Base de dados : MEDLINE
Pesquisa : D05.500.562.625.875 [Categoria DeCS]
Referências encontradas : 297 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 30 ir para página                         

  1 / 297 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28768703
[Au] Autor:Lundsgaard AM; Sjøberg KA; Høeg LD; Jeppesen J; Jordy AB; Serup AK; Fritzen AM; Pilegaard H; Myrmel LS; Madsen L; Wojtaszewski JFP; Richter EA; Kiens B
[Ad] Endereço:Section of Molecular Physiology, Department of Nutrition, Exercise and Sports, Faculty of Science, University of Copenhagen, Copenhagen, Denmark.
[Ti] Título:Opposite Regulation of Insulin Sensitivity by Dietary Lipid Versus Carbohydrate Excess.
[So] Source:Diabetes;66(10):2583-2595, 2017 Oct.
[Is] ISSN:1939-327X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:To understand the mechanisms in lipid-induced insulin resistance, a more physiological approach is to enhance fatty acid (FA) availability through the diet. Nine healthy men ingested two hypercaloric diets (in 75% excess of habitual caloric intake) for 3 days, enriched in unsaturated FA (78 energy % [E%] fat) (UNSAT) or carbohydrates (80 E% carbohydrate) (CHO) as well as a eucaloric control diet (CON). Compared with CON, the UNSAT diet reduced whole-body and leg glucose disposal during a hyperinsulinemic-euglycemic clamp, while decreasing hepatic glucose production. In muscle, diacylglycerol (DAG) and intramyocellular triacylglycerol were increased. The accumulated DAG was -1,3 DAG, which is known not to activate PKC, and insulin signaling was intact. UNSAT decreased PDH-E1α protein content and increased inhibitory PDH-E1α Ser phosphorylation and FA oxidation. CHO increased whole-body and leg insulin sensitivity, while increasing hepatic glucose production. After CHO, muscle PDH-E1α Ser phosphorylation was decreased, and glucose oxidation increased. After UNSAT, but not CHO, muscle glucose-6-phosphate content was 103% higher compared with CON during the clamp. Thus, PDH-E1α expression and covalent regulation, and hence the tricarboxylic acid cycle influx of pyruvate-derived acetyl-CoA relative to ß-oxidation-derived acetyl-CoA, are suggested to impact on insulin-stimulated glucose uptake. Taken together, the oxidative metabolic fluxes of glucose and FA are powerful and opposite regulators of insulin action in muscle.
[Mh] Termos MeSH primário: Metabolismo dos Carboidratos/fisiologia
Gorduras na Dieta/efeitos adversos
Resistência à Insulina/fisiologia
[Mh] Termos MeSH secundário: Adulto
Ciclo do Ácido Cítrico/genética
Ciclo do Ácido Cítrico/fisiologia
Diglicerídeos/metabolismo
Ácidos Graxos/sangue
Ácidos Graxos/metabolismo
Seres Humanos
Fígado/metabolismo
Masculino
Músculo Esquelético/metabolismo
Oxirredução
Fosforilação/genética
Fosforilação/fisiologia
Piruvato Desidrogenase (Lipoamida)/genética
Piruvato Desidrogenase (Lipoamida)/metabolismo
Triglicerídeos/metabolismo
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dietary Fats); 0 (Diglycerides); 0 (Fatty Acids); 0 (Triglycerides); EC 1.2.4.1 (Pyruvate Dehydrogenase (Lipoamide)); EC 1.2.4.1 (pyruvate dehydrogenase E1alpha subunit)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170804
[St] Status:MEDLINE
[do] DOI:10.2337/db17-0046


  2 / 297 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28100006
[Au] Autor:Shuai Z; Wang J; Badamagunta M; Choi J; Yang G; Zhang W; Kenny TP; Guggenheim K; Kurth MJ; Ansari AA; Voss J; Coppel RL; Invernizzi P; Leung PSC; Gershwin ME
[Ad] Endereço:Department of Rheumatology and Immunology, The First Affiliated Hospital of Anhui Medical University, Hefei, China.
[Ti] Título:The fingerprint of antimitochondrial antibodies and the etiology of primary biliary cholangitis.
