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Pesquisa : D08.811.913.050.134.150 [Categoria DeCS]
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[PMID]:26819073
[Au] Autor:Madeira MS; Rolo ES; Alfaia CM; Pires VR; Luxton R; Doran O; Bessa RJ; Prates JA
[Ti] Título:Influence of betaine and arginine supplementation of reduced protein diets on fatty acid composition and gene expression in the muscle and subcutaneous adipose tissue of cross-bred pigs.
[So] Source:Br J Nutr;115(6):937-50, 2016 Mar 28.
[Is] ISSN:1475-2662
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The isolated or combined effects of betaine and arginine supplementation of reduced protein diets (RPD) on fat content, fatty acid composition and mRNA levels of genes controlling lipid metabolism in pig m. longissimus lumborum and subcutaneous adipose tissue (SAT) were assessed. The experiment was performed on forty intact male pigs (Duroc×Large White×Landrace cross-breed) with initial and final live weights of 60 and 93 kg, respectively. Pigs were randomly assigned to one of the following five diets (n 8): 16·0 % of crude protein (control), 13·0 % of crude protein (RPD), RPD supplemented with 0·33 % of betaine, RPD supplemented with 1·5 % of arginine and RPD supplemented with 0·33 % of betaine and 1·5 % of arginine. Data confirmed that RPD increase intramuscular fat (IMF) content and total fat content in SAT. The increased total fat content in SAT was accompanied by higher GLUT type 4, lipoprotein lipase and stearoyl-CoA desaturase mRNA expression levels. In addition, the supplementation of RPD with betaine and/or arginine did not affect either IMF or total fat in SAT. However, dietary betaine supplementation slightly affected fatty acid composition in both muscle and SAT. This effect was associated with an increase of carnitine O-acetyltransferase mRNA levels in SAT but not in muscle, which suggests that betaine might be involved in the differential regulation of some key genes of lipid metabolism in pig muscle and SAT. Although the arginine-supplemented diet decreased the mRNA expression level of PPARG in muscle and SAT, it did not influence fat content or fatty acid composition in any of these pig tissues.
[Mh] Termos MeSH primário: Arginina/administração & dosagem
Betaína/administração & dosagem
Dieta com Restrição de Proteínas/veterinária
Regulação da Expressão Gênica no Desenvolvimento
Metabolismo dos Lipídeos
Músculo Liso/metabolismo
Gordura Subcutânea Abdominal/metabolismo
[Mh] Termos MeSH secundário: Adiposidade
Animais
Carnitina O-Acetiltransferase/genética
Carnitina O-Acetiltransferase/metabolismo
Cruzamentos Genéticos
Dieta com Restrição de Proteínas/efeitos adversos
Ácidos Graxos/análise
Ácidos Graxos/metabolismo
Qualidade dos Alimentos
Transportador de Glucose Tipo 4/genética
Transportador de Glucose Tipo 4/metabolismo
Lipase Lipoproteica/genética
Lipase Lipoproteica/metabolismo
Masculino
Carne/análise
Músculo Liso/enzimologia
Músculo Liso/crescimento & desenvolvimento
Especificidade de Órgãos
Portugal
RNA Mensageiro/metabolismo
Estearoil-CoA Dessaturase/genética
Estearoil-CoA Dessaturase/metabolismo
Gordura Subcutânea Abdominal/enzimologia
Gordura Subcutânea Abdominal/crescimento & desenvolvimento
Sus scrofa
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE; RANDOMIZED CONTROLLED TRIAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fatty Acids); 0 (Glucose Transporter Type 4); 0 (RNA, Messenger); 3SCV180C9W (Betaine); 94ZLA3W45F (Arginine); EC 1.14.19.1 (Stearoyl-CoA Desaturase); EC 2.3.1.7 (Carnitine O-Acetyltransferase); EC 3.1.1.34 (Lipoprotein Lipase)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:160623
[Lr] Data última revisão:
160623
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160129
[St] Status:MEDLINE


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[PMID]:26748706
[Au] Autor:Davies MN; Kjalarsdottir L; Thompson JW; Dubois LG; Stevens RD; Ilkayeva OR; Brosnan MJ; Rolph TP; Grimsrud PA; Muoio DM
[Ad] Endereço:Sarah W. Stedman Nutrition and Metabolism Center, Duke Molecular Physiology Institute, Duke University, Durham, NC 27701, USA.
