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Pesquisa : D08.811.682.047.820.150 [Categoria DeCS]
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[PMID]:28923398
[Au] Autor:Sun LN; Zhi Z; Chen LY; Zhou Q; Li XM; Gan WJ; Chen S; Yang M; Liu Y; Shen T; Xu Y; Li JM
[Ad] Endereço:Department of Pathology and Pathophysiology, Medical College of Soochow University, Soochow University, Suzhou 215123, People's Republic of China.
[Ti] Título:SIRT1 suppresses colorectal cancer metastasis by transcriptional repression of miR-15b-5p.
[So] Source:Cancer Lett;409:104-115, 2017 Nov 28.
[Is] ISSN:1872-7980
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:The class III deacetylase sirtuin 1 (SIRT1), a member of the sirtuin family proteins, plays a key role in many types of cancers including colorectal cancer (CRC). Here we report that SIRT1 suppressed CRC metastasis in vitro and in vivo as a negative regulator for miR-15b-5p transcription. Mechanistically, SIRT1 impaired regulatory effects of activator protein (AP-1) on miR-15b-5p trans-activation through deacetylation of AP-1. Importantly, acyl-CoA oxidase 1 (ACOX1), a key enzyme of the fatty acid oxidation (FAO) pathway, was found as a direct target for miR-15b-5p. SIRT1 expression was positively correlated with ACOX1 expression in CRC cells and in xenografts. Moreover, ACOX1 overexpression attenuated the augmentation of migration and invasion of CRC cells by miR-15b-5p overexpression. In conclusion, our study demonstrated a functional role of the SIRT1/miR-15b-5p/ACOX1 axis in CRC metastasis and suggested a potential target for metastatic CRC therapy.
[Mh] Termos MeSH primário: Neoplasias Colorretais/genética
MicroRNAs/genética
Sirtuína 1/genética
[Mh] Termos MeSH secundário: 3-Hidroxiacil-CoA Desidrogenases/metabolismo
Acetil-CoA C-Aciltransferase/metabolismo
Animais
Células CACO-2
Isomerases de Ligação Dupla Carbono-Carbono/metabolismo
Linhagem Celular Tumoral
Neoplasias Colorretais/metabolismo
Neoplasias Colorretais/patologia
Enoil-CoA Hidratase/metabolismo
Células HCT116
Células HT29
Xenoenxertos
Seres Humanos
Camundongos
Camundongos Endogâmicos BALB C
Camundongos Nus
MicroRNAs/metabolismo
Metástase Neoplásica
Racemases e Epimerases/metabolismo
Transdução de Sinais
Sirtuína 1/metabolismo
Transcrição Genética
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MIRN15 microRNA, human); 0 (MicroRNAs); 0 (fatty acid oxidation complex); EC 1.1.1.- (3-Hydroxyacyl CoA Dehydrogenases); EC 2.3.1.16 (Acetyl-CoA C-Acyltransferase); EC 3.5.1.- (SIRT1 protein, human); EC 3.5.1.- (Sirtuin 1); EC 4.2.1.17 (Enoyl-CoA Hydratase); EC 5.1.- (Racemases and Epimerases); EC 5.3.3.- (Carbon-Carbon Double Bond Isomerases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170920
[St] Status:MEDLINE


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[PMID]:28791828
[Au] Autor:Mozrzymas R; Konikowska K; Regulska-Ilow B
[Ad] Endereço:Regional Specialist Hospital in Wroclaw, Research and Development Center, Poland.
[Ti] Título:Energy exchangers with LCT as a precision method for diet control in LCHADD.
[So] Source:Adv Clin Exp Med;26(3):515-525, 2017 May-Jun.