[So] Source:Hepatology;65(5):1670-1682, 2017 May.
[Is] ISSN:1527-3350
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The identification of environmental factors that lead to loss of tolerance has been coined the holy grail of autoimmunity. Our work has focused on the reactivity of antimitochondrial autoantibodies (AMA) to chemical xenobiotics and has hypothesized that a modified peptide within PDC-E2, the major mitochondrial autoantigen, will have been immunologically recognized at the time of loss of tolerance. Herein, we successfully applied intein technology to construct a PDC-E2 protein fragment containing amino acid residues 177-314 of PDC-E2 by joining a recombinant peptide spanning residues 177-252 (PDC-228) with a 62-residue synthetic peptide from 253 to 314 (PP), which encompasses PDC-E2 inner lipoyl domain (ILD). We named this intein-constructed fragment PPL. Importantly, PPL, as well as lipoic acid conjugated PPL (LA-PPL) and xenobiotic 2-octynoic acid conjugated PPL (2OA-PPL), are recognized by AMA. Of great importance, AMA has specificity for the 2OA-modified PDC-E2 ILD peptide backbone distinct from antibodies that react with native lipoylated PDC-E2 peptide. Interestingly, this unique AMA subfraction is of the immunoglobulin M isotype and more dominant in early-stage primary biliary cholangitis (PBC), suggesting that exposure to 2OA-PPL-like compounds occurs early in the generation of AMA. To understand the structural basis of this differential recognition, we analyzed PPL, LA-PPL, and 2OA-PPL using electron paramagnetic resonance spectroscopy, with confirmations by enzyme-linked immunosorbent assay, immunoblotting, and affinity antibody analysis. We demonstrate that the conformation of PDC-E2 ILD is altered when conjugated with 2OA, compared to conjugation with lipoic acid. CONCLUSION: A molecular understanding of the conformation of xenobiotic-modified PDC-E2 is critical for understanding xenobiotic modification and loss of tolerance in PBC with widespread implications for a role of environmental chemicals in the induction of autoimmunity. (Hepatology 2017;65:1670-1682).
[Mh] Termos MeSH primário: Autoanticorpos/sangue
Colangite/induzido quimicamente
Mitocôndrias/imunologia
Piruvato Desidrogenase (Lipoamida)/efeitos dos fármacos
Xenobióticos/toxicidade
[Mh] Termos MeSH secundário: Afinidade de Anticorpos
Estudos de Casos e Controles
Colangite/sangue
Colangite/imunologia
Espectroscopia de Ressonância de Spin Eletrônica
Ensaio de Imunoadsorção Enzimática
Seres Humanos
Inteínas
Piruvato Desidrogenase (Lipoamida)/química
Piruvato Desidrogenase (Lipoamida)/imunologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Autoantibodies); 0 (Xenobiotics); EC 1.2.4.1 (Pyruvate Dehydrogenase (Lipoamide))
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170523
[Lr] Data última revisão:
170523
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170119
[St] Status:MEDLINE
[do] DOI:10.1002/hep.29059


  3 / 297 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28076853
[Au] Autor:Zhong Y; Li X; Ji Y; Li X; Li Y; Yu D; Yuan Y; Liu J; Li H; Zhang M; Ji Z; Fan D; Wen J; Goscinski MA; Yuan L; Hao B; Nesland JM; Suo Z
[Ad] Endereço:Department of Oncology, The First Affiliated Hospital of Zhengzhou University, Zhengzhou, Henan Province, China.
[Ti] Título:Pyruvate dehydrogenase expression is negatively associated with cell stemness and worse clinical outcome in prostate cancers.
[So] Source:Oncotarget;8(8):13344-13356, 2017 Feb 21.
