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[PMID]:29270996
[Au] Autor:Maldonado MR; Bracht L; de Sá-Nakanishi AB; Corrêa RCG; Comar JF; Peralta RM; Bracht A
[Ad] Endereço:Department of Biochemistry, University of Maringá, Maringá, Brazil.
[Ti] Título:Actions of p-synephrine on hepatic enzyme activities linked to carbohydrate metabolism and ATP levels in vivo and in the perfused rat liver.
[So] Source:Cell Biochem Funct;36(1):4-12, 2018 Jan.
[Is] ISSN:1099-0844
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:p-Synephrine is one of the main active components of the fruit of Citrus aurantium (bitter orange). Extracts of the bitter orange and other preparations containing p-synephrine have been used worldwide to promote weight loss and for sports performance. The purpose of the study was to measure the action of p-synephrine on hepatic enzyme activities linked to carbohydrate and energy metabolism and the levels of adenine mononucleotides. Enzymes and adenine mononucleotides were measured in the isolated perfused rat liver and in vivo after oral administration of the drug (50 and 300 mg/kg) by using standard techniques. p-Synephrine increased the activity of glycogen phosphorylase in vivo and in the perfused liver. It decreased, however, the activities of pyruvate kinase and pyruvate dehydrogenase also in vivo and in the perfused liver. p-Synephrine increased the hepatic pools of adenosine diphosphate and adenosine triphosphate. Stimulation of glycogen phosphorylase is consistent with the reported increased glycogenolysis in the perfused liver and increased glycemia in rats. The decrease in the pyruvate dehydrogenase activity indicates that p-synephrine is potentially capable of inhibiting the transformation of carbohydrates into lipids. The capability of increasing the adenosine triphosphate-adenosine diphosphate pool indicates a beneficial effect of p-synephrine on the cellular energetics.
[Mh] Termos MeSH primário: Trifosfato de Adenosina/metabolismo
Metabolismo dos Carboidratos/efeitos dos fármacos
Fígado/efeitos dos fármacos
Fígado/enzimologia
Sinefrina/farmacologia
[Mh] Termos MeSH secundário: Administração Oral
Animais
Citrus/química
Glicogênio Fosforilase/metabolismo
Fígado/irrigação sanguínea
Fígado/cirurgia
Masculino
Complexo Piruvato Desidrogenase/antagonistas & inibidores
Complexo Piruvato Desidrogenase/metabolismo
Piruvato Quinase/antagonistas & inibidores
Piruvato Quinase/metabolismo
Ratos
Ratos Wistar
Sinefrina/administração & dosagem
Sinefrina/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pyruvate Dehydrogenase Complex); 8L70Q75FXE (Adenosine Triphosphate); EC 2.4.1.- (Glycogen Phosphorylase); EC 2.7.1.40 (Pyruvate Kinase); PEG5DP7434 (Synephrine)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180308
[Lr] Data última revisão:
180308
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171223
[St] Status:MEDLINE
[do] DOI:10.1002/cbf.3311


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[PMID]:29231630
[Au] Autor:Bliksrud YT
[Ti] Título:Tenuous link between chronic fatigue syndrome and pyruvate dehydrogenase deficiency.
[Ti] Título:Svak kobling mellom kronisk utmattelsessyndrom og pyruvat dehydrogenasemangel..
[So] Source:Tidsskr Nor Laegeforen;137(23-24), 2017 12 12.
[Is] ISSN:0807-7096
[Cp] País de publicação:Norway
[La] Idioma:eng; nor
[Mh] Termos MeSH primário: Síndrome de Fadiga Crônica
Complexo Piruvato Desidrogenase/metabolismo
[Mh] Termos MeSH secundário: Síndrome de Fadiga Crônica/etiologia
Síndrome de Fadiga Crônica/metabolismo
Seres Humanos
Doença da Deficiência do Complexo de Piruvato Desidrogenase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pyruvate Dehydrogenase Complex)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180301
[Lr] Data última revisão:
180301
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171213
[St] Status:MEDLINE
[do] DOI:10.4045/tidsskr.17.0948


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[PMID]:29297219
[Au] Autor:Lucenko MT; Andrievskaya IA; Dolzhikova IV
[Ti] Título:Energy Metabolism in the Placenta and the Role of Disturbances in the Development of Placental Insufficiency at an Exacerbation of Cytomegalovirus Infection.
