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

No abstract is available for this paper.

• Publication year

  2004

• Venue

  Nature reviews. Drug discovery

• Publication date

  2004-04-01

• Fields of study

  Medicine

• Identifiers
  DOI 10.1038/nrd1344
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar

• No claims are published for this paper.

• No concepts are published for this paper.

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  2005cited by this paper
• Pioglitazone treatment activates AMP-activated protein kinase in rat liver and adipose tissue in vivo.

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• A role for the malonyl-CoA/long-chain acyl-CoA pathway of lipid signaling in the regulation of insulin secretion in response to both fuel and nonfuel stimuli.

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• Effects of chronic AICAR treatment on fiber composition, enzyme activity, UCP3, and PGC-1 in rat muscles.

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• AMPK as a metabolic switch in rat muscle, liver and adipose tissue after exercise.

  2003cited by this paper
• The Transcription Factor SREBP-1c Is Instrumental in the Development of β-Cell Dysfunction*

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• Glucose autoregulates its uptake in skeletal muscle: involvement of AMP-activated protein kinase.

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• Physical exercise-induced hyperinsulinemic hypoglycemia is an autosomal-dominant trait characterized by abnormal pyruvate-induced insulin release.

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• Minireview: malonyl CoA, AMP-activated protein kinase, and adiposity.

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• Activation of peroxisome proliferator-activated receptor δ induces fatty acid β-oxidation in skeletal muscle and attenuates metabolic syndrome

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• Management of cellular energy by the AMP‐activated protein kinase system

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• Triglyceride accumulation protects against fatty acid-induced lipotoxicity

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• Involvement of AMP-activated protein kinase in glucose uptake stimulated by the globular domain of adiponectin in primary rat adipocytes.

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• The Anti-diabetic Drugs Rosiglitazone and Metformin Stimulate AMP-activated Protein Kinase through Distinct Signaling Pathways*

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• Diet-induced insulin resistance in mice lacking adiponectin/ACRP30

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• Hyperglycemia-induced apoptosis in human umbilical vein endothelial cells: inhibition by the AMP-activated protein kinase activation.

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• Malonyl-CoA signaling, lipid partitioning, and glucolipotoxicity: role in beta-cell adaptation and failure in the etiology of diabetes.

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• Adiponectin stimulates glucose utilization and fatty-acid oxidation by activating AMP-activated protein kinase

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• Lipotoxic diseases.

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• AMP kinase is required for mitochondrial biogenesis in skeletal muscle in response to chronic energy deprivation

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• Metformin increases AMP-activated protein kinase activity in skeletal muscle of subjects with type 2 diabetes.

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• The antidiabetic drug metformin activates the AMP-activated protein kinase cascade via an adenine nucleotide-independent mechanism.

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• Stimulation of acetyl-CoA carboxylase gene expression by glucose requires insulin release and sterol regulatory element binding protein 1c in pancreatic MIN6 beta-cells.

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• Free fatty acid-induced hepatic insulin resistance: a potential role for protein kinase C-delta.

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• Leptin-replacement therapy for lipodystrophy.

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• Alcoholic steatosis and steatohepatitis.

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• Genetic manipulations of fatty acid metabolism in beta-cells are associated with dysregulated insulin secretion.

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• 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*

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• Enhanced muscle fat oxidation and glucose transport by ACRP30 globular domain: Acetyl–CoA carboxylase inhibition and AMP-activated protein kinase activation

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• Minireview: Secondary β-Cell Failure in Type 2 Diabetes-A Convergence of Glucotoxicity and Lipotoxicity.

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• Malonyl-CoA decarboxylase is not a substrate of AMP-activated protein kinase in rat fast-twitch skeletal muscle or an islet cell line.

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• Reversal of Obesity- and Diet-Induced Insulin Resistance with Salicylates or Targeted Disruption of Ikkβ

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• The AMP‐activated protein kinase prevents ceramide synthesis de novo and apoptosis in astrocytes

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• AMP-activated protein kinase regulates gene expression by direct phosphorylation of nuclear proteins.

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• Insulin and contraction directly stimulate UCP2 and UCP3 mRNA expression in rat skeletal muscle in vitro.

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• Regulation of muscle GLUT-4 transcription by AMP-activated protein kinase.

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• Diseases of liporegulation: new perspective on obesity and related disorders

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• Acute Regulation of Fatty Acid Oxidation and AMP-Activated Protein Kinase in Human Umbilical Vein Endothelial Cells

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• Role of AMP-activated protein kinase in mechanism of metformin action.

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• Dysregulation of Fatty Acid Metabolism in the Etiology of Type 2 Diabetes

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• AMP-activated protein kinase, super metabolic regulator.

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• Animal Models of Steatosis

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• AMP-activated protein kinase and hepatic genes involved in glucose metabolism.

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• Proteolytic cleavage product of 30-kDa adipocyte complement-related protein increases fatty acid oxidation in muscle and causes weight loss in mice.

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• Malonyl-CoA and AMP-activated protein kinase (AMPK): possible links between insulin resistance in muscle and early endothelial cell damage in diabetes.

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• Hepatocyte Nuclear Factor-4α Involved in Type 1 Maturity-Onset Diabetes of the Young Is a Novel Target of AMP-Activated Protein Kinase

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• Skeletal muscle lipid content and insulin resistance: evidence for a paradox in endurance-trained athletes.

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• The fat-derived hormone adiponectin reverses insulin resistance associated with both lipoatrophy and obesity

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• Continuous Fatty Acid Oxidation and Reduced Fat Storage in Mice Lacking Acetyl-CoA Carboxylase 2

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• 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*

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• 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) beta-cells.

  2001cited by this paper
• A role for AMP-activated protein kinase in contraction- and hypoxia-regulated glucose transport in skeletal muscle.

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