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[PMID]:29229387
[Au] Autor:Pan Y; Jing J; Qiao L; Liu J; Zhao J; An L; Li B; Wang W; Liang C; Liu W
[Ad] Endereço:College of Animal Science and Veterinary Medicine, Shanxi Agricultural University, Taigu, Shanxi 030801, China.
[Ti] Título:miR-124-3p affects the formation of intramuscular fat through alterations in branched chain amino acid consumption in sheep.
[So] Source:Biochem Biophys Res Commun;495(2):1769-1774, 2018 01 08.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Intramuscular fat is used to determine meat quality in animals; however, factors affecting branched chain amino acid (BCAA) catabolism, which fuels adipogenesis and lipogenesis, remain unclear. To better understand the post-transcriptional influence on BCAA catabolism during adipogenesis, we investigated the role of miR-124-3p. Stromal vascular fraction (SVF) cells were isolated from skeletal muscle of sheep, and induced to differentiate. We determined the roles of miR-124-3p and its predicted target, branched chain keto acid dehydrogenase E1, alpha polypeptide (BCKDHA), in adipogenic differentiation and lipogenesis of SVFs after overexpressing or inhibiting miR-124-3p or BCKDHA, respectively. miR-124-3p altered the luciferase activity of constructs containing 3'-UTR of BCKDHA and the formation of lipid droplets, along with the adipogenic markers and BCAA consumption. Besides, the adipogenic performance and BCAA consumption in BCKDHA-overexpressing or knocked-down SVFs and the expression of adipogenic marker genes were altered. We demonstrate that miR-124-3p is an important factor for adipogenesis and provide insights into the formation of intramuscular fat in animals.
[Mh] Termos MeSH primário: Adipogenia/genética
Aminoácidos de Cadeia Ramificada/metabolismo
MicroRNAs/genética
Ovinos/crescimento & desenvolvimento
Ovinos/genética
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida)/genética
3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida)/metabolismo
Adipócitos/citologia
Adipócitos/metabolismo
Adipogenia/fisiologia
Animais
Diferenciação Celular/genética
MicroRNAs/metabolismo
Músculo Esquelético/citologia
Músculo Esquelético/crescimento & desenvolvimento
Músculo Esquelético/metabolismo
Ovinos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (Amino Acids, Branched-Chain); 0 (MicroRNAs); EC 1.2.4.4 (3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide))
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171213
[St] Status:MEDLINE


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[PMID]:28490063
[Au] Autor:Wang B; Bai Y; Fan T; Zheng X; Cai Y
[Ad] Endereço:The Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 Lihu Road, Wuxi, Jiangsu 214122, China.
[Ti] Título:Characterisation of a thiamine diphosphate-dependent alpha-keto acid decarboxylase from Proteus mirabilis JN458.
[So] Source:Food Chem;232:19-24, 2017 Oct 01.
[Is] ISSN:0308-8146
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Alpha-keto acid decarboxylases can convert keto acids to their corresponding aldehydes, which are often volatile aroma compounds. The gene encoding α-keto acid decarboxylase in Proteus mirabilis JN458 was cloned, and the enzyme overexpressed in Escherichia coli BL21 (DE3), purified in high yield, and characterised. The molecular weight is 62.291kDa by MALDI-TOF MS, and optimum activity at pH 6.0 and 40-50°C. The enzyme is a typical decarboxylase, dependent on thiamine diphosphate and Mg as cofactors. For the decarboxylation reaction, the enzyme displayed a broad substrate range. Kinetic parameters were determined using 4-methyl-2-oxopentanoic acid, phenyl pyruvate and 3-methyl-2-oxopentanoic acid as substrates. K and k values for phenyl pyruvate were 0.62mM and 77.38s , respectively, and the k /K value was 124.81mM s . The enzyme properties suggest it may act effectively under cheese ripening conditions.
[Mh] Termos MeSH primário: 3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida)/metabolismo
Proteínas de Bactérias/metabolismo
Proteus mirabilis/enzimologia
Tiamina Pirofosfato/metabolismo
[Mh] Termos MeSH secundário: 3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida)/química
Proteínas de Bactérias/química
Ativação Enzimática
Cinética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); EC 1.2.4.4 (3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)); Q57971654Y (Thiamine Pyrophosphate)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170816
[Lr] Data última revisão:
170816
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170512
[St] Status:MEDLINE