[So] Source:Vestn Ross Akad Med Nauk;71(3):177-82, 2016.
[Is] ISSN:0869-6047
[Cp] País de publicação:Russia (Federation)
[La] Idioma:eng
[Ab] Resumo:Objective: Determine the characteristics of placental energy metabolism and to establish its role in the development of placental insufficiency at an exacerbation of cytomegalovirus (CMV) infection in 25­28 weeks of gestation. Methods: In a prospective study of the case-control type included pregnant, delivery on term of 37­38 weeks. The sample of 50 pregnant women, including 25 CMV-seropositive with exacerbation of CMV infection at 25­28 weeks of gestation and with the titer of IgG antibodies to CMV 1: 1600 at the time of the study and 25 CMV-seronegative women the same pregnancy. The study was conducted at the obstetric department of pathology of pregnancy and laboratory «Etiopathogenesis mechanisms and recovery processes with non-specific lung diseases¼ Far Eastern Scientific Center of Physiology and Pathology of Respiration together with the urban maternity ward at City Hospital in the period from 2014 to 2015. The activity of pyruvate dehydrogenase, α-ketoglutarate dehydrogenase and a dehydrogenase lipoic acid was determined by histochemical methods on cryostat sections of fresh frozen tissue placenta by the method of R. Lilly. Evaluation of the intensity of histochemical reactions carried out by the program cytophotometry Scion. The morphology of the placenta was studied in paraffin sections stained with hematoxylin Böhmer-eosin, van Gieson's picrofuchsin and alcian blue by Steedman. Results: Exacerbation of CMV infection at 25­28 weeks of gestation leads to a decrease in the intensity of the histochemical reaction of pyruvate dehydrogenase in 2.4 times, lipoic acid dehydrogenase ­ in 2.9 times, and α-ketoglutarate dehydrogenase ­ in 1.5 times in the syncytiotrophoblast villous placenta. The placental morphological structure study showed villi in a state of death or necrotic changes, as well as increasing the number of avascular immature villi. In the maternal part of the placenta were marked constriction clearances, hypertrophy of muscle and connective tissue layers blood vessels. Conclusion: The findings suggest that the exacerbation of CMV infection at 25­28 weeks of pregnancy causes a decrease in the intensity of energy metabolism in the placenta by suppressing the activity of the enzymes α-ketoglutarate dehydrogenase and pyruvate dehydrogenase complex, which is accompanied by disturbances of the morphological structure of the placental barrier, the development of placental insufficiency.
[Mh] Termos MeSH primário: Infecções por Citomegalovirus
Complexo Cetoglutarato Desidrogenase/metabolismo
Insuficiência Placentária/metabolismo
Complicações Infecciosas na Gravidez
Complexo Piruvato Desidrogenase/metabolismo
Trofoblastos
[Mh] Termos MeSH secundário: Adulto
Estudos de Casos e Controles
Citomegalovirus/isolamento & purificação
Infecções por Citomegalovirus/diagnóstico
Infecções por Citomegalovirus/metabolismo
Infecções por Citomegalovirus/fisiopatologia
Metabolismo Energético
Feminino
Seres Humanos
Insuficiência Placentária/diagnóstico
Gravidez
Complicações Infecciosas na Gravidez/diagnóstico
Complicações Infecciosas na Gravidez/metabolismo
Complicações Infecciosas na Gravidez/fisiopatologia
Estatística como Assunto
Trofoblastos/metabolismo
Trofoblastos/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pyruvate Dehydrogenase Complex); EC 1.2.4.2 (Ketoglutarate Dehydrogenase Complex)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180104
[St] Status:MEDLINE


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[PMID]:29059435
[Au] Autor:Stacpoole PW
[Ad] Endereço:Division of Endocrinology, Diabetes and Metabolism, Department of Medicine, and Department of Biochemistry and Molecular Biology, University of Florida College of Medicine, Gainesville, FL.