[Is] ISSN:1899-5276
[Cp] País de publicação:Poland
[La] Idioma:eng
[Ab] Resumo:Long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency (LCHADD) is a rare genetic disease. The LCHADD treatment is mainly based on special diet. In this diet, energy from long-chain triglycerides (LCT) cannot exceed 10%, however energy intake from the consumption of medium-chain triglycerides (MCTs) should increase. The daily intake of energy should be compatible with energy requirements and treatment should involve frequent meals including during the night to avoid periods of fasting. In fact, there are no recommendations for total content of LCT in all of the allowed food in the LCHADD diet. The aim of the study was to present a new method of diet composition in LCHADD with the use of blocks based on energy exchangers with calculated LCT content. In the study, the diet schema was shown for calculating the energy requirements and LCT content in the LCHADD diet. How to create the diet was also shown, based on a food pyramid developed for patients with LCHADD. The blocks will make it possible, in a quick and simple way, to create a balanced diet which provides adequate energy value, essential nutrients and LCT content. This method can be used by doctors and dietitians who specialize in treating rare metabolic diseases. It can also be used by patients and their families for accurate menu planning with limited LCT content.
[Mh] Termos MeSH primário: 3-Hidroxiacil-CoA Desidrogenases/deficiência
Cardiomiopatias/dietoterapia
Ingestão de Energia/fisiologia
Erros Inatos do Metabolismo Lipídico/dietoterapia
Miopatias Mitocondriais/dietoterapia
Proteína Mitocondrial Trifuncional/deficiência
Doenças do Sistema Nervoso/dietoterapia
Rabdomiólise/dietoterapia
Triglicerídeos/metabolismo
[Mh] Termos MeSH secundário: Adulto
Idoso
Cardiomiopatias/metabolismo
Criança
Pré-Escolar
Dieta/métodos
Feminino
Seres Humanos
Lactente
Recém-Nascido
Erros Inatos do Metabolismo Lipídico/metabolismo
Masculino
Meia-Idade
Miopatias Mitocondriais/metabolismo
Proteína Mitocondrial Trifuncional/metabolismo
Doenças do Sistema Nervoso/metabolismo
Rabdomiólise/metabolismo
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Triglycerides); EC 1.1.1.- (3-Hydroxyacyl CoA Dehydrogenases); EC 2.3.1.16 (Mitochondrial Trifunctional Protein)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171004
[Lr] Data última revisão:
171004
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170810
[St] Status:MEDLINE
[do] DOI:10.17219/acem/62132


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[PMID]:28526709
[Au] Autor:Thapa D; Zhang M; Manning JR; Guimarães DA; Stoner MW; O'Doherty RM; Shiva S; Scott I
[Ad] Endereço:Division of Cardiology, Department of Medicine, University of Pittsburgh, Pittsburgh, Pennsylvania.
[Ti] Título:Acetylation of mitochondrial proteins by GCN5L1 promotes enhanced fatty acid oxidation in the heart.
[So] Source:Am J Physiol Heart Circ Physiol;313(2):H265-H274, 2017 Aug 01.
[Is] ISSN:1522-1539
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lysine acetylation is a reversible posttranslational modification and is particularly important in the regulation of mitochondrial metabolic enzymes. Acetylation uses acetyl-CoA derived from fuel metabolism as a cofactor, thereby linking nutrition to metabolic activity. In the present study, we investigated how mitochondrial acetylation status in the heart is controlled by food intake and how these changes affect mitochondrial metabolism. We found that there was a significant increase in cardiac mitochondrial protein acetylation in mice fed a long-term high-fat diet and that this change correlated with an increase in the abundance of the mitochondrial acetyltransferase-related protein GCN5L1. We showed that the acetylation status of several mitochondrial fatty acid oxidation enzymes (long-chain acyl-CoA dehydrogenase, short-chain acyl-CoA dehydrogenase, and hydroxyacyl-CoA dehydrogenase) and a pyruvate oxidation enzyme (pyruvate dehydrogenase) was significantly upregulated in high-fat diet-fed mice and that the increase in long-chain and short-chain acyl-CoA dehydrogenase acetylation correlated with increased enzymatic activity. Finally, we demonstrated that the acetylation of mitochondrial fatty acid oxidation proteins was decreased after GCN5L1 knockdown and that the reduced acetylation led to diminished fatty acid oxidation in cultured H9C2 cells. These data indicate that lysine acetylation promotes fatty acid oxidation in the heart and that this modification is regulated in part by the activity of GCN5L1. Recent research has shown that acetylation of mitochondrial fatty acid oxidation enzymes has greatly contrasting effects on their activity in different tissues. Here, we provide new evidence that acetylation of cardiac mitochondrial fatty acid oxidation enzymes by GCN5L1 significantly upregulates their activity in diet-induced obese mice.
