1
  • 74
    • 0038584871 scopus 로고    scopus 로고
    • Role for AMP-activated protein kinase in glucose-stimulated insulin secretion and preproinsulin gene expression
    • da Silva Xavier, G. et al. Role for AMP-activated protein kinase in glucose-stimulated insulin secretion and preproinsulin gene expression. Biochem. J. 371, 761-774 (2003).
    • (2003) Biochem. J. , vol.371 , pp. 761-774
    • da Silva Xavier, G.1
  • 75
    • 0032213768 scopus 로고    scopus 로고
    • AMP-activated protein kinase is activated by low glucose in cell lines derived from pancreatic β-cells, and may regulate insulin release
    • Salt, I. P., Johnson, G., Ashcroft, S. J. & Hardie, D. G. AMP-activated protein kinase is activated by low glucose in cell lines derived from pancreatic β-cells, and may regulate insulin release. Biochem. J. 335, 533-539 (1998).
    • (1998) Biochem. J. , vol.335 , pp. 533-539
    • Salt, I.P.1    Johnson, G.2    Ashcroft, S.J.3    Hardie, D.G.4
  • 76
    • 0027199057 scopus 로고
    • Glucose regulates acetyl-CoA carboxylase gene expression in a pancreatic β-cell line (INS-1)
    • Brun, T., Roche, E., Kim, K. H. & Prentki, M. Glucose regulates acetyl-CoA carboxylase gene expression in a pancreatic β -cell line (INS-1). J. Biol. Chem. 268, 18905-18911 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 18905-18911
    • Brun, T.1    Roche, E.2    Kim, K.H.3    Prentki, M.4
  • 77
    • 0031750277 scopus 로고    scopus 로고
    • Long-term exposure of β-INS cells to high glucose concentrations increases anaplerosis, lipogenesis, and lipogenic gene expression
    • Roche, E. et al. Long-term exposure of β-INS cells to high glucose concentrations increases anaplerosis, lipogenesis, and lipogenic gene expression. Diabetes 47, 1086-1094 (1998).
    • (1998) Diabetes , vol.47 , pp. 1086-1094
    • Roche, E.1
  • 78
    • 0036329638 scopus 로고    scopus 로고
    • Stimulation of acetyl-CoA carboxylase gene expression by glucose requires insulin release and sterol regulatory element binding protein 1c in pancreatic MIN6 β-cells
    • Andreolas, C. et al. Stimulation of acetyl-CoA carboxylase gene expression by glucose requires insulin release and sterol regulatory element binding protein 1c in pancreatic MIN6 β-cells. Diabetes 51, 2536-2545 (2002).
    • (2002) Diabetes , vol.51 , pp. 2536-2545
    • Andreolas, C.1
  • 79
    • 0042922453 scopus 로고    scopus 로고
    • Saturated fatty acids synergize with elevated glucose to cause pancreatic β-cell death
    • El-Assaad, W. et al. Saturated fatty acids synergize with elevated glucose to cause pancreatic β-cell death. Endocrinology 144, 4154-4163 (2003).
    • (2003) Endocrinology , vol.144 , pp. 4154-4163
    • El-Assaad, W.1
  • 80
    • 0036095269 scopus 로고    scopus 로고
    • Hyperglycemia-induced apoptosis in human umbilical vein endothelial cells: Inhibition by the AMP-activated protein kinase activation
    • Ido, Y., Carling, D. & Ruderman, N. Hyperglycemia-induced apoptosis in human umbilical vein endothelial cells: inhibition by the AMP-activated protein kinase activation. Diabetes 51, 159-167 (2002).
    • (2002) Diabetes , vol.51 , pp. 159-167
    • Ido, Y.1    Carling, D.2    Ruderman, N.3
  • 81
    • 0037034257 scopus 로고    scopus 로고
    • Reduction in the incidence of type 2 diabetes with lifestyle intervention or metformin
    • Knowler, W. C. et al. Reduction in the incidence of type 2 diabetes with lifestyle intervention or metformin. N. Engl. J. Med. 346, 393-403 (2002).
    • (2002) N. Engl. J. Med. , vol.346 , pp. 393-403
    • Knowler, W.C.1
  • 82
    • 0036724346 scopus 로고    scopus 로고
    • Preservation of pancreatic β-cell function and prevention of type 2 diabetes by pharmacological treatment of insulin resistance in high-risk Hispanic women
    • Buchanan, T. A. et al. Preservation of pancreatic β-cell function and prevention of type 2 diabetes by pharmacological treatment of insulin resistance in high-risk Hispanic women. Diabetes 51, 2796-2803 (2002).
    • (2002) Diabetes , vol.51 , pp. 2796-2803
    • Buchanan, T.A.1
  • 83
    • 0037180771 scopus 로고    scopus 로고
    • Inflammation in atherosclerosis
    • Libby, P. Inflammation in atherosclerosis. Nature 420, 868-874 (2002).
    • (2002) Nature , vol.420 , pp. 868-874
    • Libby, P.1
  • 84
    • 0035985081 scopus 로고    scopus 로고
    • Vascular function, insulin resistance and fatty acids
    • Steinberg, H. O. & Baron, A. D. Vascular function, insulin resistance and fatty acids. Diabetologia 45, 623-634 (2002).
    • (2002) Diabetologia , vol.45 , pp. 623-634
    • Steinberg, H.O.1    Baron, A.D.2
  • 85
    • 0033036636 scopus 로고    scopus 로고
    • AMP-activated protein kinase phosphorylation of endothelial NO synthase
    • Chen, Z. P. et al. AMP-activated protein kinase phosphorylation of endothelial NO synthase. FEBS Lett. 443, 285-289 (1999).