[Ti] Título:Therapeutic Targeting of the Pyruvate Dehydrogenase Complex/Pyruvate Dehydrogenase Kinase (PDC/PDK) Axis in Cancer.
[So] Source:J Natl Cancer Inst;109(11), 2017 Nov 01.
[Is] ISSN:1460-2105
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The mitochondrial pyruvate dehydrogenase complex (PDC) irreversibly decarboxylates pyruvate to acetyl coenzyme A, thereby linking glycolysis to the tricarboxylic acid cycle and defining a critical step in cellular bioenergetics. Inhibition of PDC activity by pyruvate dehydrogenase kinase (PDK)-mediated phosphorylation has been associated with the pathobiology of many disorders of metabolic integration, including cancer. Consequently, the PDC/PDK axis has long been a therapeutic target. The most common underlying mechanism accounting for PDC inhibition in these conditions is post-transcriptional upregulation of one or more PDK isoforms, leading to phosphorylation of the E1α subunit of PDC. Such perturbations of the PDC/PDK axis induce a "glycolytic shift," whereby affected cells favor adenosine triphosphate production by glycolysis over mitochondrial oxidative phosphorylation and cellular proliferation over cellular quiescence. Dichloroacetate is the prototypic xenobiotic inhibitor of PDK, thereby maintaining PDC in its unphosphorylated, catalytically active form. However, recent interest in the therapeutic targeting of the PDC/PDK axis for the treatment of cancer has yielded a new generation of small molecule PDK inhibitors. Ongoing investigations of the central role of PDC in cellular energy metabolism and its regulation by pharmacological effectors of PDKs promise to open multiple exciting vistas into the biochemical understanding and treatment of cancer and other diseases.
[Mh] Termos MeSH primário: Neoplasias/tratamento farmacológico
Neoplasias/metabolismo
Complexo Piruvato Desidrogenase/antagonistas & inibidores
[Mh] Termos MeSH secundário: Acetilcoenzima A/metabolismo
Trifosfato de Adenosina/biossíntese
Biomimética
Ciclo do Ácido Cítrico/fisiologia
Ácido Dicloroacético/farmacologia
Metabolismo Energético
Glicólise
Seres Humanos
Isoenzimas/metabolismo
Mitocôndrias/metabolismo
NAD/metabolismo
Fosforilação Oxidativa
Proteínas Serina-Treonina Quinases/metabolismo
Complexo Piruvato Desidrogenase/metabolismo
Ácido Pirúvico/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Isoenzymes); 0 (Pyruvate Dehydrogenase Complex); 0U46U6E8UK (NAD); 72-89-9 (Acetyl Coenzyme A); 8558G7RUTR (Pyruvic Acid); 8L70Q75FXE (Adenosine Triphosphate); 9LSH52S3LQ (Dichloroacetic Acid); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.11.2 (pyruvate dehydrogenase (acetyl-transferring) kinase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171024
[St] Status:MEDLINE
[do] DOI:10.1093/jnci/djx071


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[PMID]:28934276
[Au] Autor:Piao L; Fang YH; Kubler MM; Donnino MW; Sharp WW
[Ad] Endereço:Section of Emergency Medicine; Department of Medicine, University of Chicago, Chicago, Illinois, United States of America.
[Ti] Título:Enhanced pyruvate dehydrogenase activity improves cardiac outcomes in a murine model of cardiac arrest.