[Is] ISSN:1949-2553
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cells generate adenosine-5'-triphosphate (ATP), the major currency for energy-consuming reactions, through mitochondrial oxidative phosphorylation (OXPHOS) and glycolysis. One of the remarkable features of cancer cells is aerobic glycolysis, also known as the "Warburg Effect", in which cancer cells rely preferentially on glycolysis instead of mitochondrial OXPHOS as the main energy source even in the presence of high oxygen tension. One of the main players in controlling OXPHOS is the mitochondrial gatekeeperpyruvate dehydrogenase complex (PDHc) and its major subunit is E1α (PDHA1). To further analyze the function of PDHA1 in cancer cells, it was knock out (KO) in the human prostate cancer cell line LnCap and a stable KO cell line was established. We demonstrated that PDHA1 gene KO significantly decreased mitochondrial OXPHOS and promoted anaerobic glycolysis, accompanied with higher stemness phenotype including resistance to chemotherapy, enhanced migration ability and increased expression of cancer stem cell markers. We also examined PDHA1 protein expression in prostate cancer tissues by immunohistochemistry and observed that reduced PDHA1 protein expression in clinical prostate carcinomas was significantly correlated with poor prognosis. Collectively, our results show that negative PDHA1 gene expressionis associated with significantly higher cell stemness in prostate cancer cells and reduced protein expression of this gene is associated with shorter clinical outcome in prostate cancers.
[Mh] Termos MeSH primário: Células-Tronco Neoplásicas/patologia
Neoplasias da Próstata/patologia
Piruvato Desidrogenase (Lipoamida)/metabolismo
[Mh] Termos MeSH secundário: Idoso
Idoso de 80 Anos ou mais
Western Blotting
Linhagem Celular Tumoral
Citometria de Fluxo
Técnicas de Inativação de Genes
Seres Humanos
Imuno-Histoquímica
Estimativa de Kaplan-Meier
Masculino
Meia-Idade
Células-Tronco Neoplásicas/enzimologia
Reação em Cadeia da Polimerase
Prognóstico
Neoplasias da Próstata/enzimologia
Neoplasias da Próstata/mortalidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.2.4.1 (Pyruvate Dehydrogenase (Lipoamide)); EC 1.2.4.1 (pyruvate dehydrogenase E1alpha subunit)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170821
[Lr] Data última revisão:
170821
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170112
[St] Status:MEDLINE
[do] DOI:10.18632/oncotarget.14527


  4 / 297 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28028037
[Au] Autor:Gudiksen A; Bertholdt L; Vingborg MB; Hansen HW; Ringholm S; Pilegaard H
[Ad] Endereço:Section for Cell Biology and Physiology, Department of Biology, University of Copenhagen, Copenhagen, Denmark.
[Ti] Título:Muscle interleukin-6 and fasting-induced PDH regulation in mouse skeletal muscle.
[So] Source:Am J Physiol Endocrinol Metab;312(3):E204-E214, 2017 Mar 01.
[Is] ISSN:1522-1555
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fasting prompts a metabolic shift in substrate utilization from carbohydrate to predominant fat oxidation in skeletal muscle, and pyruvate dehydrogenase (PDH) is seen as a controlling link between the competitive oxidation of carbohydrate and fat during metabolic challenges like fasting. Interleukin (IL)-6 has been proposed to be released from muscle with concomitant effects on both glucose and fat utilization. The aim was to test the hypothesis that muscle IL-6 has a regulatory impact on fasting-induced suppression of skeletal muscle PDH. Skeletal muscle-specific IL-6 knockout (IL-6 MKO) mice and floxed littermate controls (control) were either fed or fasted for 6 or 18 h. Lack of muscle IL-6 elevated the respiratory exchange ratio in the fed and early fasting state, but not with prolonged fasting. Activity of PDH in the active form (PDHa) was higher in fed and fasted IL-6 MKO than in control mice at 18 h, but not at 6 h, whereas lack of muscle IL-6 did not prevent downregulation of PDHa activity in skeletal muscle or changes in plasma and muscle substrate levels in response to 18 h of fasting. Phosphorylation of three of four sites on PDH-E1α increased with 18 h of fasting, but was lower in IL-6 MKO mice than in control. In addition, both PDK4 mRNA and protein increased with 6 and 18 h of fasting in both genotypes, but PDK4 protein was lower in IL-6 MKO than in control. In conclusion, skeletal muscle IL-6 seems to regulate whole body substrate utilization in the fed, but not fasted, state and influence skeletal muscle PDHa activity in a circadian manner. However, skeletal muscle IL-6 is not required for maintaining metabolic flexibility in response to fasting.