    • (1999) FEBS Lett. , vol.443 , pp. 285-289
    • Chen, Z.P.1
  • 86
    • 4243511832 scopus 로고    scopus 로고
    • The AMP-kinase (AMPK) activator, AICAR, inhibits the increase in oxidative stress induced by hyperglycemia and palmitate
    • Ido, Y. et al. The AMP-kinase (AMPK) activator, AICAR, inhibits the increase in oxidative stress induced by hyperglycemia and palmitate. Diabetes 51, A396 (2002).
    • (2002) Diabetes , vol.51
    • Ido, Y.1
  • 88
    • 0038644536 scopus 로고    scopus 로고
    • Nonalcoholic steatohepatitis: Summary of an AASLD Single Topic Conference
    • Neuschwander-Tetri, B. A. & Caldwell, S. H. Nonalcoholic steatohepatitis: summary of an AASLD Single Topic Conference. Hepatology 37, 1202-1219 (2003).
    • (2003) Hepatology , vol.37 , pp. 1202-1219
    • Neuschwander-Tetri, B.A.1    Caldwell, S.H.2
  • 89
    • 0035078599 scopus 로고    scopus 로고
    • Animal models of steatosis
    • Koteish, A. & Diehl, A. M. Animal models of steatosis. Semin. Liver Dis. 21, 89-104 (2001).
    • (2001) Semin. Liver Dis. , vol.21 , pp. 89-104
    • Koteish, A.1    Diehl, A.M.2
  • 90
    • 0037785066 scopus 로고    scopus 로고
    • NASH - Hepatic metabolism and not simply the metabolic syndrome
    • Green, R. M. NASH - hepatic metabolism and not simply the metabolic syndrome. Hepatology 38, 14-17 (2003).
    • (2003) Hepatology , vol.38 , pp. 14-17
    • Green, R.M.1
  • 91
    • 0036785633 scopus 로고    scopus 로고
    • Free fatty acid-induced hepatic insulin resistance a potential role for protein kinase C-delta
    • Lam, T. K. et al. Free fatty acid-induced hepatic insulin resistance a potential role for protein kinase C-delta. Am. J. Physiol. Endocrinol. Metab. 283, E682-E691 (2002).
    • (2002) Am. J. Physiol. Endocrinol. Metab. , vol.283
    • Lam, T.K.1
  • 92
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee, M. Biochemistry and molecular cell biology of diabetic complications. Nature 414, 813-820 (2001).
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 93
    • 0033517284 scopus 로고    scopus 로고
    • Leptin reverses insulin resistance and diabetes mellitus in mice with congenital lipodystrophy
    • Shimomura, I., Hammer, R. E., Ikemoto, S., Brown, M. S. & Goldstein, J. L. Leptin reverses insulin resistance and diabetes mellitus in mice with congenital lipodystrophy. Nature 401, 73-76 (1999).
    • (1999) Nature , vol.401 , pp. 73-76
    • Shimomura, I.1    Hammer, R.E.2    Ikemoto, S.3    Brown, M.S.4    Goldstein, J.L.5
  • 94
    • 0041302377 scopus 로고    scopus 로고
    • The fat-derived hormone adiponectin alleviates alcoholic and nonalcoholic fatty liver disease in mice
    • Xu, A., Wang, Y. et al. The fat-derived hormone adiponectin alleviates alcoholic and nonalcoholic fatty liver disease in mice. J. Clin. Invest. 112, 91-100 (2003).
    • (2003) J. Clin. Invest. , vol.112 , pp. 91-100
    • Xu, A.1    Wang, Y.2
  • 95
    • 0141532275 scopus 로고    scopus 로고
    • Improved Nonalcoholic steatohepatitis after 48 weeks of treatment with the PPAR-γ ligand rosiglitazone
    • Neuschwander-Tetri, B. A. et al. Improved Nonalcoholic steatohepatitis after 48 weeks of treatment with the PPAR-γ ligand rosiglitazone. Hepatology 38, 1008-1017 (2003).
    • (2003) Hepatology , vol.38 , pp. 1008-1017
    • Neuschwander-Tetri, B.A.1
  • 96
    • 0036851817 scopus 로고    scopus 로고
    • Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase
    • Yamauchi, T. et al. Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase. Nature Med. 8, 1288-1295 (2002).
    • (2002) Nature Med. , vol.8 , pp. 1288-1295
    • Yamauchi, T.1
  • 97
    • 0037059013 scopus 로고    scopus 로고
    • Enhanced muscle fat oxidation and glucose transport by ACRP30 globular domain: Acetyl-CoA carboxylase inhibition and AMP-activated protein kinase activation
    • Tomas, E. et al. Enhanced muscle fat oxidation and glucose transport by ACRP30 globular domain: acetyl-CoA carboxylase inhibition and AMP-activated protein kinase activation. Proc. Natl Acad. Sci. USA 99, 16309-16313 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 16309-16313
    • Tomas, E.1
  • 98
    • 85047689953 scopus 로고
    • 5-aminoimidazole-4-carboxamide ribonucleoside. A specific method for activating AMP-activated protein kinase in intact cells
    • Corton, J. M., Gillespie, J. G., Hawley, S. A. & Hardie, D. G. 5-aminoimidazole-4-carboxamide ribonucleoside. A specific method for activating AMP-activated protein kinase in intact cells. Eur. J. Biochem. 229, 558-565 (1995).