[So] Source:PLoS One;12(9):e0185046, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:RATIONALE: Post-ischemic changes in cellular metabolism alter myocardial and neurological function. Pyruvate dehydrogenase (PDH), the limiting step in mitochondrial glucose oxidation, is inhibited by increased expression of PDH kinase (PDK) during ischemia/reperfusion injury. This results in decreased utilization of glucose to generate cellular ATP. Post-cardiac arrest (CA) hypothermia improves outcomes and alters metabolism, but its influence on PDH and PDK activity following CA are unknown. We hypothesized that therapeutic hypothermia (TH) following CA is associated with the inhibition of PDK activity and increased PDH activity. We further hypothesized that an inhibitor of PDK activity, dichloroacetate (DCA), would improve PDH activity and post-CA outcomes. METHODS AND RESULTS: Anesthetized and ventilated adult female C57BL/6 wild-type mice underwent a 12-minute KCl-induced CA followed by cardiopulmonary resuscitation. Compared to normothermic (37°C) CA controls, administering TH (30°C) improved overall survival (72-hour survival rate: 62.5% vs. 28.6%, P<0.001), post-resuscitation myocardial function (ejection fraction: 50.9±3.1% vs. 27.2±2.0%, P<0.001; aorta systolic pressure: 132.7±7.3 vs. 72.3±3.0 mmHg, P<0.001), and neurological scores at 72-hour post CA (9.5±1.3 vs. 5.4±1.3, P<0.05). In both heart and brain, CA increased lactate concentrations (1.9-fold and 3.1-fold increase, respectively, P<0.01), decreased PDH enzyme activity (24% and 50% reduction, respectively, P<0.01), and increased PDK protein expressions (1.2-fold and 1.9-fold, respectively, P<0.01). In contrast, post-CA treatment with TH normalized lactate concentrations (P<0.01 and P<0.05) and PDK expressions (P<0.001 and P<0.05), while increasing PDH activity (P<0.01 and P<0.01) in both the heart and brain. Additionally, treatment with DCA (0.2 mg/g body weight) 30 min prior to CA improved both myocardial hemodynamics 2 hours post-CA (aortic systolic pressure: 123±3 vs. 96±4 mmHg, P<0.001) and 72-hour survival rates (50% vs. 19%, P<0.05) in normothermic animals. CONCLUSIONS: Enhanced PDH activity in the setting of TH or DCA administration is associated with improved post-CA resuscitation outcomes. PDH is a promising therapeutic target for improving post-CA outcomes.
[Mh] Termos MeSH primário: Ácido Dicloroacético/uso terapêutico
Parada Cardíaca/terapia
Hipotermia Induzida
Complexo Piruvato Desidrogenase/metabolismo
[Mh] Termos MeSH secundário: Animais
Reanimação Cardiopulmonar
Terapia Combinada
Feminino
Parada Cardíaca/enzimologia
Parada Cardíaca/mortalidade
Hemodinâmica
Camundongos
Camundongos Endogâmicos C57BL
Taxa de Sobrevida
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pyruvate Dehydrogenase Complex); 9LSH52S3LQ (Dichloroacetic Acid)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170922
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0185046


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[PMID]:28886081
[Au] Autor:Wan X; Liu Y; Zhao Y; Sun X; Fan D; Guo L
[Ad] Endereço:Department of Medical Oncology, First Affiliated Hospital, China Medical University, Shenyang, Liaoning, P.R. China.
[Ti] Título:Orexin A affects HepG2 human hepatocellular carcinoma cells glucose metabolism via HIF-1α-dependent and -independent mechanism.