[Mh] Termos MeSH primário: Jejum/metabolismo
Interleucina-6/genética
Músculo Esquelético/metabolismo
Piruvato Desidrogenase (Lipoamida)/metabolismo
[Mh] Termos MeSH secundário: Animais
Immunoblotting
Imunoprecipitação
Masculino
Camundongos
Camundongos Knockout
Fosforilação
Proteínas Serina-Treonina Quinases/genética
RNA Mensageiro/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Reação em Cadeia da Polimerase Via Transcriptase Reversa
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Interleukin-6); 0 (RNA, Messenger); 0 (interleukin-6, mouse); EC 1.2.4.1 (Pyruvate Dehydrogenase (Lipoamide)); EC 1.2.4.1 (pyruvate dehydrogenase E1alpha subunit); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.2 (pyruvate dehydrogenase (acetyl-transferring) kinase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170626
[Lr] Data última revisão:
170626
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161229
[St] Status:MEDLINE
[do] DOI:10.1152/ajpendo.00291.2016


  5 / 297 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27986918
[Au] Autor:Guo J; Hezaveh S; Tatur J; Zeng AP; Jandt U
[Ad] Endereço:Institute of Bioprocess and Biosystems Engineering, Technische Universität Hamburg, 21073 Hamburg, Germany.
[Ti] Título:Reengineering of the human pyruvate dehydrogenase complex: from disintegration to highly active agglomerates.
[So] Source:Biochem J;474(5):865-875, 2017 Feb 20.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The pyruvate dehydrogenase complex (PDC) plays a central role in cellular metabolism and regulation. As a metabolite-channeling multi-enzyme complex it acts as a complete nanomachine due to its unique geometry and by coupling a cascade of catalytic reactions using 'swinging arms'. Mammalian and specifically human PDC (hPDC) is assembled from multiple copies of E1 and E3 bound to a large E2/E3BP 60-meric core. A less restrictive and smaller catalytic core, which is still active, is highly desired for both fundamental research on channeling mechanisms and also to create a basis for further modification and engineering of new enzyme cascades. Here, we present the first experimental results of the successful disintegration of the E2/E3BP core while retaining its activity. This was achieved by C-terminal α-helixes double truncations (eight residues from E2 and seven residues from E3BP). Disintegration of the hPDC core via double truncations led to the formation of highly active (approximately 70% of wildtype) apparently unordered clusters or agglomerates and inactive non-agglomerated species (hexamer/trimer). After additional deletion of N-terminal 'swinging arms', the aforementioned C-terminal truncations also caused the formation of agglomerates of minimized E2/E3BP complexes. It is likely that these 'swinging arm' regions are not solely responsible for the formation of the large agglomerates.
[Mh] Termos MeSH primário: Acetilcoenzima A/química
Di-Hidrolipoamida Desidrogenase/química
Di-Hidrolipoil-Lisina-Resíduo Acetiltransferase/química
Piruvato Desidrogenase (Lipoamida)/química
Complexo Piruvato Desidrogenase/química
Ácido Pirúvico/química
[Mh] Termos MeSH secundário: Acetilcoenzima A/metabolismo
Sequência de Aminoácidos
Animais
Domínio Catalítico
Clonagem Molecular
Di-Hidrolipoamida Desidrogenase/genética
Di-Hidrolipoamida Desidrogenase/metabolismo
Di-Hidrolipoil-Lisina-Resíduo Acetiltransferase/genética
Di-Hidrolipoil-Lisina-Resíduo Acetiltransferase/metabolismo
Escherichia coli/genética
Escherichia coli/metabolismo
Expressão Gênica
Seres Humanos
Cinética
Mutação
Engenharia de Proteínas
Multimerização Proteica
Estrutura Secundária de Proteína
Piruvato Desidrogenase (Lipoamida)/genética
Piruvato Desidrogenase (Lipoamida)/metabolismo
Complexo Piruvato Desidrogenase/genética
Complexo Piruvato Desidrogenase/metabolismo
Ácido Pirúvico/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Relação Estrutura-Atividade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pyruvate Dehydrogenase Complex); 0 (Recombinant Proteins); 72-89-9 (Acetyl Coenzyme A); 8558G7RUTR (Pyruvic Acid); EC 1.2.4.1 (Pyruvate Dehydrogenase (Lipoamide)); EC 1.8.1.4 (Dihydrolipoamide Dehydrogenase); EC 2.3.1.12 (Dihydrolipoyllysine-Residue Acetyltransferase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170614
[Lr] Data última revisão:
170614
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161218
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20160916


  6 / 297 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27983572
[Au] Autor:Jablonska E; Reszka E; Gromadzinska J; Wieczorek E; Krol MB; Raimondi S; Socha K; Borawska MH; Wasowicz W
[Ad] Endereço:Nofer Institute of Occupational Medicine, Department of Toxicology and Carcinogenesis, Sw. Teresy 8 Street, 91-348 Lodz, Poland. ewa.jablonska@imp.lodz.pl.