[Mh] Termos MeSH primário: Acetiltransferases/metabolismo
Metabolismo Energético
Ácidos Graxos/metabolismo
Mitocôndrias Cardíacas/enzimologia
Proteínas Mitocondriais/metabolismo
Miócitos Cardíacos/enzimologia
Proteínas do Tecido Nervoso/metabolismo
Obesidade/enzimologia
Processamento de Proteína Pós-Traducional
[Mh] Termos MeSH secundário: 3-Hidroxiacil-CoA Desidrogenases/genética
3-Hidroxiacil-CoA Desidrogenases/metabolismo
Acetilação
Acetiltransferases/genética
Acil-CoA Desidrogenase/genética
Acil-CoA Desidrogenase/metabolismo
Animais
Linhagem Celular
Dieta Hiperlipídica
Modelos Animais de Doenças
Regulação Enzimológica da Expressão Gênica
Lisina
Masculino
Camundongos Endogâmicos C57BL
Proteínas Mitocondriais/genética
Proteínas do Tecido Nervoso/genética
Obesidade/genética
Oxirredução
Complexo Piruvato Desidrogenase/genética
Complexo Piruvato Desidrogenase/metabolismo
Interferência de RNA
Ratos
Sirtuína 3/genética
Sirtuína 3/metabolismo
Sirtuínas/genética
Sirtuínas/metabolismo
Fatores de Tempo
Transfecção
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acids); 0 (GCN5L1 protein, rat); 0 (Gcn5l1 protein, mouse); 0 (Mitochondrial Proteins); 0 (Nerve Tissue Proteins); 0 (Pyruvate Dehydrogenase Complex); 0 (SIRT-3 protein, rat); 0 (Sirt3 protein, mouse); EC 1.1.1.- (3-Hydroxyacyl CoA Dehydrogenases); EC 1.3.8.7 (Acyl-CoA Dehydrogenase); EC 2.3.1.- (Acetyltransferases); EC 3.5.1.- (Sirtuin 3); EC 3.5.1.- (Sirtuins); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171122
[Lr] Data última revisão:
171122
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170521
[St] Status:MEDLINE
[do] DOI:10.1152/ajpheart.00752.2016


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[PMID]:28188816
[Au] Autor:Dilly SJ; Clark AJ; Marsh A; Mitchell DA; Cain R; Fishwick CW; Taylor PC
[Ad] Endereço:ValiRx plc, 3rd Floor, 16 Upper Woburn Place, London, WC1H 0BS, UK.
[Ti] Título:A chemical genomics approach to drug reprofiling in oncology: Antipsychotic drug risperidone as a potential adenocarcinoma treatment.
[So] Source:Cancer Lett;393:16-21, 2017 May 01.
[Is] ISSN:1872-7980
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Drug reprofiling is emerging as an effective paradigm for discovery of cancer treatments. Herein, an antipsychotic drug is immobilised using the Magic Tag chemical genomics tool and screened against a T7 bacteriophage displayed library of polypeptides from Drosophila melanogaster, as a whole genome model, to uncover an interaction with a section of 17-ß-HSD10, a proposed prostate cancer target. A computational study and enzyme inhibition assay with full length human 17-ß-HSD10 identifies risperidone as a drug reprofiling candidate. When formulated with rumenic acid, risperidone slows proliferation of PC3 prostate cancer cells in vitro and retards PC3 prostate cancer tumour growth in vivo in xenografts in mice, presenting an opportunity to reprofile risperidone as a cancer treatment.