    • (1995) Eur. J. Biochem. , vol.229 , pp. 558-565
    • Corton, J.M.1    Gillespie, J.G.2    Hawley, S.A.3    Hardie, D.G.4
  • 99
    • 0037031840 scopus 로고    scopus 로고
    • Coordinate regulation of malonyl-CoA decarboxylase, sn-glycerol-3-phosphate acyltransferase, and acetyl-CoA carboxylase by AMP-activated protein kinase in rat tissues in response to exercise
    • Park, H. et al. Coordinate regulation of malonyl-CoA decarboxylase, sn-glycerol-3-phosphate acyltransferase, and acetyl-CoA carboxylase by AMP-activated protein kinase in rat tissues in response to exercise. J. Biol. Chem. 277, 32571-32577 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 32571-32577
    • Park, H.1
  • 100
    • 0031731021 scopus 로고    scopus 로고
    • The activation of p38 MAPK by the β-adrenergic agonist isoproterenol in rat epididymal fat cells
    • Moule, S. K. & Denton, R. M. The activation of p38 MAPK by the β-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
  • 101
    • 0037983775 scopus 로고    scopus 로고
    • Involvement of AMP-activated protein kinase in glucose uptake stimulated by the globular domain of adiponectin in primary rat adipocytes
    • Wu, X. et al. Involvement of AMP-activated protein kinase in glucose uptake stimulated by the globular domain of adiponectin in primary rat adipocytes. Diabetes 52, 1355-1363 (2003).
    • (2003) Diabetes , vol.52 , pp. 1355-1363
    • Wu, X.1
  • 102
    • 0345374578 scopus 로고    scopus 로고
    • Malonyl CoA, AMP-activated protein kinase, and adiposity
    • Ruderman, N., Saha, A. & Kraegen, E. W. Malonyl CoA, AMP-activated protein kinase, and adiposity. Endocrinology 144, 5161-5171 (2003).
    • (2003) Endocrinology , vol.144 , pp. 5161-5171
    • Ruderman, N.1    Saha, A.2    Kraegen, E.W.3
  • 103
    • 0020027151 scopus 로고
    • Muscle glucose metabolism following exercise in the rat: Increased sensitivity to insulin
    • Richter, E. A., Garetto, L. P., Goodman, M. N. & Ruderman, N. B. Muscle glucose metabolism following exercise in the rat: increased sensitivity to insulin. J. Clin. Invest. 69, 785-793 (1982).
    • (1982) J. Clin. Invest. , vol.69 , pp. 785-793
    • Richter, E.A.1    Garetto, L.P.2    Goodman, M.N.3    Ruderman, N.B.4
  • 104
    • 0004172105 scopus 로고    scopus 로고
    • 2nd edn (eds Ruderman, N., Devlin, J. R., Schneider, S. H. & Kriska, A.) (American Diabetes Association, Alexandria)
    • Skerrett, P. J. & Manson, J. E. in Handbook of Exercise in Diabetes 2nd edn (eds Ruderman, N., Devlin, J. R., Schneider, S. H. & Kriska, A.) 158-182 (American Diabetes Association, Alexandria, 2002).
    • (2002) Handbook of Exercise in Diabetes , pp. 158-182
    • Skerrett, P.J.1    Manson, J.E.2
  • 105
    • 0030935652 scopus 로고    scopus 로고
    • Effects of diet and exercise in preventing NIDDM in people with impaired glucose tolerance. The Da Qing IGT and Diabetes Study
    • Pan, X. R. et al. Effects of diet and exercise in preventing NIDDM in people with impaired glucose tolerance. The Da Qing IGT and Diabetes Study. Diabetes Care 20, 537-544 (1997).
    • (1997) Diabetes Care , vol.20 , pp. 537-544
    • Pan, X.R.1
  • 106
    • 0035799806 scopus 로고    scopus 로고
    • Prevention of type 2 diabetes mellitus by changes in lifestyle among subjects with impaired glucose tolerance
    • Tuomilehto, J. et al. Prevention of type 2 diabetes mellitus by changes in lifestyle among subjects with impaired glucose tolerance. N. Engl. J. Med. 344, 1343-1350 (2001).
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1343-1350
    • Tuomilehto, J.1
  • 107
    • 0035852760 scopus 로고    scopus 로고
    • Proteolytic cleavage product of 30-kDa adipocyte complement-related protein increases fatty acid oxidation in muscle and causes weight loss in mice
    • Fruebis, J. et al. Proteolytic cleavage product of 30-kDa adipocyte complement-related protein increases fatty acid oxidation in muscle and causes weight loss in mice. Proc. Natl Acad. Sci. USA 98, 2005-2010 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2005-2010
    • Fruebis, J.1
  • 108
    • 0042330251 scopus 로고    scopus 로고
    • The adipocyte - At the crossroads of energy homeostasis, inflammation and atherosclerosis
    • Rajala, M. W., Scherer, P. E. The adipocyte - at the crossroads of energy homeostasis, inflammation and atherosclerosis. Endocrinology 144, 3765-3773 (2003).
    • (2003) Endocrinology , vol.144 , pp. 3765-3773
    • Rajala, M.W.1    Scherer, P.E.2
  • 109
    • 0036063777 scopus 로고    scopus 로고
    • Diet-induced insulin resistance in mice lacking adiponectin/ACRP30
    • Maeda, N. et al. Diet-induced insulin resistance in mice lacking adiponectin/ACRP30. Nature Med. 8, 731-737 (2002).