[Ti] Título:The Effect of Selenium Supplementation on Glucose Homeostasis and the Expression of Genes Related to Glucose Metabolism.
[So] Source:Nutrients;8(12), 2016 Dec 13.
[Is] ISSN:2072-6643
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:The aim of the study was to evaluate the effect of selenium supplementation on the expression of genes associated with glucose metabolism in humans, in order to explain the unclear relationship between selenium and the risk of diabetes. For gene expression analysis we used archival samples of cDNA from 76 non-diabetic subjects supplemented with selenium in the previous study. The supplementation period was six weeks and the daily dose of selenium was 200 µg (as selenium yeast). Blood for mRNA isolation was collected at four time points: before supplementation, after two and four weeks of supplementation, and after four weeks of washout. The analysis included 15 genes encoding selected proteins involved in insulin signaling and glucose metabolism. In addition, HbA1c and fasting plasma glucose were measured at three and four time points, respectively. Selenium supplementation was associated with a significantly decreased level of HbA1c but not fasting plasma glucose (FPG) and significant down-regulation of seven genes: , , , , , , and . These results suggest that selenium may affect glycemic control at different levels of regulation, linked to insulin signaling, glycolysis, and pyruvate metabolism. Further research is needed to investigate mechanisms of such transcriptional regulation and its potential implication in direct metabolic effects.
[Mh] Termos MeSH primário: Glicemia/efeitos dos fármacos
Glicemia/genética
Regulação da Expressão Gênica/efeitos dos fármacos
Selênio/farmacologia
Oligoelementos/farmacologia
[Mh] Termos MeSH secundário: Adulto
Antígenos CD/sangue
Antígenos CD/metabolismo
Glicemia/metabolismo
Suplementos Nutricionais
Regulação para Baixo/efeitos dos fármacos
Jejum/sangue
Feminino
Genes myc/efeitos dos fármacos
Hemoglobina A Glicada/análise
Hemoglobina A Glicada/efeitos dos fármacos
Homeostase
Seres Humanos
Lactato Desidrogenases/sangue
Lactato Desidrogenases/metabolismo
Masculino
Oxigenases de Função Mista/sangue
Oxigenases de Função Mista/metabolismo
Piruvato Desidrogenase (Lipoamida)/sangue
Piruvato Desidrogenase (Lipoamida)/metabolismo
RNA Mensageiro/sangue
RNA Mensageiro/isolamento & purificação
Receptor de Insulina/sangue
Receptor de Insulina/metabolismo
Receptores de Adiponectina/sangue
Receptores de Adiponectina/metabolismo
Proteínas Repressoras/sangue
Proteínas Repressoras/metabolismo
Selênio/administração & dosagem
Oligoelementos/administração & dosagem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ADIPOR1 protein, human); 0 (Antigens, CD); 0 (Blood Glucose); 0 (Glycated Hemoglobin A); 0 (RNA, Messenger); 0 (Receptors, Adiponectin); 0 (Repressor Proteins); 0 (Trace Elements); 0 (hemoglobin A1c protein, human); EC 1.- (Mixed Function Oxygenases); EC 1.1.- (Lactate Dehydrogenases); EC 1.14.11.- (HIF1AN protein, human); EC 1.2.4.1 (Pyruvate Dehydrogenase (Lipoamide)); EC 2.7.10.1 (INSR protein, human); EC 2.7.10.1 (Receptor, Insulin); H6241UJ22B (Selenium)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161217
[St] Status:MEDLINE


  7 / 297 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27725411
[Au] Autor:Takahashi Y; Tamura Y; Matsunaga Y; Kitaoka Y; Terada S; Hatta H
[Ad] Endereço:Department of Sports Sciences, The University of Tokyo.