[Mh] Termos MeSH primário: 17-Hidroxiesteroide Desidrogenases/antagonistas & inibidores
3-Hidroxiacil-CoA Desidrogenases/antagonistas & inibidores
Adenocarcinoma/tratamento farmacológico
Antineoplásicos/farmacologia
Antipsicóticos/farmacologia
Drosophila melanogaster/efeitos dos fármacos
Reposicionamento de Medicamentos/métodos
Inibidores Enzimáticos/farmacologia
Genômica/métodos
Neoplasias da Próstata/tratamento farmacológico
Risperidona/farmacologia
[Mh] Termos MeSH secundário: 17-Hidroxiesteroide Desidrogenases/química
17-Hidroxiesteroide Desidrogenases/genética
17-Hidroxiesteroide Desidrogenases/metabolismo
3-Hidroxiacil-CoA Desidrogenases/química
3-Hidroxiacil-CoA Desidrogenases/genética
3-Hidroxiacil-CoA Desidrogenases/metabolismo
Adenocarcinoma/enzimologia
Adenocarcinoma/genética
Animais
Antineoplásicos/química
Antipsicóticos/química
Bacteriófago T7/genética
Linhagem Celular Tumoral
Proliferação Celular/efeitos dos fármacos
Relação Dose-Resposta a Droga
Drosophila melanogaster/enzimologia
Drosophila melanogaster/genética
Composição de Medicamentos
Inibidores Enzimáticos/química
Biblioteca Gênica
Seres Humanos
Ácidos Linoleicos Conjugados/química
Masculino
Camundongos Nus
Simulação de Acoplamento Molecular
Terapia de Alvo Molecular
Neoplasias da Próstata/enzimologia
Neoplasias da Próstata/genética
Conformação Proteica
Risperidona/química
Relação Estrutura-Atividade
Fatores de Tempo
Carga Tumoral/efeitos dos fármacos
Ensaios Antitumorais Modelo de Xenoenxerto
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antineoplastic Agents); 0 (Antipsychotic Agents); 0 (Enzyme Inhibitors); 0 (Linoleic Acids, Conjugated); 1839-11-8 (9,11-linoleic acid); EC 1.1.- (17 beta-hydroxysteroid dehydrogenase type 10, Drosophila); EC 1.1.- (17-Hydroxysteroid Dehydrogenases); EC 1.1.1.- (3-Hydroxyacyl CoA Dehydrogenases); EC 1.1.1.35 (HSD17B10 protein, human); L6UH7ZF8HC (Risperidone)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170814
[Lr] Data última revisão:
170814
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170212
[St] Status:MEDLINE


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[PMID]:28082069
[Au] Autor:Hroch L; Guest P; Benek O; Soukup O; Janockova J; Dolezal R; Kuca K; Aitken L; Smith TK; Gunn-Moore F; Zala D; Ramsay RR; Musilek K
[Ad] Endereço:Charles University in Prague, Faculty of Pharmacy in Hradec Kralove, Department of Pharmaceutical Chemistry and Drug Control, Heyrovskeho 1203, 500 05 Hradec Kralove, Czech Republic; University Hospital, Biomedical Research Center, Sokolska 581, 500 05 Hradec Kralove, Czech Republic.
[Ti] Título:Synthesis and evaluation of frentizole-based indolyl thiourea analogues as MAO/ABAD inhibitors for Alzheimer's disease treatment.
[So] Source:Bioorg Med Chem;25(3):1143-1152, 2017 Feb 01.
[Is] ISSN:1464-3391
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Alzheimer's disease (AD) is a neurodegenerative disorder associated with an excessive accumulation of amyloid-beta peptide (Aß). Based on the multifactorial nature of AD, preparation of multi-target-directed ligands presents a viable option to address more pathological events at one time. A novel class of asymmetrical disubstituted indolyl thioureas have been designed and synthesized to interact with monoamine oxidase (MAO) and/or amyloid-binding alcohol dehydrogenase (ABAD). The design combines the features of known MAO inhibitors scaffolds (e.g. rasagiline or ladostigil) and a frentizole moiety with potential to interact with ABAD. Evaluation against MAO identified several compounds that inhibited in the low to moderate micromolar range. The most promising compound (19) inhibited human MAO-A and MAO-B with IC values of 6.34µM and 0.30µM, respectively. ABAD activity evaluation did not show any highly potent compound, but the compound series allowed identification of structural features to assist the future development of ABAD inhibitors. Finally, several of the compounds were found to be potent inhibitors of horseradish peroxidase (HRP), preventing the use of the Amplex™ Red assay to detect hydrogen peroxide produced by MAO, highlighting the need for serious precautions when using an enzyme-coupled assay.