[Ti] Título:The Acetyl Group Buffering Action of Carnitine Acetyltransferase Offsets Macronutrient-Induced Lysine Acetylation of Mitochondrial Proteins.
[So] Source:Cell Rep;14(2):243-54, 2016 Jan 12.
[Is] ISSN:2211-1247
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lysine acetylation (AcK), a posttranslational modification wherein a two-carbon acetyl group binds covalently to a lysine residue, occurs prominently on mitochondrial proteins and has been linked to metabolic dysfunction. An emergent theory suggests mitochondrial AcK occurs via mass action rather than targeted catalysis. To test this hypothesis, we performed mass spectrometry-based acetylproteomic analyses of quadriceps muscles from mice with skeletal muscle-specific deficiency of carnitine acetyltransferase (CrAT), an enzyme that buffers the mitochondrial acetyl-CoA pool by converting short-chain acyl-CoAs to their membrane permeant acylcarnitine counterparts. CrAT deficiency increased tissue acetyl-CoA levels and susceptibility to diet-induced AcK of broad-ranging mitochondrial proteins, coincident with diminished whole body glucose control. Sub-compartment acetylproteome analyses of muscles from obese mice and humans showed remarkable overrepresentation of mitochondrial matrix proteins. These findings reveal roles for CrAT and L-carnitine in modulating the muscle acetylproteome and provide strong experimental evidence favoring the nonenzymatic carbon pressure model of mitochondrial AcK.
[Mh] Termos MeSH primário: Carnitina O-Acetiltransferase/metabolismo
Lisina/metabolismo
Proteínas Mitocondriais/metabolismo
[Mh] Termos MeSH secundário: Acetilação
Animais
Seres Humanos
Camundongos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Mitochondrial Proteins); EC 2.3.1.7 (Carnitine O-Acetyltransferase); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1611
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160111
[St] Status:MEDLINE


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[PMID]:26154055
[Au] Autor:Seiler SE; Koves TR; Gooding JR; Wong KE; Stevens RD; Ilkayeva OR; Wittmann AH; DeBalsi KL; Davies MN; Lindeboom L; Schrauwen P; Schrauwen-Hinderling VB; Muoio DM
[Ad] Endereço:Department of Pharmacology and Cancer Biology, Duke University, Durham, NC 27704, USA.
[Ti] Título:Carnitine Acetyltransferase Mitigates Metabolic Inertia and Muscle Fatigue during Exercise.
[So] Source:Cell Metab;22(1):65-76, 2015 Jul 07.
[Is] ISSN:1932-7420
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acylcarnitine metabolites have gained attention as biomarkers of nutrient stress, but their physiological relevance and metabolic purpose remain poorly understood. Short-chain carnitine conjugates, including acetylcarnitine, derive from their corresponding acyl-CoA precursors via the action of carnitine acetyltransferase (CrAT), a bidirectional mitochondrial matrix enzyme. We show here that contractile activity reverses acetylcarnitine flux in muscle, from net production and efflux at rest to net uptake and consumption during exercise. Disruption of this switch in mice with muscle-specific CrAT deficiency resulted in acetyl-CoA deficit, perturbed energy charge, and diminished exercise tolerance, whereas acetylcarnitine supplementation produced opposite outcomes in a CrAT-dependent manner. Likewise, in exercise-trained compared to untrained humans, post-exercise phosphocreatine recovery rates were positively associated with CrAT activity and coincided with dramatic shifts in muscle acetylcarnitine dynamics. These findings show acetylcarnitine serves as a critical acetyl buffer for working muscles and provide insight into potential therapeutic strategies for combatting exercise intolerance.
[Mh] Termos MeSH primário: Acetilcoenzima A/metabolismo
Carnitina O-Acetiltransferase/metabolismo
Carnitina/análogos & derivados
Fadiga Muscular
Músculos/enzimologia
[Mh] Termos MeSH secundário: Animais
Carnitina/sangue
Carnitina/metabolismo
Exercício
Seres Humanos
Camundongos Endogâmicos C57BL
Músculos/metabolismo
Condicionamento Físico Animal
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (acylcarnitine); 72-89-9 (Acetyl Coenzyme A); EC 2.3.1.7 (Carnitine O-Acetyltransferase); S7UI8SM58A (Carnitine)
[Em] Mês de entrada:1604
[Cu] Atualização por classe:161019
[Lr] Data última revisão:
161019
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150709
[St] Status:MEDLINE


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[PMID]:25645937
[Au] Autor:Li Q; Deng S; Ibarra RA; Anderson VE; Brunengraber H; Zhang GF
[Ad] Endereço:From the Departments of Nutrition and.