[Ti] Título:Effects of Taurine Administration on Carbohydrate Metabolism in Skeletal Muscle during the Post-Exercise Phase.
[So] Source:J Nutr Sci Vitaminol (Tokyo);62(4):257-264, 2016.
[Is] ISSN:1881-7742
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:We previously reported that taurine (2-aminoethanesulfonic acid; dose: 0.5 mg/g body weight) administration after treadmill running at 25 m/min for 90 min increased the glycogen concentration in the skeletal muscle of ICR mice at 120 min after the exercise (Takahashi et al. 2014). In the current study, we further investigated the effects of taurine administration on glycogen repletion and carbohydrate metabolism in the tibialis anterior muscle after endurance exercise. The metabolomic profiles of the tibialis anterior muscle at 120 min after the exercise were analyzed by a capillary electrophoresis-time-of-flight mass spectrometry (n=6). Fructose-1,6-bisphosphate (F1,6P), a glycogenolytic/glycolytic intermediate produced by phosphofructokinase, was significantly lower in the taurine-treated group than that in the control group (p<0.01). Dihydroxyacetonephosphate (DHAP), a downstream product of F1,6P was lower (p=0.05) and glycerol 3-phosphate, a downstream product of F1,6P and DHAP, tended to be lower (p=0.09) in the taurine-treated group than in the controls. At that time, phosphorylated Ser on the E1α subunit of pyruvate dehydrogenase (PDH) tended to be higher in the taurine-treated mice than in the controls (p=0.09, n=5). There was a positive correlation between phosphorylation of the PDH E1α subunit at Ser and glycogen concentration (r=0.73, p<0.05). Our results showed that the enhanced glycogen repletion in skeletal muscle by taurine treatment during the post-exercise phase was accompanied by the lower levels of glycogenolytic/glycolytic intermediates.
[Mh] Termos MeSH primário: Metabolismo dos Carboidratos/efeitos dos fármacos
Músculo Esquelético/efeitos dos fármacos
Condicionamento Físico Animal
Taurina/administração & dosagem
[Mh] Termos MeSH secundário: Animais
Glicerofosfatos/metabolismo
Glicogênio/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos ICR
Músculo Esquelético/metabolismo
Fosforilação
Piruvato Desidrogenase (Lipoamida)/metabolismo
Corrida
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glycerophosphates); 1EQV5MLY3D (Taurine); 9005-79-2 (Glycogen); 9NTI6P3O4X (alpha-glycerophosphoric acid); EC 1.2.4.1 (Pyruvate Dehydrogenase (Lipoamide)); EC 1.2.4.1 (pyruvate dehydrogenase E1alpha subunit)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170512
[Lr] Data última revisão:
170512
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161012
[St] Status:MEDLINE


  8 / 297 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:27379520
[Au] Autor:Li A; Zhang Y; Zhao Z; Wang M; Zan L
[Ad] Endereço:College of Animal Science and Technology, Northwest A&F University, Yangling 712100, Shaanxi, P. R. China.
[Ti] Título:Molecular Characterization and Transcriptional Regulation Analysis of the Bovine PDHB Gene.