    • (2002) Nature Med. , vol.8 , pp. 731-737
    • Maeda, N.1
  • 110
    • 0037180472 scopus 로고    scopus 로고
    • Adiponectin reduces atherosclerosis in apolipoprotein E-deficient mice
    • Okamoto, Y. et al. Adiponectin reduces atherosclerosis in apolipoprotein E-deficient mice. Circulation 106, 2767-2770 (2002).
    • (2002) Circulation , vol.106 , pp. 2767-2770
    • Okamoto, Y.1
  • 111
    • 0037462684 scopus 로고    scopus 로고
    • Globular adiponectin protected ob/ob mice from diabetes and ApoE-deficient mice from atherosclerosis
    • Yamauchi, T. et al. Globular adiponectin protected ob/ob mice from diabetes and ApoE-deficient mice from atherosclerosis. J. Biol. Chem. 278, 2461-2468 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 2461-2468
    • Yamauchi, T.1
  • 112
    • 0032779351 scopus 로고    scopus 로고
    • Molecular mechanism of metabolic syndrome X: Contribution of adipocytokines adipocyte-derived bioactive substances
    • Matsuzawa, Y., Funahashi, T. & Nakamura, T. Molecular mechanism of metabolic syndrome X: contribution of adipocytokines adipocyte-derived bioactive substances. Ann. NY Acad. Sci. 892, 146-154 (1999).
    • (1999) Ann. NY Acad. Sci. , vol.892 , pp. 146-154
    • Matsuzawa, Y.1    Funahashi, T.2    Nakamura, T.3
  • 113
    • 0013375847 scopus 로고    scopus 로고
    • AMP-kinase activation prevents TNF-α induced ICAM expression by inhibiting NF-κB transactivation but not by inhibiting their translocation or DNA-binding
    • Ido, Y., Yagihashi, N., Cacicedo, J. M., Ruderman, N. B. AMP-kinase activation prevents TNF-α induced ICAM expression by inhibiting NF-κB transactivation but not by inhibiting their translocation or DNA-binding. Diabetes 51, A458 (2002).
    • (2002) Diabetes , vol.51
    • Ido, Y.1    Yagihashi, N.2    Cacicedo, J.M.3    Ruderman, N.B.4
  • 114
    • 0242329843 scopus 로고    scopus 로고
    • Adiponectin: Linking the fat cell to insulin sensitivity
    • Goldfine, A. B. & Kahn, C. R. Adiponectin: linking the fat cell to insulin sensitivity. Lancet 362, 1431-1432 (2003).
    • (2003) Lancet , vol.362 , pp. 1431-1432
    • Goldfine, A.B.1    Kahn, C.R.2
  • 115
    • 0037122766 scopus 로고    scopus 로고
    • Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase
    • Minokoshi, Y. et al. Leptin stimulates fatty-acid oxidation by activating AMP-activated protein kinase. Nature 415, 339-343 (2002).
    • (2002) Nature , vol.415 , pp. 339-343
    • Minokoshi, Y.1
  • 116
    • 0033857387 scopus 로고    scopus 로고
    • Treatment of insulin resistance with peroxisome proliferator-activated receptor-γ agonists
    • Olefsky, J. M. Treatment of insulin resistance with peroxisome proliferator-activated receptor-γ agonists. J. Clin. Invest. 106, 467-472 (2000).
    • (2000) J. Clin. Invest. , vol.106 , pp. 467-472
    • Olefsky, J.M.1
  • 117
    • 0036310037 scopus 로고    scopus 로고
    • The effects of rosiglitazone on insulin sensitivity, lipolysis, and hepatic and skeletal muscle triglyceride content in patients with type 2 diabetes
    • Mayerson, A. B. et al. The effects of rosiglitazone on insulin sensitivity, lipolysis, and hepatic and skeletal muscle triglyceride content in patients with type 2 diabetes. Diabetes 51, 797-802 (2002).
    • (2002) Diabetes , vol.51 , pp. 797-802
    • Mayerson, A.B.1
  • 118
    • 0141611978 scopus 로고    scopus 로고
    • The central role of fat and effect of peroxisome proliferator-activated receptor-γ on progression of insulin resistance and cardiovascular disease
    • Hsueh, W. A. & Law, R. The central role of fat and effect of peroxisome proliferator-activated receptor-γ on progression of insulin resistance and cardiovascular disease. Am. J. Cardiol. 92, 3J-9J (2003).
    • (2003) Am. J. Cardiol. , vol.92
    • Hsueh, W.A.1    Law, R.2
  • 119
    • 0141835015 scopus 로고    scopus 로고
    • Insulin resistance, inflammation, and the prediabetic state
    • Haffner, S. M. Insulin resistance, inflammation, and the prediabetic state. Am. J. Cardiol. 92, 18J-26J (2003).
    • (2003) Am. J. Cardiol. , vol.92
    • Haffner, S.M.1
  • 120
    • 0346374720 scopus 로고    scopus 로고
    • Pioglitazone treatment activates AMP-activated protein kinase (AMPK) in both liver and adipose tissue in the rat
    • Saha, A., Ye, J., Assiti, M., Kraegen, E., Ruderman, N. B. & Arilucca, P. R. Pioglitazone treatment activates AMP-activated protein kinase (AMPK) in both liver and adipose tissue in the rat. Biochem. Biophys. Res. Commun. 314, 580-585 (2004).