[Mh] Termos MeSH primário: 3-Hidroxiacil-CoA Desidrogenases/antagonistas & inibidores
Doença de Alzheimer/tratamento farmacológico
Benzotiazóis/farmacologia
Inibidores Enzimáticos/farmacologia
Monoaminoxidase/metabolismo
Compostos de Fenilureia/farmacologia
Tioureia/farmacologia
[Mh] Termos MeSH secundário: 3-Hidroxiacil-CoA Desidrogenases/metabolismo
Doença de Alzheimer/metabolismo
Benzotiazóis/química
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Seres Humanos
Estrutura Molecular
Compostos de Fenilureia/química
Relação Estrutura-Atividade
Tioureia/síntese química
Tioureia/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Benzothiazoles); 0 (Enzyme Inhibitors); 0 (Phenylurea Compounds); 7EY946394I (frentizole); EC 1.1.1.- (3-Hydroxyacyl CoA Dehydrogenases); EC 1.1.1.35 (HSD17B10 protein, human); EC 1.4.3.4 (Monoamine Oxidase); GYV9AM2QAG (Thiourea)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170114
[St] Status:MEDLINE


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[PMID]:28012365
[Au] Autor:Boerrigter-Eenling R; Alewijn M; Weesepoel Y; van Ruth S
[Ad] Endereço:Wageningen University and Research, RIKILT Wageningen Research, P.O. Box 230, 6700 AE Wageningen, The Netherlands. Electronic address: rita.boerrigter-eenling@wur.nl.
[Ti] Título:New approaches towards discrimination of fresh/chilled and frozen/thawed chicken breasts by HADH activity determination: Customized slope fitting and chemometrics.
[So] Source:Meat Sci;126:43-49, 2017 Apr.
[Is] ISSN:1873-4138
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Fresh/chilled chicken breasts retail at a higher price than their frozen/thawed counterparts. Verification of the fresh/thawed status of chicken meat is determined by measuring ß-hydroxyacyl-Coenzyme A-hydrogenase (HADH) activity present in meat intra-cellular liquids spectrophotometrically. However, considerable numbers of reference samples are required for the current arithmetic method, adding to laboratory costs. Therefore, two alternative mathematical approaches which do not require such reference samples were developed and evaluated: curve fitting and multivariate classification. The approaches were developed using 55 fresh/thawed fillet samples. The performance of the methods was examined by an independent validation set which consisted of 16 samples. Finally, the approach was tested in practice in a market study. With the exception of two minor false classifications, both newly proposed methods performed equally well as the classical method. All three methods were able to identify two apparent fraudulent cases in the market study. Therefore, the experiments showed that the costs of HADH measurements can be reduced by adapting alternative mathematics.
[Mh] Termos MeSH primário: 3-Hidroxiacil-CoA Desidrogenases/metabolismo
Manipulação de Alimentos
Produtos Avícolas/análise
[Mh] Termos MeSH secundário: Animais
Galinhas
Congelamento
Modelos Teóricos
Análise Multivariada
Reprodutibilidade dos Testes
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.1.1.- (3-Hydroxyacyl CoA Dehydrogenases)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170713
[Lr] Data última revisão:
170713
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161225
[St] Status:MEDLINE


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[PMID]:27836993
[Au] Autor:Irshad Z; Dimitri F; Christian M; Zammit VA
[Ad] Endereço:Translational and Experimental Medicine, Division of Biomedical Sciences, Warwick Medical School, CV4 7AL, United Kingdom.
[Ti] Título:Diacylglycerol acyltransferase 2 links glucose utilization to fatty acid oxidation in the brown adipocytes.
[So] Source:J Lipid Res;58(1):15-30, 2017 Jan.
[Is] ISSN:1539-7262
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Brown adipose tissue uptake of glucose and fatty acids is very high during nonshivering thermogenesis. Adrenergic stimulation markedly increases glucose uptake, de novo lipogenesis, and FA oxidation simultaneously. The mechanism that enables this concerted response has hitherto been unknown. Here, we find that in primary brown adipocytes and brown adipocyte-derived cell line (IMBAT-1), acute inhibition and longer-term knockdown of DGAT2 links the increased de novo synthesis of fatty acids from glucose to a pool of TAG that is simultaneously hydrolyzed, providing FA for mitochondrial oxidation. DGAT1 does not contribute to this pathway, but uses exogenous FA and glycerol to synthesize a functionally distinct pool of TAG to which DGAT2 also contributes. The DGAT2-dependent channelling of C from glucose into TAG and CO was reproduced in ß3-agonist-stimulated primary brown adipocytes. Knockdown of DGAT2 in IMBAT-1 affected the mRNA levels of UCP1 and genes important in FA activation and esterification. Therefore, in ß3-agonist activated brown adipocytes, DGAT2 specifically enables channelling of de novo synthesized FA into a rapidly mobilized pool of TAG, which is simultaneously hydrolyzed to provide substrates for mitochondrial fatty acid oxidation.
[Mh] Termos MeSH primário: Adipócitos Marrons/metabolismo
Diacilglicerol O-Aciltransferase/genética
Ácidos Graxos/metabolismo
Metabolismo dos Lipídeos/genética
[Mh] Termos MeSH secundário: 3-Hidroxiacil-CoA Desidrogenases/metabolismo
Acetil-CoA C-Aciltransferase/metabolismo
Animais
Isomerases de Ligação Dupla Carbono-Carbono/metabolismo
Linhagem Celular
Enoil-CoA Hidratase/metabolismo
Esterificação
Regulação da Expressão Gênica/genética
Técnicas de Silenciamento de Genes
Glucose/metabolismo
Lipogênese/genética
Camundongos
Oxirredução
Racemases e Epimerases/metabolismo
Triglicerídeos/metabolismo
Proteína Desacopladora 1/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acids); 0 (Triglycerides); 0 (Ucp1 protein, mouse); 0 (Uncoupling Protein 1); 0 (fatty acid oxidation complex); EC 1.1.1.- (3-Hydroxyacyl CoA Dehydrogenases); EC 2.3.1.16 (Acetyl-CoA C-Acyltransferase); EC 2.3.1.20 (DGAT2 protein, mouse); EC 2.3.1.20 (Dgat1 protein, mouse); EC 2.3.1.20 (Diacylglycerol O-Acyltransferase); EC 4.2.1.17 (Enoyl-CoA Hydratase); EC 5.1.- (Racemases and Epimerases); EC 5.3.3.- (Carbon-Carbon Double Bond Isomerases); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170922
[Lr] Data última revisão:
170922
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161113
[St] Status:MEDLINE
[do] DOI:10.1194/jlr.M068197


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[PMID]:27793615
[Au] Autor:Liang S; Li W; Zhang Y; Tang X; He J; Bai Y; Li D; Wang Y; Chen Q
[Ad] Endereço:School of Life Sciences, Lanzhou University, 222 Tian Shui South Road, 730000 Lanzhou, China.
[Ti] Título:Seasonal variation of metabolism in lizard Phrynocephalus vlangalii at high altitude.
[So] Source:Comp Biochem Physiol A Mol Integr Physiol;203:341-347, 2017 Jan.
[Is] ISSN:1531-4332
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Seasonal acclimatization is important for animals to live optimally in the varying environment. Phrynocephalus vlangalii, a species of lizard endemic in China, distributes on Qinghai-Tibet Plateau ranging from 2000 to 4600m above sea level. To dissect how this lizard mediate metabolism to adapt various season, the preferred body temperature (Tb), standard metabolic rate (SMR), mitochondrial respiration rates and activities of four metabolic enzymes in this species were tested in different seasons (spring, summer, and autumn). The results showed that the preferred Tb was the lowest in spring and the highest in summer. SMR, maximal mitochondrial respiration rates in liver and skeletal muscle were the highest in spring. Similarly, higher activities of lactate dehydrogenase (LDH), citrate synthase (CS) and cytochrome c oxidase (CCO) activities of liver and skeletal muscle were observed in spring. However, ß-hydroxyacyl coenzyme A dehydrogenase (HOAD) activities of liver and skeletal muscle were higher in autumn. On the whole, seasonal variation of metabolism is the highest in spring and the lowest in summer. Seasonal variation of metabolism is the opposite of preferred body temperature, this may be one of the mechanisms to adapt to the environment in P. vlangalii. Our results suggested that P. vlangalii at high altitude has certain adaptive characteristics on metabolism in different seasons.
[Mh] Termos MeSH primário: Aclimatação
Regulação da Temperatura Corporal
Metabolismo Energético
Fígado/metabolismo
Lagartos/fisiologia
Músculo Esquelético/metabolismo
[Mh] Termos MeSH secundário: 3-Hidroxiacil-CoA Desidrogenases/metabolismo
Altitude
Animais
Comportamento Animal
China
Citrato (si)-Sintase/metabolismo
Complexo IV da Cadeia de Transporte de Elétrons/metabolismo
Hibernação
L-Lactato Desidrogenase/metabolismo
Fígado/enzimologia
Masculino
Mitocôndrias Hepáticas/enzimologia
Mitocôndrias Hepáticas/metabolismo
Mitocôndrias Musculares/enzimologia
Mitocôndrias Musculares/metabolismo
Músculo Esquelético/enzimologia
Estações do Ano
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.1.1.- (3-Hydroxyacyl CoA Dehydrogenases); EC 1.1.1.27 (L-Lactate Dehydrogenase); EC 1.9.3.1 (Electron Transport Complex IV); EC 2.3.3.1 (Citrate (si)-Synthase)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170726
[Lr] Data última revisão:
170726
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161031
[St] Status:MEDLINE


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[PMID]:27685008
[Au] Autor:Morville T; Rosenkilde M; Munch-Andersen T; Andersen PR; Kjær Groenbæk K; Helbo S; Kristensen M; Vigelsø Hansen A; Mattsson N; Rasmusen HK; Guadalupe-Grau A; Fago A; Neigaard Hansen C; Twelkmeyer B; Løvind Andersen J; Dela F; Wulff Helge J
[Ad] Endereço:1Xlab, Center for Healthy Aging, Department of Biomedical Sciences, University of Copenhagen, Copenhagen, DENMARK; 2Department of Bioscience, Zoophysiology, Aarhus University, Aarhus, DENMARK; 3Department of Cardiology, University Hospital of Bispebjerg, Copenhagen, DENMARK; 4Department of Clinical Science, Intervention and Technology, Karolinska Institutet, Stockholm, SWEDEN; 5Department of Anaesthesia and Intensive Care, Karolinska University Hospital, Huddinge, Stockholm, SWEDEN; and 6Institute of Sports Medicine Copenhagen, Bispebjerg Hospital, Copenhagen, DENMARK.
[Ti] Título:Repeated Prolonged Exercise Decreases Maximal Fat Oxidation in Older Men.
[So] Source:Med Sci Sports Exerc;49(2):308-316, 2017 Feb.
[Is] ISSN:1530-0315
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:INTRODUCTION/PURPOSE: Fat metabolism and muscle adaptation was investigated in six older trained men (age, 61 ± 4 yr; VË™O2max, 48 ± 2 mL·kg·min) after repeated prolonged exercise). METHODS: A distance of 2706 km (1681 miles) cycling was performed over 14 d, and a blood sample and a muscle biopsy were obtained at rest after an overnight fast before and 30 h after the completion of the cycling. VË™O2max and maximal fat oxidation were measured using incremental exercise tests. HR was continuously sampled during cycling to estimate exercise intensity. RESULTS: The daily duration of exercise was 10 h and 31 ± 37 min, and the mean intensity was 53% ± 1% of VË™O2max. Body weight remained unchanged. VË™O2max and maximal fat oxidation rate decreased by 6% ± 2% (P = 0.04) and 32% ± 8% (P < 0.01), respectively. The exercise intensity that elicits maximal fat oxidation was not significantly decreased. Plasma free fatty acid (FA) concentration decreased (P < 0.002) from 500 ± 77 µmol·L to 160 ± 38 µmol·L. Plasma glucose concentration as well as muscle glycogen, myoglobin, and triacylglycerol content remained unchanged. Muscle citrate synthase and ß-hydroxy-acyl-CoA-dehydrogenase activities were unchanged, but the protein expression of HKII, GLUT4, and adipose triacylglycerol lipase were significantly increased. CONCLUSIONS: Overall, the decreased maximal fat oxidation was probably due to lower exogenous plasma fatty acid availability and the muscle adaptation pattern indicates an increased glucose transport capacity and an increased muscle lipolysis capacity supporting an increased contribution of exogenous glucose and endogenous fat during exercise.
[Mh] Termos MeSH primário: Exercício/fisiologia
Metabolismo dos Lipídeos
Músculo Esquelético/metabolismo
Resistência Física/fisiologia
[Mh] Termos MeSH secundário: 3-Hidroxiacil-CoA Desidrogenases/metabolismo
Glicemia/metabolismo
Citrato (si)-Sintase/metabolismo
Ácidos Graxos não Esterificados/sangue
Transportador de Glucose Tipo 4/metabolismo
Glicogênio/metabolismo
Hexoquinase/metabolismo
Seres Humanos
Insulina/sangue
Ácido Láctico/sangue
Lipase/metabolismo
Masculino
Meia-Idade
Mioglobina/metabolismo
Oxirredução
Triglicerídeos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Blood Glucose); 0 (Fatty Acids, Nonesterified); 0 (Glucose Transporter Type 4); 0 (Insulin); 0 (Myoglobin); 0 (Triglycerides); 33X04XA5AT (Lactic Acid); 9005-79-2 (Glycogen); EC 1.1.1.- (3-Hydroxyacyl CoA Dehydrogenases); EC 2.3.3.1 (Citrate (si)-Synthase); EC 2.7.1.1 (Hexokinase); EC 3.1.1.3 (Lipase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171010
[Lr] Data última revisão:
171010
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160930
[St] Status:MEDLINE
[do] DOI:10.1249/MSS.0000000000001107


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[PMID]:27639177
[Au] Autor:Kivelä TT
[Ad] Endereço:Paediatric Ophthalmology Service, Department of Ophthalmology, University of Helsinki and Helsinki University Hospital, Helsinki, Finland.
[Ti] Título:Early dietary therapy for long-chain 3-hydroxyacyl-CoA dehydrogenase deficiency can maintain vision despite subnormal retinal function.
[So] Source:Acta Paediatr;105(12):1461, 2016 12.
[Is] ISSN:1651-2227
[Cp] País de publicação:Norway
[La] Idioma:eng
[Mh] Termos MeSH primário: 3-Hidroxiacil-CoA Desidrogenases/deficiência
Erros Inatos do Metabolismo Lipídico/dietoterapia
[Mh] Termos MeSH secundário: Cardiomiopatias
Seres Humanos
Miopatias Mitocondriais
Doenças do Sistema Nervoso
[Pt] Tipo de publicação:JOURNAL ARTICLE; COMMENT
[Nm] Nome de substância:
EC 1.1.1.- (3-Hydroxyacyl CoA Dehydrogenases)
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170817
[Lr] Data última revisão:
170817
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160918
[St] Status:MEDLINE
[do] DOI:10.1111/apa.13595



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