[So] Source:PLoS One;11(7):e0157445, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The pyruvate dehydrogenase beta subunit (PDHB) is a subunit of pyruvate dehydrogenase (E1), which catalyzes pyruvate into acetyl-CoA and provides a linkage between the tricarboxylic acid cycle (TCA) and the glycolysis pathway. Previous studies demonstrated PDHB to be positively related to the intramuscular fat (IMF) content. However, the transcriptional regulation of PDHB remains unclear. In our present study, the cDNA of bovine PDHB was cloned and the genomic structure was analyzed. The phylogenetic tree showed bovine PDHB to be closely related to goat and sheep, and least related to chicken. Spatial expression pattern analysis revealed the products of bovine PDHB to be widely expressed with the highest level in the fat of testis. To understand the transcriptional regulation of bovine PDHB, 1899 base pairs (bp) of the 5'-regulatory region was cloned. Sequence analysis neither found consensus TATA-box nor CCAAT-box in the 5'-flanking region of bovine PDHB. However, a CpG island was predicted from nucleotides -284 to +117. Serial deletion constructs of the 5'-flanking region, evaluated in dual-luciferase reporter assay, revealed the core promoter to be located 490bp upstream from the transcription initiation site (+1). Electrophoretic mobility shift assay (EMSA) and chromatin immunoprecipitation assay (ChIP) in combination with asite-directed mutation experiment indicated both myogenin (MYOG) and the CCAAT/enhancer-binding protein beta (C/EBPß) to be important transcription factors for bovine PDHB in skeletal muscle cells and adipocytes. Our results provide an important basis for further investigation of the bovine PDHB function and regulation in cattle.
[Mh] Termos MeSH primário: Região 5´-Flanqueadora/genética
Bovinos/genética
Regulação Enzimológica da Expressão Gênica
Regiões Promotoras Genéticas/genética
Piruvato Desidrogenase (Lipoamida)/genética
[Mh] Termos MeSH secundário: Células 3T3-L1
Tecido Adiposo/metabolismo
Animais
Sequência de Bases
Sítios de Ligação/genética
Proteína beta Intensificadora de Ligação a CCAAT/metabolismo
Linhagem Celular
Clonagem Molecular
Ilhas de CpG/genética
Perfilação da Expressão Gênica/métodos
Masculino
Camundongos
Miogenina/metabolismo
Filogenia
Ligação Proteica
Subunidades Proteicas/genética
Piruvato Desidrogenase (Lipoamida)/classificação
Análise de Sequência de DNA
Homologia de Sequência do Ácido Nucleico
Testículo/metabolismo
Sítio de Iniciação de Transcrição
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CCAAT-Enhancer-Binding Protein-beta); 0 (Myogenin); 0 (Protein Subunits); EC 1.2.4.1 (Pyruvate Dehydrogenase (Lipoamide))
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170731
[Lr] Data última revisão:
170731
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160706
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0157445


  9 / 297 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27357730
[Au] Autor:Zhao H; Pflug BR; Lai X; Wang M
[Ad] Endereço:Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, IN, USA.
[Ti] Título:Pyruvate dehydrogenase alpha 1 as a target of omega-3 polyunsaturated fatty acids in human prostate cancer through a global phosphoproteomic analysis.
[So] Source:Proteomics;16(17):2419-31, 2016 Sep.
[Is] ISSN:1615-9861
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Prostate cancer is one of the leading cancers in men. Taking dietary supplements, such as fish oil (FO), which is rich in n-3 polyunsaturated fatty acids (PUFAs), has been employed as a strategy to lower prostate cancer risk and control disease progression. In this study, we investigated the global phosphoproteomic changes induced by FO using a combination of phosphoprotein-enrichment strategy and high-resolution tandem mass spectrometry. We found that FO induces many more phosphorylation changes than oleic acid when they both are compared to control group. Quantitative comparison between untreated group and FO- or oleic acid-treated groups uncovered a number of important protein phosphorylation changes induced by n-3PUFAs. This phosphoproteomic discovery study and the follow-up Western Blot validation study elucidate that phosphorylation levels of the two regulatory serine residues in pyruvate dehydrogenase alpha 1 (PDHA1), serine-232 and serine-300, are significantly decreased upon FO treatment. As expected, increased pyruvate dehydrogenase activity was also observed. This study suggests that FO-induced phosphorylation changes in PDHA1 is more likely related to the glucose metabolism pathway, and n-3 PUFAs may have a role in controlling the balance between lipid and glucose oxidation.
