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Pesquisa : D08.811.913.050.080 [Categoria DeCS]
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[PMID]:29311546
[Au] Autor:Yang JE; Park SJ; Kim WJ; Kim HJ; Kim BJ; Lee H; Shin J; Lee SY
[Ad] Endereço:Metabolic and Biomolecular Engineering National Research Laboratory, Department of Chemical and Biomolecular Engineering (BK21 Plus Program), Center for Systems and Synthetic Biotechnology, Institute for the BioCentury, Korea Advanced Institute of Science and Technology (KAIST), Daejeon, 34141, Repu
[Ti] Título:One-step fermentative production of aromatic polyesters from glucose by metabolically engineered Escherichia coli strains.
[So] Source:Nat Commun;9(1):79, 2018 01 08.
[Is] ISSN:2041-1723
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Aromatic polyesters are widely used plastics currently produced from petroleum. Here we engineer Escherichia coli strains for the production of aromatic polyesters from glucose by one-step fermentation. When the Clostridium difficile isocaprenoyl-CoA:2-hydroxyisocaproate CoA-transferase (HadA) and evolved polyhydroxyalkanoate (PHA) synthase genes are overexpressed in a D-phenyllactate-producing strain, poly(52.3 mol% 3-hydroxybutyrate (3HB)-co-47.7 mol% D-phenyllactate) can be produced from glucose and sodium 3HB. Also, various poly(3HB-co-D-phenyllactate) polymers having 11.0, 15.8, 20.0, 70.8, and 84.5 mol% of D-phenyllactate are produced from glucose as a sole carbon source by additional expression of Ralstonia eutropha ß-ketothiolase (phaA) and reductase (phaB) genes. Fed-batch culture of this engineered strain produces 13.9 g l of poly(61.9 mol% 3HB-co-38.1 mol% D-phenyllactate). Furthermore, different aromatic polyesters containing D-mandelate and D-3-hydroxy-3-phenylpropionate are produced from glucose when feeding the corresponding monomers. The engineered bacterial system will be useful for one-step fermentative production of aromatic polyesters from renewable resources.
[Mh] Termos MeSH primário: Escherichia coli/metabolismo
Fermentação
Glucose/metabolismo
Engenharia Metabólica/métodos
Poliésteres/metabolismo
[Mh] Termos MeSH secundário: Ácido 3-Hidroxibutírico/metabolismo
Acetil-CoA C-Aciltransferase/genética
Acetil-CoA C-Aciltransferase/metabolismo
Aciltransferases/genética
Aciltransferases/metabolismo
Proteínas de Bactérias/genética
Proteínas de Bactérias/metabolismo
Clostridium difficile/enzimologia
Clostridium difficile/genética
Coenzima A-Transferases/genética
Coenzima A-Transferases/metabolismo
Cupriavidus necator/enzimologia
Cupriavidus necator/genética
Escherichia coli/genética
Lactatos/metabolismo
Oxirredutases/genética
Oxirredutases/metabolismo
Polietilenotereftalatos/metabolismo
Polímeros/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Lactates); 0 (Polyesters); 0 (Polyethylene Terephthalates); 0 (Polymers); 156-05-8 (3-phenyllactic acid); EC 1.- (Oxidoreductases); EC 2.3.- (Acyltransferases); EC 2.3.1.- (poly(3-hydroxyalkanoic acid) synthase); EC 2.3.1.16 (Acetyl-CoA C-Acyltransferase); EC 2.8.3.- (Coenzyme A-Transferases); IY9XDZ35W2 (Glucose); TZP1275679 (3-Hydroxybutyric Acid)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180305
[Lr] Data última revisão:
180305
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180110
[St] Status:MEDLINE
[do] DOI:10.1038/s41467-017-02498-w


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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]:28369071
[Au] Autor:Martines AMF; van Eunen K; Reijngoud DJ; Bakker BM
[Ad] Endereço:Laboratory of Pediatrics, University of Groningen, University Medical Center Groningen, The Netherlands.
[Ti] Título:The promiscuous enzyme medium-chain 3-keto-acyl-CoA thiolase triggers a vicious cycle in fatty-acid beta-oxidation.