    • (2004) Biochem. Biophys. Res. Commun. , vol.314 , pp. 580-585
    • Saha, A.1    Ye, J.2    Assiti, M.3    Kraegen, E.4    Ruderman, N.B.5    Arilucca, P.R.6
  • 121
    • 0036789137 scopus 로고    scopus 로고
    • The effect of thiazolidinediones on plasma adiponectin levels in normal, obese, and type 2 diabetic subjects
    • Yu, J. G. et al. The effect of thiazolidinediones on plasma adiponectin levels in normal, obese, and type 2 diabetic subjects. Diabetes 51, 2968-2974 (2002).
    • (2002) Diabetes , vol.51 , pp. 2968-2974
    • Yu, J.G.1
  • 122
    • 9144271149 scopus 로고    scopus 로고
    • Activation of peroxisome proliferator-activated receptor delta induces fatty acid β-oxidation in skeletal muscle and attenuates metabolic syndrome
    • Tanaka, T. et al. Activation of peroxisome proliferator-activated receptor delta induces fatty acid β -oxidation in skeletal muscle and attenuates metabolic syndrome. Proc. Natl Acad. Sci. USA 100, 15924-15929 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 15924-15929
    • Tanaka, T.1
  • 123
    • 0034773404 scopus 로고    scopus 로고
    • Role of AMP-activated protein kinase in mechanism of metformin action
    • Zhou, G. et al. Role of AMP-activated protein kinase in mechanism of metformin action. J. Clin. Invest. 108, 1167-1174 (2001).
    • (2001) J. Clin. Invest. , vol.108 , pp. 1167-1174
    • Zhou, G.1
  • 124
    • 0036299982 scopus 로고    scopus 로고
    • Metformin increases AMP-activated protein kinase, activity in skeletal muscle of subjects with type 2 diabetes
    • Musi, N. et al. Metformin increases AMP-activated protein kinase, activity in skeletal muscle of subjects with type 2 diabetes. Diabetes 51, 2074-2081 (2002).
    • (2002) Diabetes , vol.51 , pp. 2074-2081
    • Musi, N.1
  • 125
    • 0032511566 scopus 로고    scopus 로고
    • Effect of intensive blood-glucose control with metformin on complications in overweight patients with type 2 diabetes (UKPDS 34)
    • UK Prospective Diabetes Study (UKPDS) Group
    • Effect of intensive blood-glucose control with metformin on complications in overweight patients with type 2 diabetes (UKPDS 34). UK Prospective Diabetes Study (UKPDS) Group. Lancet 352, 854-865 (1998).
    • (1998) Lancet , vol.352 , pp. 854-865
  • 126
    • 0037219409 scopus 로고    scopus 로고
    • Are oxidative stress-activated signaling pathways mediators of insulin resistance and β-cell dysfunction?
    • Evans, J. L., Goldfine, I. D., Maddux, B. A. & Grodsky G. M. Are oxidative stress-activated signaling pathways mediators of insulin resistance and β-cell dysfunction? Diabetes 52, 1-8 (2003).
    • (2003) Diabetes , vol.52 , pp. 1-8
    • Evans, J.L.1    Goldfine, I.D.2    Maddux, B.A.3    Grodsky, G.M.4
  • 127
    • 0033765672 scopus 로고    scopus 로고
    • High glucose level and free fatty acid stimulate reactive oxygen species production through protein kinase C-dependent activation of NAD(P)H oxidase in cultured vascular cells
    • Inoguchi, T. et al. High glucose level and free fatty acid stimulate reactive oxygen species production through protein kinase C-dependent activation of NAD(P)H oxidase in cultured vascular cells. Diabetes 49, 1939-1945 (2000).
    • (2000) Diabetes , vol.49 , pp. 1939-1945
    • Inoguchi, T.1
  • 128
    • 0031841949 scopus 로고    scopus 로고
    • Regulation of insulin-stimulated glucose transporter GLUT4 translocation and Akt kinase activity by ceramide
    • Summers, S. A., Garza, L. A., Zhou, H. & Bimbaum, M. J. Regulation of insulin-stimulated glucose transporter GLUT4 translocation and Akt kinase activity by ceramide. Mol. Cell. Biol. 18, 5457-5464 (1998).
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5457-5464
    • Summers, S.A.1    Garza, L.A.2    Zhou, H.3    Bimbaum, M.J.4
  • 129
    • 0035793432 scopus 로고    scopus 로고
    • The AMP-activated protein kinase prevents ceramide synthesis de novo and apoptosis in astrocytes
    • Blazquez, C., Geelen, M. J., Velasco, G. & Guzman, M. The AMP-activated protein kinase prevents ceramide synthesis de novo and apoptosis in astrocytes. FEBS Lett. 489, 149-153 (2001).
    • (2001) FEBS Lett. , vol.489 , pp. 149-153
    • Blazquez, C.1    Geelen, M.J.2    Velasco, G.3    Guzman, M.4
  • 130
    • 13844284443 scopus 로고    scopus 로고
    • Palmitate-induced cultured bovine retinal pericyte (BRP) apoptosis is inhibited by activating AMP-activated protein kinase (AMPK), by expression of Cu, Zn superoxide dismutase (SOD1) and dominant negative mutant IκB
    • Cacicedo, J. M., Yagihashi, N., Adachi, T., Ruderman, N. R., and Yasudo, I. Palmitate-induced cultured bovine retinal pericyte (BRP) apoptosis is inhibited by activating AMP-activated protein kinase (AMPK), by expression of Cu, Zn superoxide dismutase (SOD1) and dominant negative mutant IκB. Diabetes 52, A199 (2003).