[Mh] Termos MeSH primário: Ácidos Graxos Ômega-3/uso terapêutico
Óleos de Peixe/uso terapêutico
Fosfoproteínas/metabolismo
Neoplasias da Próstata/dietoterapia
Piruvato Desidrogenase (Lipoamida)/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Animais
Linhagem Celular Tumoral
Suplementos Nutricionais/análise
Seres Humanos
Masculino
Ácidos Oleicos/uso terapêutico
Fosfopeptídeos/análise
Fosfopeptídeos/metabolismo
Fosfoproteínas/análise
Fosforilação
Próstata/metabolismo
Neoplasias da Próstata/metabolismo
Proteoma/análise
Proteoma/metabolismo
Piruvato Desidrogenase (Lipoamida)/química
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acids, Omega-3); 0 (Fish Oils); 0 (Oleic Acids); 0 (Phosphopeptides); 0 (Phosphoproteins); 0 (Proteome); EC 1.2.4.1 (Pyruvate Dehydrogenase (Lipoamide)); EC 1.2.4.1 (pyruvate dehydrogenase E1alpha subunit)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170829
[Lr] Data última revisão:
170829
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160701
[St] Status:MEDLINE
[do] DOI:10.1002/pmic.201600166


  10 / 297 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27343776
[Au] Autor:Pinheiro A; Silva MJ; Pavlu-Pereira H; Florindo C; Barroso M; Marques B; Correia H; Oliveira A; Gaspar A; Tavares de Almeida I; Rivera I
[Ad] Endereço:Metabolism & Genetics Group, Research Institute for Medicines (iMed.ULisboa), Faculty of Pharmacy, Universidade de Lisboa, Portugal.
[Ti] Título:Complex genetic findings in a female patient with pyruvate dehydrogenase complex deficiency: Null mutations in the PDHX gene associated with unusual expression of the testis-specific PDHA2 gene in her somatic cells.
[So] Source:Gene;591(2):417-24, 2016 Oct 15.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Human pyruvate dehydrogenase complex (PDC) catalyzes a key step in the generation of cellular energy and is composed by three catalytic elements (E1, E2, E3), one structural subunit (E3-binding protein), and specific regulatory elements, phosphatases and kinases (PDKs, PDPs). The E1α subunit exists as two isoforms encoded by different genes: PDHA1 located on Xp22.1 and expressed in somatic tissues, and the intronless PDHA2 located on chromosome 4 and only detected in human spermatocytes and spermatids. We report on a young adult female patient who has PDC deficiency associated with a compound heterozygosity in PDHX encoding the E3-binding protein. Additionally, in the patient and in all members of her immediate family, a full-length testis-specific PDHA2 mRNA and a 5'UTR-truncated PDHA1 mRNA were detected in circulating lymphocytes and cultured fibroblasts, being both mRNAs translated into full-length PDHA2 and PDHA1 proteins, resulting in the co-existence of both PDHA isoforms in somatic cells. Moreover, we observed that DNA hypomethylation of a CpG island in the coding region of PDHA2 gene is associated with the somatic activation of this gene transcription in these individuals. This study represents the first natural model of the de-repression of the testis-specific PDHA2 gene in human somatic cells, and raises some questions related to the somatic activation of this gene as a potential therapeutic approach for most forms of PDC deficiency.
[Mh] Termos MeSH primário: Mutação
Piruvato Desidrogenase (Lipoamida)/genética
Doença da Deficiência do Complexo de Piruvato Desidrogenase/genética
Complexo Piruvato Desidrogenase/genética
[Mh] Termos MeSH secundário: Adulto
Células Cultivadas
Feminino
Fibroblastos/metabolismo
Dosagem de Genes
Expressão Gênica
Heterozigoto
Seres Humanos
Masculino
Complexo Piruvato Desidrogenase/metabolismo
RNA Mensageiro
Testículo/metabolismo
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (PDHX protein, human); 0 (Pyruvate Dehydrogenase Complex); 0 (RNA, Messenger); EC 1.2.4.1 (PDHA2 protein, human); EC 1.2.4.1 (Pyruvate Dehydrogenase (Lipoamide))
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170127
[Lr] Data última revisão:
170127
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160626
[St] Status:MEDLINE



página 1 de 30 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde