Search results for "PDK4"

showing 3 items of 3 documents

Activation of PPARβ/δ prevents hyperglycaemia-induced impairment of Kv7 channels and cAMP-mediated relaxation in rat coronary arteries.

2016

PPARβ/δ activation protects against endothelial dysfunction in diabetic models. Elevated glucose is known to impair cAMP-induced relaxation and Kv channel function in coronary arteries (CA). Herein, we aimed to analyse the possible protective effects of the PPARβ/δ agonist GW0742 on the hyperglycaemic-induced impairment of cAMP-induced relaxation and Kv channel function in rat CA. As compared with low glucose (LG), incubation under high glucose (HG) conditions attenuated the relaxation induced by the adenylate cyclase activator forskolin in CA and this was prevented by GW0742. The protective effect of GW0742 was supressed by a PPARβ/δ antagonist. In myocytes isolated from CA under LG, forsk…

0301 basic medicineAgonistMalemedicine.medical_specialtymedicine.drug_classPDK4Protein Serine-Threonine Kinasesmedicine.disease_causeGW0742Diabetes Mellitus Experimental03 medical and health scienceschemistry.chemical_compoundInternal medicinemedicineCyclic AMPAnimalsHumansPPAR deltaRats WistarPPAR-betaForskolinAntagonistPyruvate Dehydrogenase Acetyl-Transferring KinaseGeneral MedicineHyperpolarization (biology)Coronary VesselsPotassium channelRatsVasodilationThiazoles030104 developmental biologyEndocrinologychemistryHyperglycemiaKCNQ1 Potassium ChannelReactive Oxygen SpeciesOxidative stressClinical science (London, England : 1979)
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PPARβ activation restores the high glucose-induced impairment of insulin signalling in endothelial cells

2014

Background and Purpose PPARβ enhances insulin sensitivity in adipocytes and skeletal muscle cells, but its effects on insulin signalling in endothelial cells are not known. We analysed the effects of the PPARβ/δ (PPARβ) agonists, GW0742 and L165041, on impaired insulin signalling induced by high glucose in HUVECs and aortic and mesenteric arteries from diabetic rats. Experimental Approach Insulin-stimulated NO production, Akt-Ser 473 and eNOS-Ser 1177 phosphorylation, and reactive oxygen species (ROS) production were studied in HUVECs incubated in low- or high-glucose medium. Insulin-stimulated relaxations and protein phosphorylation in vessels from streptozotocin (STZ)-induced diabetic rat…

2. Zero hungerPharmacologymedicine.medical_specialtyPyruvate dehydrogenase kinaseInsulinmedicine.medical_treatmentPDK4Oxidative phosphorylationBiologyStreptozotocinmedicine.diseaseInsulin resistanceEndocrinologyInternal medicinemedicinePhosphorylationProtein phosphorylationmedicine.drugBritish Journal of Pharmacology
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Effects of high-fat diet and physical activity on pyruvate dehydrogenase kinase-4 in mouse skeletal muscle

2012

Abstract Background The expression of PDK4 is elevated by diabetes, fasting and other conditions associated with the switch from the utilization of glucose to fatty acids as an energy source. It is previously shown that peroxisome proliferator-activated receptor γ coactivator 1α (PGC-1α), a master regulator of energy metabolism, coactivates in cell lines pyruvate dehydrogenase kinase-4 (PDK4) gene expression via the estrogen-related receptor α (ERRα). We investigated the effects of long-term high-fat diet and physical activity on the expression of PDK4, PGC-1α and ERRα and the amount and function of mitochondria in skeletal muscle. Methods Insulin resistance was induced by a high-fat (HF) d…

medicine.medical_specialtyPyruvate dehydrogenase kinaseEndocrinology Diabetes and MetabolismPDK4Skeletal muscleMedicine (miscellaneous)lcsh:TX341-641Pyruvate dehydrogenase phosphataseBiologyInternal medicineCoactivatormedicinelcsh:RC620-627Nutrition and DieteticsResearchSkeletal muscleFuel switchingPeroxisomePyruvate dehydrogenase complexLipidsMitochondrialcsh:Nutritional diseases. Deficiency diseasesEndocrinologymedicine.anatomical_structureGlucoseBiochemistryEnergy sourcelcsh:Nutrition. Foods and food supplyNutrition & Metabolism
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