    • (2003) Diabetes , vol.52
    • Cacicedo, J.M.1    Yagihashi, N.2    Adachi, T.3    Ruderman, N.R.4    Yasudo, I.5
  • 131
    • 0037184925 scopus 로고    scopus 로고
    • Mechanism by which fatty acids inhibit insulin activation of insulin receptor substrate-1 (IRS-1)-associated phosphatidylinositol 3-kinase activy in muscle
    • Yu, C. et al. Mechanism by which fatty acids inhibit insulin activation of insulin receptor substrate-1 (IRS-1)-associated phosphatidylinositol 3-kinase activy in muscle. J. Biol. Chem. 277, 50230-50236 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 50230-50236
    • Yu, C.1
  • 132
    • 0036308313 scopus 로고    scopus 로고
    • The hexosamine signaling pathway: A new road to drug discovery
    • Marshall, S. The hexosamine signaling pathway: a new road to drug discovery. Curr. Opin. Endocrinol. Diabetes 9, 160-167 (2002).
    • (2002) Curr. Opin. Endocrinol. Diabetes , vol.9 , pp. 160-167
    • Marshall, S.1
  • 133
    • 0033664020 scopus 로고    scopus 로고
    • Overexpression of glutamine: Fructose-6-phosphate amidotransferase in the liver of transgenic mice results in enhanced glycogen storage, hyperlipidemia, obesity, and impaired glucose tolerance
    • Veerababu, G. et al. Overexpression of glutamine: fructose-6-phosphate amidotransferase in the liver of transgenic mice results in enhanced glycogen storage, hyperlipidemia, obesity, and impaired glucose tolerance. Diabetes 49, 02070-2078 (2000).
    • (2000) Diabetes , vol.49 , pp. 2070-2078
    • Veerababu, G.1
  • 134
    • 0038054341 scopus 로고    scopus 로고
    • PGC-1α-responsive genes involved in oxidative phosphorylation are coordinately downregulated in human diabetes
    • Mootha, V. K. et al. PGC-1α-responsive genes involved in oxidative phosphorylation are coordinately downregulated in human diabetes. Nature Genet. 34, 267-273 (2003).
    • (2003) Nature Genet. , vol.34 , pp. 267-273
    • Mootha, V.K.1
  • 135
    • 0037477855 scopus 로고    scopus 로고
    • Coordinated reduction of genes of oxidative metabolism in humans with insulin resistance and diabetes: Potential role of PGC1 and NRF1
    • Patti, M. E. et al. Coordinated reduction of genes of oxidative metabolism in humans with insulin resistance and diabetes: Potential role of PGC1 and NRF1. Proc. Natl Acad. Sci. USA 100, 8466-8471 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 8466-8471
    • Patti, M.E.1
  • 136
    • 0036788293 scopus 로고    scopus 로고
    • Dysfunction of mitochondria in human skeletal muscle in type 2 diabetes
    • Kelley, D. E., He, J., Menshikova, E. V. & Ritov, V. B. Dysfunction of mitochondria in human skeletal muscle in type 2 diabetes. Diabetes 51, 2944-2950 (2002).
    • (2002) Diabetes , vol.51 , pp. 2944-2950
    • Kelley, D.E.1    He, J.2    Menshikova, E.V.3    Ritov, V.B.4
  • 137
    • 0038025371 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in the elderly: Possible role in insulin resistance
    • Petersen, K. F. et al. Mitochondrial dysfunction in the elderly: possible role in insulin resistance. Science 300, 1140-1142 (2003).
    • (2003) Science , vol.300 , pp. 1140-1142
    • Petersen, K.F.1
  • 138
    • 0026806837 scopus 로고
    • Ten-year experience with an exercise-based outpatient life-style modification program in the treatment of diabetes mellittus
    • Schneider, S. H., Khachadurian, A. K., Amorosa, L. F., Clemow, L. & Ruderman, N. B. Ten-year experience with an exercise-based outpatient life-style modification program in the treatment of diabetes mellittus. Diabetes Care 15, 1800-1810 (1992).
    • (1992) Diabetes Care , vol.15 , pp. 1800-1810
    • Schneider, S.H.1    Khachadurian, A.K.2    Amorosa, L.F.3    Clemow, L.4    Ruderman, N.B.5
  • 139
    • 0036083787 scopus 로고    scopus 로고
    • Nonalcoholic steatosis and steatohepatitis IV. Nonalcoholic fatty liver disease abnormalities in macrophage function and cytokines
    • Diehl, A. M. Nonalcoholic steatosis and steatohepatitis IV. Nonalcoholic fatty liver disease abnormalities in macrophage function and cytokines. Am. J. Physiol. Gastrointest. Liver Physiol. 282, G1-G5 (2002).
    • (2002) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.282
    • Diehl, A.M.1
  • 140
    • 0037230114 scopus 로고    scopus 로고
    • Mitochondrial dysfunction is involved in apoptosis induced by serum withdrawal and fatty acids in the β-cell line INS-1
    • Maestre, I. et al. Mitochondrial dysfunction is involved in apoptosis induced by serum withdrawal and fatty acids in the β-cell line INS-1. Endocrinology 144, 335-345 (2003).