[So] Source:PLoS Comput Biol;13(4):e1005461, 2017 Apr.
[Is] ISSN:1553-7358
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondrial fatty-acid beta-oxidation (mFAO) plays a central role in mammalian energy metabolism. Multiple severe diseases are associated with defects in this pathway. Its kinetic structure is characterized by a complex wiring of which the functional implications have hardly been explored. Repetitive cycles of reversible reactions, each cycle shortening the fatty acid by two carbon atoms, evoke competition between intermediates of different chain lengths for a common set of 'promiscuous' enzymes (enzymes with activity towards multiple substrates). In our validated kinetic model of the pathway, substrate overload causes a steep and detrimental flux decline. Here, we unravel the underlying mechanism and the role of enzyme promiscuity in it. Comparison of alternative model versions elucidated the role of promiscuity of individual enzymes. Promiscuity of the last enzyme of the pathway, medium-chain ketoacyl-CoA thiolase (MCKAT), was both necessary and sufficient to elicit the flux decline. Subsequently, Metabolic Control Analysis revealed that MCKAT had insufficient capacity to cope with high substrate influx. Next, we quantified the internal metabolic regulation, revealing a vicious cycle around MCKAT. Upon substrate overload, MCKAT's ketoacyl-CoA substrates started to accumulate. The unfavourable equilibrium constant of the preceding enzyme, medium/short-chain hydroxyacyl-CoA dehydrogenase, worked as an amplifier, leading to accumulation of upstream CoA esters, including acyl-CoA esters. These acyl-CoA esters are at the same time products of MCKAT and inhibited its already low activity further. Finally, the accumulation of CoA esters led to a sequestration of free CoA. CoA being a cofactor for MCKAT, its sequestration limited the MCKAT activity even further, thus completing the vicious cycle. Since CoA is also a substrate for distant enzymes, it efficiently communicated the 'traffic jam' at MCKAT to the entire pathway. This novel mechanism provides a basis to explore the role of mFAO in disease and elucidate similar principles in other pathways of lipid metabolism.
[Mh] Termos MeSH primário: Acetil-CoA C-Aciltransferase/metabolismo
Ácidos Graxos/metabolismo
Redes e Vias Metabólicas/fisiologia
[Mh] Termos MeSH secundário: Acetil-CoA C-Aciltransferase/fisiologia
Biologia Computacional
Simulação por Computador
Cinética
Oxirredução
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acids); EC 2.3.1.16 (Acetyl-CoA C-Acyltransferase)
[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:170404
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pcbi.1005461


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[PMID]:28255778
[Au] Autor:Paquay S; Bourillon A; Pichard S; Benoist JF; de Lonlay P; Dobbelaere D; Fouilhoux A; Guffon N; Rouvet I; Labarthe F; Mention K; Touati G; Valayannopoulos V; Ogier de Baulny H; Elmaleh-Bergès M; Acquaviva-Bourdain C; Vianey-Saban C; Schiff M
[Ad] Endereço:Reference Center for Inborn Errors of Metabolism, Robert Debré University Hospital, 48 Bd Sérurier, Paris, F-75935 Cedex 19, France.
[Ti] Título:Mitochondrial acetoacetyl-CoA thiolase deficiency: basal ganglia impairment may occur independently of ketoacidosis.
[So] Source:J Inherit Metab Dis;40(3):415-422, 2017 May.
[Is] ISSN:1573-2665
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Mitochondrial acetoacetyl-CoA thiolase (T2) deficiency affects ketone body and isoleucine catabolism. Neurological impairment may occur secondary to ketoacidotic episodes. However, we observed neuromotor abnormalities without ketoacidotic events in two T2-deficient families. We hypothesized that the neurological signs were related to the genetic defect and may occur independently of ketoacidotic episodes. We therefore conducted a retrospective review on a French T2-deficient patient series searching for neuromotor impairment. METHODS: In total, 26 cases were retrospectively analysed for clinical, biological and neuroimaging data. RESULTS: Neurological findings were observed for 6/26 (23%) patients. Among these, two had never experienced ketoacidotic episodes, though they developed extrapyramidal signs with putamen involvement. Two of the other four patients developed neurological abnormalities before the first ketoacidotic crisis, with putamen involvement in one case. The third patient developed extrapyramidal symptoms more than 10 years after the initial decompensation with globus pallidus involvement. The last patient developed extrapyramidal signs immediately after a severe ketoacidotic crisis with putaminal lesions. CONCLUSIONS: Most T2-deficient patients achieved normal neurodevelopment. However, on account of the role of T2 in isoleucine catabolism, these patients are potentially exposed to accumulation of toxic isoleucine-derived metabolites, which may contribute to neurological impairment. Our findings confirm previous observations that neurological symptoms in T2 deficiency may occur unrelated to ketoacidosis. The role of protein restriction as a preventive measure against neurological symptoms could not be established in this study and deserves further evaluation. Long-term follow-up data on children diagnosed by newborn screening may clarify the pathogenesis of this neurometabolic association.
[Mh] Termos MeSH primário: Acetil-CoA C-Acetiltransferase/deficiência
Acetil-CoA C-Aciltransferase/deficiência
Erros Inatos do Metabolismo dos Aminoácidos/metabolismo
Gânglios da Base/metabolismo
Cetose/metabolismo
Mitocôndrias/metabolismo
[Mh] Termos MeSH secundário: Acetil-CoA C-Aciltransferase/metabolismo
Adolescente
Adulto
Criança
Pré-Escolar
Feminino
Seres Humanos
Lactente
Recém-Nascido
Isoleucina/metabolismo
Corpos Cetônicos/metabolismo
Masculino
Triagem Neonatal/métodos
Estudos Retrospectivos
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ketone Bodies); 04Y7590D77 (Isoleucine); EC 2.3.1.16 (Acetyl-CoA C-Acyltransferase); EC 2.3.1.9 (Acetyl-CoA C-Acetyltransferase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170304
[St] Status:MEDLINE
[do] DOI:10.1007/s10545-017-0021-y


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[PMID]:28237113
[Au] Autor:Wang W; Subramani S
[Ad] Endereço:Section of Molecular Biology, Division of Biological Sciences, University of California, San Diego, CA, United States.
[Ti] Título:Assays to Monitor Pexophagy in Yeast.
[So] Source:Methods Enzymol;588:413-427, 2017.
[Is] ISSN:1557-7988
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Pexophagy is a selective autophagy process that degrades damaged and/or superfluous peroxisomes in the yeast vacuole or in mammalian lysosomes. The molecular mechanisms of pexophagy are well studied in yeast. Peroxisomes can be rapidly induced by oleate in the budding yeast, Saccharomyces cerevisiae, and by oleate or methanol in the methylotrophic yeast, Pichia pastoris. A number of peroxisomal matrix enzymes, such as 3-ketoacyl CoA thiolase (thiolase) and alcohol oxidase (AOX), are upregulated correspondingly to meet metabolic demands of the cells. Removal of these peroxisome-inducing carbon sources creates conditions wherein peroxisomes are superfluous and results in pexophagy and the degradation of these peroxisomal matrix enzymes. In this chapter, we discuss different assays to monitor pexophagy in yeast. These assays rely on tracking the localization of the BFP-SKL protein (a peroxisomally targeted version of the blue fluorescent protein) by microscopy, biochemical analysis of the degradation of peroxisomal matrix proteins, thiolase and AOX, and/or measuring the reduction of AOX activity during pexophagy.
[Mh] Termos MeSH primário: Acetil-CoA C-Aciltransferase/metabolismo
Oxirredutases do Álcool/metabolismo
Proteínas Fúngicas/metabolismo
Peroxissomos/metabolismo
Pichia/citologia
Saccharomyces cerevisiae/citologia
[Mh] Termos MeSH secundário: Autofagia
Ensaios Enzimáticos/métodos
Microscopia de Fluorescência/métodos
Peroxissomos/enzimologia
Peroxissomos/ultraestrutura
Pichia/enzimologia
Pichia/metabolismo
Proteólise
Saccharomyces cerevisiae/enzimologia
Saccharomyces cerevisiae/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fungal Proteins); EC 1.1.- (Alcohol Oxidoreductases); EC 1.1.3.13 (alcohol oxidase); EC 2.3.1.16 (Acetyl-CoA C-Acyltransferase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170815
[Lr] Data última revisão:
170815
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170227
[St] Status:MEDLINE


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[PMID]:28220263
[Au] Autor:Nguyen KN; Abdelkreem E; Colombo R; Hasegawa Y; Can NT; Bui TP; Le HT; Tran MT; Nguyen HT; Trinh HT; Aoyama Y; Sasai H; Yamaguchi S; Fukao T; Vu DC
[Ad] Endereço:National Children's Hospital, La Thanh Road, Dong Da District, Hanoi, Vietnam.
[Ti] Título:Characterization and outcome of 41 patients with beta-ketothiolase deficiency: 10 years' experience of a medical center in northern Vietnam.
[So] Source:J Inherit Metab Dis;40(3):395-401, 2017 May.
[Is] ISSN:1573-2665
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Beta-ketothiolase (T2) deficiency is an inherited disease of isoleucine and ketone body metabolism caused by mutations in the ACAT1 gene. Between 2005 and 2016, a total of 41 patients with T2 deficiency were identified at a medical center in northern Vietnam, with an estimated incidence of one in 190,000 newborns. Most patients manifested ketoacidotic episodes of varying severity between 6 and 18 months of age. Remarkably, 28% of patients showed high blood glucose levels (up to 23.3 mmol/L). Ketoacidotic episodes recurred in 43% of patients. The age of onset, frequency of episodes, and identified genotype did not affect patient outcomes that were generally favorable, with the exception of seven cases (five died and two had neurological sequelae). Custom-tailored acute and follow-up management was critical for a positive clinical outcome. Two null mutations, c.622C>T (p.Arg208*) and c.1006-1G>C (p.Val336fs), accounted for 66% and 19% of all identified ACAT1 mutant alleles, respectively. Most patients showed characteristic biochemical abnormalities. A newborn screening program could be expected to have a high yield in Vietnam. Investigation findings of haplotypes linked to the most common ACAT1 mutation (c.622C>T) are consistent with an ancient common founder of mutation-bearing chromosomes belonging to the Kinh ethnic population. The direct management and long-term follow-up of a large number of T2-deficient patients enabled us to study the natural history of this rare disease.
[Mh] Termos MeSH primário: Acetil-CoA C-Aciltransferase/deficiência
Erros Inatos do Metabolismo dos Aminoácidos/genética
[Mh] Termos MeSH secundário: Acetil-CoA C-Aciltransferase/genética
Alelos
Feminino
Haplótipos/genética
Seres Humanos
Recém-Nascido
Masculino
Mutação/genética
Triagem Neonatal/métodos
Vietnã
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.3.1.16 (Acetyl-CoA C-Acyltransferase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171018
[Lr] Data última revisão:
171018
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170222
[St] Status:MEDLINE
[do] DOI:10.1007/s10545-017-0026-6


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[PMID]:27933454
[Au] Autor:Kallscheuer N; Gätgens J; Lübcke M; Pietruszka J; Bott M; Polen T
[Ad] Endereço:IBG-1: Biotechnology, Institute of Bio- and Geosciences, Forschungszentrum Jülich GmbH, 52425, Jülich, Germany. n.kallscheuer@fz-juelich.de.
[Ti] Título:Improved production of adipate with Escherichia coli by reversal of ß-oxidation.
[So] Source:Appl Microbiol Biotechnol;101(6):2371-2382, 2017 Mar.
[Is] ISSN:1432-0614
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:The linear C dicarboxylic acid adipic acid is an important bulk chemical in the petrochemical industry as precursor of the polymer nylon-6,6-polyamide. In recent years, efforts were made towards the biotechnological production of adipate from renewable carbon sources using microbial cells. One strategy is to produce adipate via a reversed ß-oxidation pathway. Hitherto, the adipate titers were very low due to limiting enzyme activities for this pathway. In most cases, the CoA intermediates are non-natural substrates for the tested enzymes and were therefore barely converted. We here tested heterologous enzymes in Escherichia coli to overcome these limitations and to improve the production of adipate via a reverse ß-oxidation pathway. We tested in vitro selected enzymes for the efficient reduction of the enoyl-CoA and in the final reaction for the thioester cleavage. The genes encoding the enzymes which showed in vitro the highest activity were then used to construct an expression plasmid for a synthetic adipate pathway. Expression of paaJ, paaH, paaF, dcaA, and tesB in E. coli BL21(DE3) resulted in the production of up to 36 mg/L of adipate after 30 h of cultivation. Beside the activities of the pathway enzymes, the availability of metabolic precursors may limit the synthesis of adipate, providing another key target for further strain engineering towards high-yield production of adipate with E. coli.
[Mh] Termos MeSH primário: Acetil-CoA C-Aciltransferase/metabolismo
Adipatos/metabolismo
Enoil-CoA Hidratase/metabolismo
Proteínas de Escherichia coli/metabolismo
Escherichia coli/metabolismo
Regulação Bacteriana da Expressão Gênica
Oxirredutases/metabolismo
[Mh] Termos MeSH secundário: Acetil-CoA C-Aciltransferase/genética
Enoil-CoA Hidratase/genética
Escherichia coli/genética
Proteínas de Escherichia coli/genética
Engenharia Metabólica
Redes e Vias Metabólicas/genética
Oxirredução
Oxirredutases/genética
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adipates); 0 (Escherichia coli Proteins); 0 (Recombinant Proteins); 76A0JE0FKJ (adipic acid); EC 1.- (Oxidoreductases); EC 2.3.1.16 (Acetyl-CoA C-Acyltransferase); EC 2.3.1.174 (3-oxoadipyl-coenzyme A thiolase); EC 4.2.1.17 (Enoyl-CoA Hydratase); EC 4.2.1.17 (PaaF protein, E coli)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170307
[Lr] Data última revisão:
170307
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161210
[St] Status:MEDLINE
[do] DOI:10.1007/s00253-016-8033-3


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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


  9 / 563 MEDLINE  
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[PMID]:27871246
[Au] Autor:Werner N; Gómez M; Baeza M; Cifuentes V; Alcaíno J
[Ad] Endereço:Departamento de Ciencias Ecológicas y Centro de Biotecnología, Facultad de Ciencias, Universidad de Chile, Las Palmeras 3425, Casilla 653, Ñuñoa, Santiago, Chile.
[Ti] Título:Functional characterization of thiolase-encoding genes from Xanthophyllomyces dendrorhous and their effects on carotenoid synthesis.
[So] Source:BMC Microbiol;16(1):278, 2016 Nov 21.
[Is] ISSN:1471-2180
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The basidiomycetous yeast Xanthophyllomyces dendrorhous has been described as a potential biofactory for terpenoid-derived compounds due to its ability to synthesize astaxanthin. Functional knowledge of the genes involved in terpenoid synthesis would create opportunities to enhance carotenoid production. A thiolase enzyme catalyzes the first step in terpenoid synthesis. RESULTS: Two potential thiolase-encoding genes were found in the yeast genome; bioinformatically, one was identified as an acetyl-CoA C-acetyltransferase (ERG10), and the other was identified as a 3-ketoacyl Co-A thiolase (POT1). Heterologous complementation assays in Saccharomyces cerevisiae showed that the ERG10 gene from X. dendrorhous could complement the lack of the endogenous ERG10 gene in S. cerevisiae, thereby allowing cellular growth and sterol synthesis. X. dendrorhous heterozygous mutants for each gene were created, and a homozygous POT1 mutant was also obtained. This mutant exhibited changes in pigment composition and higher ERG10 transcript levels than the wild type strain. CONCLUSIONS: The results support the notion that the ERG10 gene in X. dendrorhous is a functional acetyl-CoA C-acetyltransferase essential for the synthesis of mevalonate in yeast. The POT1 gene would encode a functional 3-ketoacyl Co-A thiolase that is non-essential for cell growth, but its mutation indirectly affects pigment production.
[Mh] Termos MeSH primário: Acetil-CoA C-Aciltransferase/genética
Basidiomycota/enzimologia
Basidiomycota/genética
Carotenoides/biossíntese
[Mh] Termos MeSH secundário: Acetil-CoA C-Acetiltransferase/genética
Acetil-CoA C-Acetiltransferase/metabolismo
Acetil-CoA C-Aciltransferase/metabolismo
Sequência de Bases
Basidiomycota/metabolismo
Vias Biossintéticas
DNA Fúngico/genética
Genes Fúngicos
Engenharia Metabólica/métodos
Mutação
Reação em Cadeia da Polimerase
Saccharomyces cerevisiae/genética
Saccharomyces cerevisiae/metabolismo
Esteróis/biossíntese
Terpenos/metabolismo
Xantofilas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Fungal); 0 (Sterols); 0 (Terpenes); 0 (Xanthophylls); 36-88-4 (Carotenoids); 8XPW32PR7I (astaxanthine); EC 2.3.1.16 (Acetyl-CoA C-Acyltransferase); EC 2.3.1.9 (Acetyl-CoA C-Acetyltransferase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170608
[Lr] Data última revisão:
170608
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161123
[St] Status:MEDLINE


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[PMID]:27813339
[Au] Autor:Heggermont WA; Papageorgiou AP; Heymans S; van Bilsen M
[Ad] Endereço:Centre for Molecular and Vascular Biology, Department of Cardiovascular Research, University of Leuven, Belgium.
[Ti] Título:Metabolic support for the heart: complementary therapy for heart failure?
[So] Source:Eur J Heart Fail;18(12):1420-1429, 2016 Dec.
[Is] ISSN:1879-0844
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The failing heart has an increased metabolic demand and at the same time suffers from impaired energy efficiency, which is a detrimental combination. Therefore, therapies targeting the energy-deprived failing heart and rewiring cardiac metabolism are of great potential, but are lacking in daily clinical practice. Metabolic impairment in heart failure patients has been well characterized for patients with reduced ejection fraction, and is coming of age in patients with 'preserved' ejection fraction. Targeting cardiomyocyte metabolism in heart failure could complement current heart failure treatments that do improve cardiovascular haemodynamics, but not the energetic status of the heart. In this review, we discuss the hallmarks of normal cardiac metabolism, typical metabolic disturbances in heart failure, and past and present therapeutic targets that impact on cardiac metabolism.
[Mh] Termos MeSH primário: Insuficiência Cardíaca/metabolismo
Miocárdio/metabolismo
Miócitos Cardíacos/metabolismo
[Mh] Termos MeSH secundário: Acetil-CoA C-Aciltransferase/antagonistas & inibidores
Fármacos Cardiovasculares/uso terapêutico
Carnitina/análogos & derivados
Carnitina/uso terapêutico
Carnitina O-Palmitoiltransferase/antagonistas & inibidores
Ácido Dicloroacético/uso terapêutico
Metabolismo Energético
Inibidores Enzimáticos/uso terapêutico
Compostos de Epóxi/uso terapêutico
Ácidos Graxos/metabolismo
Glucose/metabolismo
Insuficiência Cardíaca/tratamento farmacológico
Insuficiência Cardíaca/fisiopatologia
Seres Humanos
Oxirredução
Perexilina/uso terapêutico
Ranolazina/uso terapêutico
Volume Sistólico
Trimetazidina/uso terapêutico
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Cardiovascular Agents); 0 (Enzyme Inhibitors); 0 (Epoxy Compounds); 0 (Fatty Acids); 17298-37-2 (propionylcarnitine); 9LSH52S3LQ (Dichloroacetic Acid); A6IEZ5M406 (Ranolazine); EC 2.3.1.16 (Acetyl-CoA C-Acyltransferase); EC 2.3.1.21 (Carnitine O-Palmitoyltransferase); IY9XDZ35W2 (Glucose); KU65374X44 (Perhexiline); MSB3DD2XP6 (etomoxir); N9A0A0R9S8 (Trimetazidine); S7UI8SM58A (Carnitine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171031
[Lr] Data última revisão:
171031
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161105
[St] Status:MEDLINE
[do] DOI:10.1002/ejhf.678



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