[So] Source:PLoS One;12(9):e0184213, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Orexins are hypothalamic neuropeptides that regulate feeding, reward, wakefulness and energy homeostasis. The present study sought to characterize the involvement of orexin A in glucose metabolism in HepG2 human hepatocellular carcinoma cells, and investigated the role of hypoxia-inducible factor-1α (HIF-1α) in the response. HepG2 cells were exposed to different concentrations of orexin A (10-9 to 10-7 M) in vitro, without or with the orexin receptor 1 (OX1R) inhibitor (SB334867), HIF-1α inhibitor (YC-1) or a combination of both inhibitors. Subsequently, OX1R, HIF-1α expression and localization, glucose uptake, glucose transporter 1 (GLUT1) expression and ATP content were measured. We further investigated the intracellular fate of glucose by measuring the gene expression of pyruvate dehydrogenase kinase 1 (PDK1), lactate dehydrogenase (LDHA) and pyruvate dehydrogenase B (PDHB), as well as metabolite levels including lactate generation and mitochondrial pyruvate dehydrogenase (PDH) activity. The activity of phosphoinositide 3-kinase (PI3K)/Akt/mammalian target of rapamycin (mTOR) pathway was also assessed. Our results showed that the expression of OX1R was predominantly located in the nucleus in HepG2 cells. Orexin A oxygen-independently promoted the mRNA and protein expression of HIF-1α as well as its nuclear accumulation in HepG2 cells and the elevated HIF-1α protein was associated, at least partly, with the activation of the PI3K/Akt/mTOR pathway. Orexin A stimulated GLUT1 expression, glucose uptake as well as ATP generation in HepG2 cells via OX1R acting through the HIF-1α pathway. Moreover, orexin A inhibited LDHA, PDK1 expression and lactate production, stimulated PDHB expression and PDH enzyme activity independent of HIF-1α. Our results indicated that orexin signaling facilitated the glucose flux into mitochondrial oxidative metabolism rather than glycolysis in HepG2 cells. These findings provide new insight into the regulation of glucose metabolism by orexin A in hepatocellular carcinoma cells.
[Mh] Termos MeSH primário: Carcinoma Hepatocelular/metabolismo
Glucose/metabolismo
Subunidade alfa do Fator 1 Induzível por Hipóxia/metabolismo
Neoplasias Hepáticas/metabolismo
Redes e Vias Metabólicas/efeitos dos fármacos
Orexinas/farmacologia
[Mh] Termos MeSH secundário: Trifosfato de Adenosina/metabolismo
Carcinoma Hepatocelular/genética
Ciclo do Ácido Cítrico/efeitos dos fármacos
Expressão Gênica
Regulação da Expressão Gênica/efeitos dos fármacos
Transportador de Glucose Tipo 1/genética
Transportador de Glucose Tipo 1/metabolismo
Glicólise
Células Hep G2
Seres Humanos
Ácido Láctico/metabolismo
Neoplasias Hepáticas/genética
Receptores de Orexina/genética
Receptores de Orexina/metabolismo
Fosfatidilinositol 3-Quinases/metabolismo
Transporte Proteico
Proteínas Proto-Oncogênicas c-akt/metabolismo
Complexo Piruvato Desidrogenase/metabolismo
Transdução de Sinais/efeitos dos fármacos
Serina-Treonina Quinases TOR/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glucose Transporter Type 1); 0 (Hypoxia-Inducible Factor 1, alpha Subunit); 0 (Orexin Receptors); 0 (Orexins); 0 (Pyruvate Dehydrogenase Complex); 33X04XA5AT (Lactic Acid); 8L70Q75FXE (Adenosine Triphosphate); EC 2.7.1.- (Phosphatidylinositol 3-Kinases); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.11.1 (Proto-Oncogene Proteins c-akt); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170909
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0184213


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[PMID]:28767746
[Au] Autor:Di W; Jia MX; Xu J; Li BL; Liu Y
[Ad] Endereço:Beijing Laboratory of Urban and Rural Ecological Environment, Beijing Key Laboratory of Ornamental Plants Germplasm Innovation and Molecular Breeding, National Engineering Research Center for Floriculture, College of Landscape Architecture, Beijing Forestry University, Beijing China.
[Ti] Título:Exogenous Catalase and Pyruvate Dehydrogenase Improve Survival and Regeneration and Affect Oxidative Stress in Cryopreserved Dendrobium nobile Protocorm-like Bodies.
[So] Source:Cryo Letters;38(3):228-238, 2017 May/Jun.