[Ti] Título:Multiple mass isotopomer tracing of acetyl-CoA metabolism in Langendorff-perfused rat hearts: channeling of acetyl-CoA from pyruvate dehydrogenase to carnitine acetyltransferase.
[So] Source:J Biol Chem;290(13):8121-32, 2015 Mar 27.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We developed an isotopic technique to assess mitochondrial acetyl-CoA turnover (≈citric acid flux) in perfused rat hearts. Hearts are perfused with buffer containing tracer [(13)C2,(2)H3]acetate, which forms M5 + M4 + M3 acetyl-CoA. The buffer may also contain one or two labeled substrates, which generate M2 acetyl-CoA (e.g. [(13)C6]glucose or [1,2-(13)C2]palmitate) or/and M1 acetyl-CoA (e.g. [1-(13)C]octanoate). The total acetyl-CoA turnover and the contributions of fuels to acetyl-CoA are calculated from the uptake of the acetate tracer and the mass isotopomer distribution of acetyl-CoA. The method was applied to measurements of acetyl-CoA turnover under different conditions (glucose ± palmitate ± insulin ± dichloroacetate). The data revealed (i) substrate cycling between glycogen and glucose-6-P and between glucose-6-P and triose phosphates, (ii) the release of small excess acetyl groups as acetylcarnitine and ketone bodies, and (iii) the channeling of mitochondrial acetyl-CoA from pyruvate dehydrogenase to carnitine acetyltransferase. Because of this channeling, the labeling of acetylcarnitine and ketone bodies released by the heart are not proxies of the labeling of mitochondrial acetyl-CoA.
[Mh] Termos MeSH primário: Acetilcoenzima A/metabolismo
Carnitina O-Acetiltransferase/metabolismo
Miocárdio/enzimologia
Complexo Piruvato Desidrogenase/metabolismo
[Mh] Termos MeSH secundário: Animais
Isótopos de Carbono/metabolismo
Deutério/metabolismo
Glucose-6-Fosfato/metabolismo
Glicólise
Técnicas In Vitro
Corpos Cetônicos/metabolismo
Masculino
Ratos Sprague-Dawley
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Carbon Isotopes); 0 (Ketone Bodies); 0 (Pyruvate Dehydrogenase Complex); 56-73-5 (Glucose-6-Phosphate); 72-89-9 (Acetyl Coenzyme A); AR09D82C7G (Deuterium); EC 2.3.1.7 (Carnitine O-Acetyltransferase)
[Em] Mês de entrada:1506
[Cu] Atualização por classe:161202
[Lr] Data última revisão:
161202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150204
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M114.631549


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[PMID]:25110000
[Au] Autor:Abo Alrob O; Lopaschuk GD
[Ad] Endereço:*Mazankowski Alberta Heart Institute, University of Alberta, Edmonton, Alberta, Canada, T6G 2S2.
[Ti] Título:Role of CoA and acetyl-CoA in regulating cardiac fatty acid and glucose oxidation.
[So] Source:Biochem Soc Trans;42(4):1043-51, 2014 Aug.
[Is] ISSN:1470-8752
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:CoA (coenzyme A) and its derivatives have a critical role in regulating cardiac energy metabolism. This includes a key role as a substrate and product in the energy metabolic pathways, as well as serving as an allosteric regulator of cardiac energy metabolism. In addition, the CoA ester malonyl-CoA has an important role in regulating fatty acid oxidation, secondary to inhibiting CPT (carnitine palmitoyltransferase) 1, a key enzyme involved in mitochondrial fatty acid uptake. Alterations in malonyl-CoA synthesis by ACC (acetyl-CoA carboxylase) and degradation by MCD (malonyl-CoA decarboxylase) are important contributors to the high cardiac fatty acid oxidation rates seen in ischaemic heart disease, heart failure, obesity and diabetes. Additional control of fatty acid oxidation may also occur at the level of acetyl-CoA involvement in acetylation of mitochondrial fatty acid ß-oxidative enzymes. We find that acetylation of the fatty acid ß-oxidative enzymes, LCAD (long-chain acyl-CoA dehydrogenase) and ß-HAD (ß-hydroxyacyl-CoA dehydrogenase) is associated with an increase in activity and fatty acid oxidation in heart from obese mice with heart failure. This is associated with decreased SIRT3 (sirtuin 3) activity, an important mitochondrial deacetylase. In support of this, cardiac SIRT3 deletion increases acetylation of LCAD and ß-HAD, and increases cardiac fatty acid oxidation. Acetylation of MCD is also associated with increased activity, decreases malonyl-CoA levels and an increase in fatty acid oxidation. Combined, these data suggest that malonyl-CoA and acetyl-CoA have an important role in mediating the alterations in fatty acid oxidation seen in heart failure.
[Mh] Termos MeSH primário: Acetilcoenzima A/metabolismo
Coenzima A/metabolismo
Glucose/metabolismo
[Mh] Termos MeSH secundário: Animais
Carnitina O-Acetiltransferase/metabolismo
Ácidos Graxos/metabolismo
Seres Humanos
Lisina/metabolismo
Oxirredução
Sirtuína 3/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T; REVIEW
[Nm] Nome de substância:
0 (Fatty Acids); 72-89-9 (Acetyl Coenzyme A); EC 2.3.1.7 (Carnitine O-Acetyltransferase); EC 3.5.1.- (Sirtuin 3); IY9XDZ35W2 (Glucose); K3Z4F929H6 (Lysine); SAA04E81UX (Coenzyme A)
[Em] Mês de entrada:1505
[Cu] Atualização por classe:140811
[Lr] Data última revisão:
140811
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140812
[St] Status:MEDLINE
[do] DOI:10.1042/BST20140094


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[PMID]:24962334
[Au] Autor:Kienesberger K; Pordes AG; Völk TG; Hofbauer R
[Ti] Título:L-carnitine and PPARα-agonist fenofibrate are involved in the regulation of Carnitine Acetyltransferase (CrAT) mRNA levels in murine liver cells.
[So] Source:BMC Genomics;15:514, 2014 Jun 24.
[Is] ISSN:1471-2164
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The carnitine acetyltransferase (CrAT) is a mitochondrial matrix protein that directly influences intramitochondrial acetyl-CoA pools. Murine CrAT is encoded by a single gene located in the opposite orientation head to head to the PPP2R4 gene, sharing a very condensed bi-directional promoter. Since decreased CrAT expression is correlated with metabolic inflexibility and subsequent pathological consequences, our aim was to reveal and define possible activators of CrAT transcription in the normal embryonic murine liver cell line BNL CL. 2 and via which nuclear factors based on key metabolites mainly regulate hepatic expression of CrAT. Here we describe a functional characterization of the CrAT promoter region under conditions of L-carnitine deficiency and supplementation as well as fenofibrate induction in cell culture cells. RESULTS: The murine CrAT promoter displays some characteristics of a housekeeping gene: it lacks a TATA-box, is very GC-rich and harbors two Sp1 binding sites. Analysis of the promoter activity of CrAT by luciferase assays uncovered a L-carnitine sensitive region within -342 bp of the transcription start. Electrophoretic mobility shift and supershift assays proved the sequence element (-228/-222) to be an L-carnitine sensitive RXRα binding site, which also showed sensitivity to application of anti-PPARα and anti-PPARbp antibodies. In addition we analysed this specific RXRα/PPARα site by Southwestern Blotting technique and could pin down three protein factors binding to this promoter element. By qPCR we could quantify the nutrigenomic effect of L-carnitine itself and fenofibrate. CONCLUSIONS: Our results indicate a cooperative interplay of L-carnitine and PPARα in transcriptional regulation of murine CrAT, which is of nutrigenomical relevance. We created experimental proof that the muCrAT gene clearly is a PPARα target. Both L-carnitine and fenofibrate are inducers of CrAT transcripts, but the important hyperlipidemic drug fenofibrate being a more potent one, as a consequence of its pharmacological interaction.
[Mh] Termos MeSH primário: Carnitina O-Acetiltransferase/genética
Carnitina/antagonistas & inibidores
Fenofibrato/farmacologia
Regulação da Expressão Gênica/efeitos dos fármacos
Hepatócitos/efeitos dos fármacos
Hepatócitos/metabolismo
PPAR alfa/antagonistas & inibidores
[Mh] Termos MeSH secundário: Regiões 5' não Traduzidas
Animais
Sequência de Bases
Carnitina/metabolismo
Carnitina/farmacologia
Núcleo Celular/metabolismo
Regulação Enzimológica da Expressão Gênica/efeitos dos fármacos
Ordem dos Genes
Camundongos
Dados de Sequência Molecular
PPAR alfa/metabolismo
PPAR alfa/farmacologia
Regiões Promotoras Genéticas
Ligação Proteica
Transporte Proteico
RNA Mensageiro/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (5' Untranslated Regions); 0 (PPAR alpha); 0 (RNA, Messenger); EC 2.3.1.7 (Carnitine O-Acetyltransferase); S7UI8SM58A (Carnitine); U202363UOS (Fenofibrate)
[Em] Mês de entrada:1502
[Cu] Atualização por classe:170220
[Lr] Data última revisão:
170220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140626
[St] Status:MEDLINE
[do] DOI:10.1186/1471-2164-15-514


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[PMID]:24742295
[Au] Autor:Zhou J; Yeung YY
[Ad] Endereço:Department of Chemistry, National University of Singapore , 3 Science Drive 3, Singapore 117543.
[Ti] Título:Synthesis of reboxetine intermediate and carnitine acetyltransferase inhibitor via NBS-induced electrophilic multicomponent reaction.
[So] Source:J Org Chem;79(10):4644-9, 2014 May 16.
[Is] ISSN:1520-6904
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:N-Bromosuccinimide-induced electrophilic multicomponent reaction has been applied to the synthesis of Reboxetine intermediate, a highly potent selective norepinephrine reuptake inhibitor. By simply changing the olefinic partner, the synthesis of a carnitine acetyltransferase inhibitor, which contains a 2,6,6-trisubstituted morpholine system, can be accomplished.
[Mh] Termos MeSH primário: Inibidores da Captação Adrenérgica/química
Inibidores da Captação Adrenérgica/farmacologia
Bromosuccinimida/química
Carnitina O-Acetiltransferase/antagonistas & inibidores
Inibidores Enzimáticos/síntese química
Morfolinas/síntese química
Norepinefrina/química
Norepinefrina/farmacologia
[Mh] Termos MeSH secundário: Carnitina O-Acetiltransferase/química
Inibidores Enzimáticos/química
Morfolinas/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Adrenergic Uptake Inhibitors); 0 (Enzyme Inhibitors); 0 (Morpholines); 8B2ZCK305O (morpholine); 947S0YZ36I (reboxetine); EC 2.3.1.7 (Carnitine O-Acetyltransferase); K8G1F2UCJF (Bromosuccinimide); X4W3ENH1CV (Norepinephrine)
[Em] Mês de entrada:1501
[Cu] Atualização por classe:140516
[Lr] Data última revisão:
140516
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140419
[St] Status:MEDLINE
[do] DOI:10.1021/jo500609a


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[PMID]:24565505
[Au] Autor:Schulte A; Lichtenstern C; Henrich M; Weigand MA; Uhle F
[Ad] Endereço:Department of Anesthesiology and Intensive Care Medicine, Justus-Liebig-University Giessen, Giessen, Germany.
[Ti] Título:Loss of vagal tone aggravates systemic inflammation and cardiac impairment in endotoxemic rats.
[So] Source:J Surg Res;188(2):480-8, 2014 May 15.
[Is] ISSN:1095-8673
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: During the course of sepsis, often myocardial depression with hemodynamic impairment occurs. Acetylcholine, the main transmitter of the parasympathetic Nervus vagus, has been shown to be of importance for the transmission of signals within the immune system and also for a variety of other functions throughout the organism. Hypothesizing a potential correlation between this dysfunction and hemodynamic impairment, we wanted to assess the impact of vagal stimulation on myocardial inflammation and function in a rat model of lipopolysaccharide (LPS)-induced septic shock. As the myocardial tissue is (sparsely) innervated by the N. vagus, there might be an important anti-inflammatory effect in the heart, inhibiting proinflammatory gene expression in cardiomyocytes and improving cardiac function. MATERIALS AND METHODS: We performed stimulation of the right cervical branch of the N. vagus in vagotomized, endotoxemic (1 mg/kg body weight LPS, intravenously) rats. Hemodynamic parameters were assessed over time using a left ventricular pressure-volume catheter. After the experiments, hearts and blood plasma were collected, and the expression of proinflammatory cytokines was measured using quantitative reverse transcription polymerase chain reaction and enzyme-linked immunosorbent assay. RESULTS: After vagotomy, the inflammatory response was aggravated, measurable by elevated cytokine levels in plasma and ventricular tissue. In concordance, cardiac impairment during septic shock was pronounced in these animals. To reverse both hemodynamic and immunologic effects of diminished vagal tone, even a brief stimulation of the N. vagus was enough during initial LPS infusion. CONCLUSIONS: Overall, the N. vagus might play a major role in maintaining hemodynamic stability and cardiac immune homeostasis during septic shock.
[Mh] Termos MeSH primário: Regulação para Baixo/fisiologia
Endotoxemia/fisiopatologia
Miocárdio/patologia
Miócitos Cardíacos/patologia
Choque Séptico/fisiopatologia
Nervo Vago/patologia
[Mh] Termos MeSH secundário: Anestesia
Animais
Carnitina O-Acetiltransferase/metabolismo
Colina O-Acetiltransferase/metabolismo
Endotoxemia/patologia
Hemodinâmica
Inflamação/patologia
Inflamação/fisiopatologia
Interleucina-1beta/sangue
Masculino
Ratos
Ratos Endogâmicos Lew
Choque Séptico/patologia
Fator de Necrose Tumoral alfa/sangue
Vagotomia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Interleukin-1beta); 0 (Tumor Necrosis Factor-alpha); EC 2.3.1.6 (Choline O-Acetyltransferase); EC 2.3.1.7 (Carnitine O-Acetyltransferase)
[Em] Mês de entrada:1406
[Cu] Atualização por classe:140414
[Lr] Data última revisão:
140414
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140226
[St] Status:MEDLINE


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[PMID]:24395925
[Au] Autor:Seiler SE; Martin OJ; Noland RC; Slentz DH; DeBalsi KL; Ilkayeva OR; An J; Newgard CB; Koves TR; Muoio DM
[Ad] Endereço:Department of Pharmacology and Cancer Biology, Duke University, Durham, NC 27704.
[Ti] Título:Obesity and lipid stress inhibit carnitine acetyltransferase activity.
[So] Source:J Lipid Res;55(4):635-44, 2014 Apr.
[Is] ISSN:1539-7262
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Carnitine acetyltransferase (CrAT) is a mitochondrial matrix enzyme that catalyzes the interconversion of acetyl-CoA and acetylcarnitine. Emerging evidence suggests that this enzyme functions as a positive regulator of total body glucose tolerance and muscle activity of pyruvate dehydrogenase (PDH), a mitochondrial enzyme complex that promotes glucose oxidation and is feedback inhibited by acetyl-CoA. Here, we used tandem mass spectrometry-based metabolic profiling to identify a negative relationship between CrAT activity and muscle content of lipid intermediates. CrAT specific activity was diminished in muscles from obese and diabetic rodents despite increased protein abundance. This reduction in enzyme activity was accompanied by muscle accumulation of long-chain acylcarnitines (LCACs) and acyl-CoAs and a decline in the acetylcarnitine/acetyl-CoA ratio. In vitro assays demonstrated that palmitoyl-CoA acts as a direct mixed-model inhibitor of CrAT. Similarly, in primary human myocytes grown in culture, nutritional and genetic manipulations that promoted mitochondrial influx of fatty acids resulted in accumulation of LCACs but a pronounced decrease of CrAT-derived short-chain acylcarnitines. These results suggest that lipid-induced antagonism of CrAT might contribute to decreased PDH activity and glucose disposal in the context of obesity and diabetes.
[Mh] Termos MeSH primário: Carnitina O-Acetiltransferase/metabolismo
Obesidade/enzimologia
[Mh] Termos MeSH secundário: Acetilcoenzima A/metabolismo
Animais
Carnitina/análogos & derivados
Carnitina/metabolismo
Carnitina O-Palmitoiltransferase/metabolismo
Células Cultivadas
Diabetes Mellitus/enzimologia
Seres Humanos
Metabolismo dos Lipídeos
Masculino
Fibras Musculares Esqueléticas/enzimologia
Complexo Piruvato Desidrogenase/metabolismo
Ratos Wistar
Ratos Zucker
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Pyruvate Dehydrogenase Complex); 0 (acylcarnitine); 72-89-9 (Acetyl Coenzyme A); EC 2.3.1.21 (Carnitine O-Palmitoyltransferase); EC 2.3.1.7 (Carnitine O-Acetyltransferase); S7UI8SM58A (Carnitine)
[Em] Mês de entrada:1412
[Cu] Atualização por classe:161202
[Lr] Data última revisão:
161202
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140108
[St] Status:MEDLINE
[do] DOI:10.1194/jlr.M043448


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[PMID]:23581822
[Au] Autor:Liberti D; Rollins JA; Dobinson KF
[Ad] Endereço:Department of Plant Pathology, University of Florida, Gainesville 32611, USA.
[Ti] Título:Peroxysomal carnitine acetyl transferase influences host colonization capacity in Sclerotinia sclerotiorum.
[So] Source:Mol Plant Microbe Interact;26(7):768-80, 2013 Jul.
[Is] ISSN:0894-0282
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In lower eukaryotes, the glyoxylate cycle allows cells to utilize two-carbon compounds when simple sugars are not available. In filamentous fungi, glyoxylate metabolism is coupled with ß-oxidation of fatty acids, and both are localized to ubiquitous eukaryotic organelles called peroxisomes. Acetyl coenzyme A (acetyl-CoA) produced during ß-oxidation is transported via the cytosol into mitochondria for further metabolism. A peroxisomal-specific pathway for acetyl-CoA transport requiring peroxisomal carnitine acetyl transferase (CAT) activity has been identified in Magnaporthe grisea peroxisomes. Here, we report that a Sclerotinia sclerotiorum ortholog of the M. grisea peroxisomal CAT-encoding gene Pth2 (herein designated Ss-pth2) is required for virulence-associated host colonization. Null (ss-pth2) mutants, obtained by in vitro transposon mutagenesis, failed to utilize fatty acids, acetate, or glycerol as sole carbon sources for growth. Gene expression analysis of these mutants showed altered levels of transcript accumulation for glyoxylate cycle enzymes. Ss-pth2 disruption also affected sclerotial, apothecial, and appressorial development and morphology, as well as oxalic acid accumulation when cultured with acetate or oleic acid as sole carbon nutrient sources. Although mutants were able to penetrate and initially colonize host tissue, subsequent colonization was impaired. Genetic complementation with the wild-type Ss-pth2 restored wild-type virulence phenotypes. These findings suggest an essential role in S. sclerotiorum for the peroxisomal metabolic pathways for oxalic acid synthesis and host colonization.
[Mh] Termos MeSH primário: Ascomicetos/enzimologia
Carnitina O-Acetiltransferase/genética
Peroxissomos/enzimologia
Doenças das Plantas/microbiologia
Feijão de Soja/microbiologia
[Mh] Termos MeSH secundário: Acetilcoenzima A/metabolismo
Ascomicetos/genética
Ascomicetos/crescimento & desenvolvimento
Ascomicetos/patogenicidade
Transporte Biológico
Carnitina O-Acetiltransferase/metabolismo
Citosol/enzimologia
Ácidos Graxos/metabolismo
Proteínas Fúngicas/genética
Proteínas Fúngicas/metabolismo
Expressão Gênica
Regulação Fúngica da Expressão Gênica
Teste de Complementação Genética
Mitocôndrias/enzimologia
Mutagênese Insercional
Ácido Oxálico/metabolismo
Oxirredução
Fenótipo
Esporos Fúngicos
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Fatty Acids); 0 (Fungal Proteins); 72-89-9 (Acetyl Coenzyme A); 9E7R5L6H31 (Oxalic Acid); EC 2.3.1.7 (Carnitine O-Acetyltransferase)
[Em] Mês de entrada:1402
[Cu] Atualização por classe:130605
[Lr] Data última revisão:
130605
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:130416
[St] Status:MEDLINE
[do] DOI:10.1094/MPMI-03-13-0075-R



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