    • (2003) Endocrinology , vol.144 , pp. 335-345
    • Maestre, I.1
  • 141
    • 0037058977 scopus 로고    scopus 로고
    • AMP kinase is required for mitochondrial biogenesis in skeletal muscle in resonse to chronic energy deprivation
    • Zong, H. et al. AMP kinase is required for mitochondrial biogenesis in skeletal muscle in resonse to chronic energy deprivation. Proc. Natl Acad. Sci. USA 99, 15983-15987 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15983-15987
    • Zong, H.1
  • 142
    • 0036402110 scopus 로고    scopus 로고
    • Metabolic lessons from genetically lean mice
    • Reitman, M. L. Metabolic lessons from genetically lean mice. Annu. Rev. Nutr. 22, 459-482 (2002).
    • (2002) Annu. Rev. Nutr. , vol.22 , pp. 459-482
    • Reitman, M.L.1
  • 143
    • 0033965557 scopus 로고    scopus 로고
    • Surgical implantation of adipose tissue reverses diabetes in lipoatrophic mice
    • Gavrilova, O. et al. Surgical implantation of adipose tissue reverses diabetes in lipoatrophic mice. J. Clin. Invest. 105, 271-278 (2000).
    • (2000) J. Clin. Invest. , vol.105 , pp. 271-278
    • Gavrilova, O.1
  • 145
    • 0037148928 scopus 로고    scopus 로고
    • Leptin replacement therapy for lipodystrophy
    • Arioglu, E. et al. Leptin replacement therapy for lipodystrophy. N. Engl. J. Med. 346, 570-578 (2002).
    • (2002) N. Engl. J. Med. , vol.346 , pp. 570-578
    • Arioglu, E.1
  • 146
    • 0036114844 scopus 로고    scopus 로고
    • Leptin reverses insulin resistance and hepatic steatosis in patients with severe lipodystrophy
    • Petersen, K. F. et al. Leptin reverses insulin resistance and hepatic steatosis in patients with severe lipodystrophy. J. Clin. Invest. 109, 1345-1350 (2002).
    • (2002) J. Clin. Invest. , vol.109 , pp. 1345-1350
    • Petersen, K.F.1
  • 147
    • 85039535740 scopus 로고    scopus 로고
    • Rosiglitazone treatment improves insulin sensitivity in lipodystrophic patients with mandibuloacral diplasia
    • Sbraccia, P. et al. Rosiglitazone treatment improves insulin sensitivity in lipodystrophic patients with mandibuloacral diplasia. Diabetes 52, A1 (2003).
    • (2003) Diabetes , vol.52
    • Sbraccia, P.1
  • 148
    • 17944365228 scopus 로고    scopus 로고
    • The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity
    • Yamauchi, T. et al. The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity. Nature Med. 7, 941-946 (2001).
    • (2001) Nature Med. , vol.7 , pp. 941-946
    • Yamauchi, T.1
  • 149
    • 0035970805 scopus 로고    scopus 로고
    • Continuous fatty acid oxidation and reduced fat storage in mice lacking acetyl-CoA carboxylase 2
    • Abu-Elheiga, L., Matzuk, M. M., Abo-Hashema, K. A. & Wakil, S. J. Continuous fatty acid oxidation and reduced fat storage in mice lacking acetyl-CoA carboxylase 2. Science 291, 2613-2616 (2001).
    • (2001) Science , vol.291 , pp. 2613-2616
    • Abu-Elheiga, L.1    Matzuk, M.M.2    Abo-Hashema, K.A.3    Wakil, S.J.4
  • 150
    • 0032792665 scopus 로고    scopus 로고
    • AMP-activated protein kinase, a metabolic master switch: Possible roles in type 2 diabetes
    • Winder, W. W. & Hardie, D. G. AMP-activated protein kinase, a metabolic master switch: possible roles in type 2 diabetes. Am. J. Physiol. 277, E1-E10 (1999).
    • (1999) Am. J. Physiol. , vol.277
    • Winder, W.W.1    Hardie, D.G.2
  • 151
    • 0033948495 scopus 로고    scopus 로고
    • Fatty acid oxidation and the regulation of malonyl-CoA in human muscle
    • Bavenholm, P. V., Pigon, J., Saha, A. K., Ruderman, N. B. & Efendic, S. Fatty acid oxidation and the regulation of malonyl-CoA in human muscle. Diabetes 49, 1078-1083 (2000).
    • (2000) Diabetes , vol.49 , pp. 1078-1083
    • Bavenholm, P.V.1    Pigon, J.2    Saha, A.K.3    Ruderman, N.B.4    Efendic, S.5
  • 152
    • 0033855904 scopus 로고    scopus 로고
    • Exercise diminishes the activity of acetyl-CoA carboxylase in human muscle
    • Dean, D. et al. Exercise diminishes the activity of acetyl-CoA carboxylase in human muscle. Diabetes 49, 1295-1300 (2000).
    • (2000) Diabetes , vol.49 , pp. 1295-1300
    • Dean, D.1
  • 154
    • 0031009673 scopus 로고    scopus 로고
    • Contraction-induced changes in acetyl-CoA carboxylase and 5′-AMP-activated kinase in skeletal muscle
    • Vavvas, D. et al. Contraction-induced changes in acetyl-CoA carboxylase and 5′-AMP-activated kinase in skeletal muscle. J. Biol. Chem. 272, 13255-13261 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 13255-13261
    • Vavvas, D.1
  • 155
    • 0029978799 scopus 로고    scopus 로고
    • Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise
    • Winder, W. W. & Hardie, D. G. Inactivation of acetyl-CoA carboxylase and activation of AMP-activated protein kinase in muscle during exercise. Am. J. Physiol. 270, E299-E304 (1996).