[Is] ISSN:0143-2044
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Reactive oxygen species (ROS)-induced oxidative damage is responsible for viability loss in plant tissues following cryopreservation. Antioxidants may improve viability by preventing or repairing the injury. OBJECTIVE: This work aimed at studying the effect of catalase (CAT) and pyruvate dehydrogenase (PDH), which are involved in ROS metabolism and are differentially expressed during pollen cryopreservation, for cryopreservation of Dendrobium nobile Lindl. 'Hamana Lake Dream' protocorm-like bodies (PLBs). MATERIALS AND METHODS: Different concentrations of exogenous CAT or PDH were added at the loading, PVS2 treatment, unloading steps during vitrification-cryopreservation of PLBs. Their survival and regeneration were evaluated and correlated with physiological oxidative indexes. RESULTS: PLB survival increased significantly when CAT and PDH were added separately to the unloading solution at a suitable concentration. CAT at 400 U·ml increased PLB survival and regeneration by 33.5 and 14.6 percent respectively. It had no impact on the production of superoxide anion radical (·O2-) and on superoxide dismutase (SOD) activity, but it reduced the hydrogen peroxide (H O ) and malondialdehyde (MDA) contents and enhanced ascorbic acid (AsA) and endogenous CAT levels compared to PLBs cryopreserved using the standard vitrification protocol (CK1). PDH at 0.1 U·ml significantly improved PLB survival (by 2.5 percent), but it had no marked effect on regeneration compared to the CK1 group. It induced the same variations in ·O2-, AsA and endogenous CAT levels that were observed following CAT addition. However, PDH did not affect the H O and MDA content but significantly increased SOD activity. CONCLUSION: These results indicate that the addition of 400 U·ml CAT and 0.1 U·ml PDH at the unloading step increased survival of cryopreserved PLBs and that this improvement was associated with scavenging of H O and the repair of oxidative damage. Exogenous CAT also significantly improved PLB regeneration after cryopreservation, while PDH had no obvious effect. The effect of exogenous CAT on PLB survival and regeneration was stronger than that of PDH, which may be due to the increased SOD activity by PDH addition.
[Mh] Termos MeSH primário: Catalase/farmacologia
Dendrobium
Estresse Oxidativo/efeitos dos fármacos
Complexo Piruvato Desidrogenase/farmacologia
[Mh] Termos MeSH secundário: Antioxidantes/farmacologia
Catalase/metabolismo
Criopreservação/métodos
Dendrobium/efeitos dos fármacos
Dendrobium/enzimologia
Estresse Oxidativo/fisiologia
Complexo Piruvato Desidrogenase/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Regeneração/efeitos dos fármacos
Vitrificação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Pyruvate Dehydrogenase Complex); 0 (Reactive Oxygen Species); EC 1.11.1.6 (Catalase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170831
[Lr] Data última revisão:
170831
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170803
[St] Status:MEDLINE


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[PMID]:28632902
[Au] Autor:McDonald TS; Borges K
[Ad] Endereço:Department of Pharmacology, School of Biomedical Sciences, The University of Queensland, St. Lucia, Queensland, Australia.
[Ti] Título:Impaired hippocampal glucose metabolism during and after flurothyl-induced seizures in mice: Reduced phosphorylation coincides with reduced activity of pyruvate dehydrogenase.
[So] Source:Epilepsia;58(7):1172-1180, 2017 Jul.
[Is] ISSN:1528-1167
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVE: To determine changes in glucose metabolism and the enzymes involved in the hippocampus ictally and postictally in the acute mouse flurothyl seizure model. METHODS: [U- C]-Glucose was injected (i.p.) prior to, or following a 5 min flurothyl-induced seizure. Fifteen minutes later, mice were killed and the total metabolite levels and % C enrichment were analyzed in the hippocampal formation using gas chromatography-mass spectrometry. Activities of key metabolic and antioxidant enzymes and the phosphorylation status of pyruvate dehydrogenase were measured, along with lipid peroxidation. RESULTS: During seizures, total lactate levels increased 1.7-fold; however, [M + 3] enrichment of both lactate and alanine were reduced by 30% and 43%, respectively, along with a 28% decrease in phosphofructokinase activity. Postictally the % C enrichments of all measured tricarboxylic acid (TCA) cycle intermediates and the amino acids were reduced by 46-93%. At this time, pyruvate dehydrogenase (PDH) activity was 56% of that measured in controls, and there was a 1.9-fold increase in the phosphorylation of PDH at ser232. Phosphorylation of PDH is known to decrease its activity. SIGNIFICANCE: Here, we show that the increase of lactate levels during flurothyl seizures is from a source other than [U- C]-glucose, such as glycogen. Surprisingly, although we saw a reduction in phosphofructokinase activity during the seizure, metabolism of [U- C]-glucose into the TCA cycle seemed unaffected. Similar to our recent findings in the chronic phase of the pilocarpine model, postictally the metabolism of glucose by glycolysis and the TCA cycle was impaired along with reduced PDH activity. Although this decrease in activity may be a protective mechanism to reduce oxidative stress, which is observed in the flurothyl model, ATP is critical to the recovery of ion and neurotransmitter balance and return to normal brain function. Thus we identified promising novel strategies to enhance energy metabolism and recovery from seizures.
[Mh] Termos MeSH primário: Glicemia/metabolismo
Flurotila
Hipocampo/efeitos dos fármacos
Hipocampo/fisiopatologia
Complexo Piruvato Desidrogenase/metabolismo
Convulsões/induzido quimicamente
Convulsões/fisiopatologia
[Mh] Termos MeSH secundário: Alanina/metabolismo
Aminoácidos/metabolismo
Animais
Antioxidantes/metabolismo
Ciclo do Ácido Cítrico/efeitos dos fármacos
Ciclo do Ácido Cítrico/fisiologia
Cromatografia Gasosa-Espectrometria de Massas
Glicogênio/metabolismo
Ácido Láctico/metabolismo
Peroxidação de Lipídeos/efeitos dos fármacos
Peroxidação de Lipídeos/fisiologia
Masculino
Camundongos
Camundongos Endogâmicos
Fosfofrutoquinases/metabolismo
Fosforilação/fisiologia
Convulsões/patologia
Superóxido Dismutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids); 0 (Antioxidants); 0 (Blood Glucose); 0 (Pyruvate Dehydrogenase Complex); 33X04XA5AT (Lactic Acid); 9005-79-2 (Glycogen); 9Z467FG2YK (Flurothyl); EC 1.15.1.1 (Superoxide Dismutase); EC 2.7.1 - (Phosphofructokinases); OF5P57N2ZX (Alanine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170621
[St] Status:MEDLINE
[do] DOI:10.1111/epi.13796


  9 / 3332 MEDLINE  
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[PMID]:28564592
[Au] Autor:Miki Y; Tanji K; Mori F; Kakita A; Takahashi H; Wakabayashi K
[Ad] Endereço:Department of Neuropathology, Institute of Brain Science, Hirosaki University Graduate School of Medicine, Hirosaki 036-8562, Japan. Electronic address: yasuomiki@hotmail.com.
[Ti] Título:Alteration of mitochondrial protein PDHA1 in Lewy body disease and PARK14.
[So] Source:Biochem Biophys Res Commun;489(4):439-444, 2017 Aug 05.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The histopathological hallmark of Parkinson's disease (PD) and dementia with Lewy bodies (DLB) is the occurrence of insoluble fibrillary aggregates known as Lewy bodies. Mitochondria play a vital role in energy production, and the pathogenesis of PD is associated with altered cellular metabolism due to mitochondrial dysfunction. The pyruvate dehydrogenase (PDH) complex provides a primary step in aerobic glucose metabolism by catalyzing the oxidative decarboxylation of pyruvate to acetyl CoA. Pyruvate dehydrogenase alpha 1 (PDHA1) forms the core structure of the PDH complex. Dysfunction of the PDH complex leads to energy production failure, resulting in various neurological disorders. However, no study has investigated the involvement of PDHA1 in the pathogenesis of PD. In the present study, we performed immunohistochemistry and immunoblotting to clarify the involvement of PDHA1 in idiopathic PD, DLB, PARK14-linked parkinsonism (PARK14; a familial form of PD), and multiple system atrophy, in comparison with normal controls. Here we report PDHA1 as a new component of brainstem-type Lewy bodies in idiopathic PD, DLB and PARK14, the level of PDHA1 protein being significantly decreased in the putamen and substantia nigra of patients with idiopathic PD. Our findings suggest that alteration of glucose metabolism through dysfunction of the PDH complex might occur in the pathogenesis of Lewy body disease and PARK14.
[Mh] Termos MeSH primário: Doença por Corpos de Lewy/enzimologia
Doença por Corpos de Lewy/metabolismo
Proteínas Mitocondriais/metabolismo
Transtornos Parkinsonianos/enzimologia
Transtornos Parkinsonianos/metabolismo
Complexo Piruvato Desidrogenase/metabolismo
[Mh] Termos MeSH secundário: Idoso
Idoso de 80 Anos ou mais
Células HeLa
Seres Humanos
Meia-Idade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Mitochondrial Proteins); 0 (Pyruvate Dehydrogenase Complex)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170601
[St] Status:MEDLINE


  10 / 3332 MEDLINE  
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[PMID]:28539364
[Au] Autor:Guo X; Niemi NM; Coon JJ; Pagliarini DJ
[Ad] Endereço:From the Morgridge Institute for Research, Madison, Wisconsin 53715.
[Ti] Título:Integrative proteomics and biochemical analyses define Ptc6p as the pyruvate dehydrogenase phosphatase.
[So] Source:J Biol Chem;292(28):11751-11759, 2017 Jul 14.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The pyruvate dehydrogenase complex (PDC) is the primary metabolic checkpoint connecting glycolysis and mitochondrial oxidative phosphorylation and is important for maintaining cellular and organismal glucose homeostasis. Phosphorylation of the PDC E1 subunit was identified as a key inhibitory modification in bovine tissue ∼50 years ago, and this regulatory process is now known to be conserved throughout evolution. Although is a pervasive model organism for investigating cellular metabolism and its regulation by signaling processes, the phosphatase(s) responsible for activating the PDC in has not been conclusively defined. Here, using comparative mitochondrial phosphoproteomics, analyses of protein-protein interactions by affinity enrichment-mass spectrometry, and biochemistry, we define Ptc6p as the primary PDC phosphatase in Our analyses further suggest additional substrates for related phosphatases and describe the overall phosphoproteomic changes that accompany mitochondrial respiratory dysfunction. In summary, our quantitative proteomics and biochemical analyses have identified Ptc6p as the primary-and likely sole- PDC phosphatase, closing a key knowledge gap about the regulation of yeast mitochondrial metabolism. Our findings highlight the power of integrative omics and biochemical analyses for annotating the functions of poorly characterized signaling proteins.
[Mh] Termos MeSH primário: Fosfoproteínas Fosfatases/metabolismo
Processamento de Proteína Pós-Traducional
Complexo Piruvato Desidrogenase/metabolismo
Proteínas de Saccharomyces cerevisiae/metabolismo
Saccharomyces cerevisiae/enzimologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Bioquímica/métodos
Sequência Conservada
Bases de Dados de Proteínas
Ativação Enzimática
Técnicas de Inativação de Genes
Imunoprecipitação
Fosfoproteínas Fosfatases/genética
Fosforilação
Filogenia
Proteômica/métodos
Proteínas Recombinantes de Fusão/metabolismo
Proteínas de Saccharomyces cerevisiae/genética
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
Especificidade por Substrato
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Pyruvate Dehydrogenase Complex); 0 (Recombinant Fusion Proteins); 0 (Saccharomyces cerevisiae Proteins); EC 3.1.3.16 (PTC6 protein, S cerevisiae); EC 3.1.3.16 (Phosphoprotein Phosphatases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170803
[Lr] Data última revisão:
170803
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.787341



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