    • (1996) Am. J. Physiol. , vol.270
    • Winder, W.W.1    Hardie, D.G.2
  • 156
    • 0035580981 scopus 로고    scopus 로고
    • Malonyl-CoA decarboxylase is not a substrate of AMP-activated protein kinase in rat fast-twitch skeletal muscle or an islet cell line
    • Habinowski, S. A. et al. Malonyl-CoA decarboxylase is not a substrate of AMP-activated protein kinase in rat fast-twitch skeletal muscle or an islet cell line. Arch. Biochem. Biophys. 396, 71-79 (2001).
    • (2001) Arch. Biochem. Biophys. , vol.396 , pp. 71-79
    • Habinowski, S.A.1
  • 157
    • 0038199737 scopus 로고    scopus 로고
    • Management of cellular energy by the AMP-activated protein kinase system
    • Hardie, D. G., Scott, J. W., Pan, D. A. & Hudson, E. R. Management of cellular energy by the AMP-activated protein kinase system. FEBS Lett. 546, 113-120 (2003).
    • (2003) FEBS Lett. , vol.546 , pp. 113-120
    • Hardie, D.G.1    Scott, J.W.2    Pan, D.A.3    Hudson, E.R.4
  • 158
    • 0345107247 scopus 로고    scopus 로고
    • Complexes between the LKB1 tumor suppressor, STRADα/β and MO25α/β are upstream kinases in the AMP-activated protein kinase cascade
    • Hawley S. A. et al. Complexes between the LKB1 tumor suppressor, STRADα/β and MO25α/β are upstream kinases in the AMP-activated protein kinase cascade. J. Biol. 2, 28 (2003).
    • (2003) J. Biol. , vol.2 , pp. 28
    • Hawley, S.A.1
  • 159
    • 0042160131 scopus 로고    scopus 로고
    • AMPK as a metabolic switch in rat muscle, liver and adipose tissue after exercise
    • Ruderman, N. B. et al. AMPK as a metabolic switch in rat muscle, liver and adipose tissue after exercise. Acta. Physiol. Scand. 178, 435-442 (2003).
    • (2003) Acta Physiol. Scand. , vol.178 , pp. 435-442
    • Ruderman, N.B.1
  • 160
    • 0037341238 scopus 로고    scopus 로고
    • Glucose toxicity in β-cells: Type 2 diabetes, good radicals gone bad, and the glutathione connection
    • Robertson, R. P., Harmon, J., Tran, P. O., Tanaka, Y. & Takahashi, H. Glucose toxicity in β-cells: type 2 diabetes, good radicals gone bad, and the glutathione connection. Diabetes 52, 581-587 (2003).
    • (2003) Diabetes , vol.52 , pp. 581-587
    • Robertson, R.P.1    Harmon, J.2    Tran, P.O.3    Tanaka, Y.4    Takahashi, H.5
  • 161
    • 0036894375 scopus 로고    scopus 로고
    • Genetic manipulations of fatty acid metabolism in β-cells are associated with dysregulated insulin secretion
    • Eto, K. Y. T., Matsui, J., Terauchi, Y., Noda, M. & Kadowaki, T. Genetic manipulations of fatty acid metabolism in β-cells are associated with dysregulated insulin secretion. Diabetes 51, S414-S420 (2002).
    • (2002) Diabetes , vol.51
    • Eto, K.Y.T.1    Matsui, J.2    Terauchi, Y.3    Noda, M.4    Kadowaki, T.5
  • 162
    • 0037593946 scopus 로고    scopus 로고
    • The transcription factor SREBP-1c is instrumental in the development of β-cell dysfunction
    • Wang, H. et al. The transcription factor SREBP-1c is instrumental in the development of β-cell dysfunction. J. Biol. Chem. 278, 16622-16629 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 16622-16629
    • Wang, H.1
  • 163
    • 0036318319 scopus 로고    scopus 로고
    • Lipotoxicity in human pancreatic islets and the protective effect of metformin
    • Lupi, R. et al. Lipotoxicity in human pancreatic islets and the protective effect of metformin. Diabetes 51, S134-S137 (2002).
    • (2002) Diabetes , vol.51
    • Lupi, R.1
  • 164
    • 0029911348 scopus 로고    scopus 로고
    • Prevention of hyperglycemia in the Zucker diabetic fatty rat by treatment with metformin or troglitazone
    • Sreenan, S., Sturis, J., Pugh, W., Burant, C. F. & Polonsky, K. S. Prevention of hyperglycemia in the Zucker diabetic fatty rat by treatment with metformin or troglitazone. Am. J. Physiol. 271, E742-E747 (1996).
    • (1996) Am. J. Physiol. , vol.271
    • Sreenan, S.1    Sturis, J.2    Pugh, W.3    Burant, C.F.4    Polonsky, K.S.5
  • 165
    • 85039532598 scopus 로고    scopus 로고
    • A role for the malonyl-CoA/long chain acyl-CoA pathway of lipid signalling in the regulation of insulin secretion in response to both fuel and non-fuel stimuli
    • (in the press)
    • Roduit, R. et al. A role for the malonyl-CoA/long chain acyl-CoA pathway of lipid signalling in the regulation of insulin secretion in response to both fuel and non-fuel stimuli. Diabetes (in the press).
    • Diabetes
    • Roduit, R.1


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