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[PMID]:27689828
[Au] Autor:Estrada-Alcalde I; Tenorio-Guzman MR; Tovar AR; Salinas-Rubio D; Torre-Villalvazo I; Torres N; Noriega LG
[Ad] Endereço:Depto. de Fisiología de la Nutrición, Instituto Nacional de Ciencias Médicas y Nutrición "Salvador Zubirán", Ciudad de México, México.
[Ti] Título:Metabolic Fate of Branched-Chain Amino Acids During Adipogenesis, in Adipocytes From Obese Mice and C2C12 Myotubes.
[So] Source:J Cell Biochem;118(4):808-818, 2017 Apr.
[Is] ISSN:1097-4644
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Branched-chain amino acid (BCAA) catabolism is regulated by the branched-chain aminotransferase (BCAT2) and the branched-chain α-keto acid dehydrogenase complex (BCKDH). BCAT2 and BCKDH expression and activity are modified during adipogenesis and altered in adipose tissues of mice with genetic or diet-induced obesity. However, little is known about how these modifications and alterations affect the intracellular metabolic fate of BCAAs during adipogenesis, in adipocytes from mice fed a control or high-fat diet or in C2C12 myotubes. Here, we demonstrate that BCAAs are mainly incorporated into proteins during the early stages of adipocyte differentiation. However, they are oxidized and incorporated into lipids during the late days of differentiation. Conversely, 92% and 97% of BCAA were oxidized, 1.6% and 6% were used for protein synthesis and 1.2% and 1.5% were incorporated into lipids in adipocytes from epididymal and subcutaneous adipose tissue, respectively. All three pathways were decreased in adipocytes from mice fed a high-fat diet. In C2C12 myotubes, leucine is mainly used for protein synthesis and palmitate is incorporated into lipids. Interestingly, leucine decreased both palmitate oxidation and its incorporation to lipids and proteins; and palmitate increased leucine oxidation and decreased its incorporation to lipids and proteins in a dose-dependent manner. These results demonstrate that BCAA metabolic fate differs between the early and late stages of adipocyte differentiation and in adipocytes from mice fed a control or high-fat diet; and that leucine affects the metabolic fate of palmitate and vice versa in C2C12 myotubes. J. Cell. Biochem. 118: 808-818, 2017. © 2016 Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Adipócitos/metabolismo
Adipogenia/fisiologia
Aminoácidos de Cadeia Ramificada/metabolismo
Fibras Musculares Esqueléticas/metabolismo
Obesidade/metabolismo
[Mh] Termos MeSH secundário: 3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida)/genética
3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida)/metabolismo
Células 3T3-L1
Adipócitos/patologia
Adipogenia/genética
Animais
Diferenciação Celular/genética
Diferenciação Celular/fisiologia
Linhagem Celular
Células Cultivadas
Dieta Hiperlipídica/efeitos adversos
Metabolismo dos Lipídeos
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Obesidade/genética
Ácido Palmítico/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Transaminases/genética
Transaminases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids, Branched-Chain); 0 (RNA, Messenger); 2V16EO95H1 (Palmitic Acid); EC 1.2.4.4 (3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)); EC 2.6.1.- (Transaminases); EC 2.6.1.42 (branched-chain-amino-acid transaminase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161001
[St] Status:MEDLINE
[do] DOI:10.1002/jcb.25755


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[PMID]:25849292
[Au] Autor:Afzal MI; Ariceaga CC; Boulahya KA; Jacquot M; Delaunay S; Cailliez-Grimal C
[Ad] Endereço:a Laboratoire d'ingénierie des Biomolécules , Université de Lorraine , Vandoeuvre-lès-Nancy , France.
[Ti] Título:Biosynthesis and role of 3-methylbutanal in cheese by lactic acid bacteria: Major metabolic pathways, enzymes involved, and strategies for control.
[So] Source:Crit Rev Food Sci Nutr;57(2):399-406, 2017 Jan 22.
[Is] ISSN:1549-7852
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Branched chain aldehyde, 3-methylbutanal is associated as a key flavor compound with many hard and semi-hard cheese varieties. The presence and impact of this flavor compound in bread, meat, and certain beverages has been recently documented, however its presence and consequences regarding cheese flavor were not clearly reported. This paper gives an overview of the role of 3-methylbutanal in cheese, along with the major metabolic pathways and key enzymes leading to its formation. Moreover, different strategies are highlighted for the control of this particular flavor compound in specific cheese types.
[Mh] Termos MeSH primário: Aldeídos/metabolismo
Proteínas de Bactérias/metabolismo
Queijo/análise
Contaminação de Alimentos/prevenção & controle
[Mh] Termos MeSH secundário: 3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida)/metabolismo
Aldeídos/análise
Aldeídos/toxicidade
Carboxiliases/metabolismo
Carnobacterium/enzimologia
Carnobacterium/crescimento & desenvolvimento
Carnobacterium/metabolismo
Queijo/microbiologia
Enterococcus/enzimologia
Enterococcus/crescimento & desenvolvimento
Enterococcus/metabolismo
Qualidade dos Alimentos
Glutamato Desidrogenase/metabolismo
Lactobacillus/enzimologia
Lactobacillus/crescimento & desenvolvimento
Lactobacillus/metabolismo
Lactococcus/enzimologia
Lactococcus/crescimento & desenvolvimento
Lactococcus/metabolismo
Controle de Qualidade
Streptococcus/enzimologia
Streptococcus/crescimento & desenvolvimento
Streptococcus/metabolismo
Paladar
Transaminases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Aldehydes); 0 (Bacterial Proteins); 69931RWI96 (isovalerylaldehyde); EC 1.2.4.4 (3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)); EC 1.4.1.2 (Glutamate Dehydrogenase); EC 2.6.1.- (Transaminases); EC 4.1.1.- (Carboxy-Lyases)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170221
[Lr] Data última revisão:
170221
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150408
[St] Status:MEDLINE


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[PMID]:27974115
[Au] Autor:Li T; Wang Y; Li C; Xu WW; Niu FH; Zhang D
[Ad] Endereço:Department of Pediatrics, Affiliated Hospital of Jining Medical University, Jining, Shandong 272000, China. jyfylitao@163.com.
[Ti] Título:[Maple syrup urine disease and gene mutations in twin neonates].
[So] Source:Zhongguo Dang Dai Er Ke Za Zhi;18(12):1242-1246, 2016 Dec.
[Is] ISSN:1008-8830
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:OBJECTIVE: To investigate the clinical features of one pair of twin neonates with maple syrup urine disease (MSUD) in the Chinese Han population and pathogenic mutations in related genes, and to provide guidance for the early diagnosis and treatment of MSUD. METHODS: The clinical and imaging data of the twin neonates were collected. The peripheral blood samples were collected from the twin neonates and their parents to detect the genes related to MSUD (BCKDHA, BCKDHB, DBT, and DLD). The loci with gene mutations were identified, and a bioinformatic analysis was performed. RESULTS: Two mutations were detected in the BCKDHB gene, missense mutation c.304G>A (p.Gly102Arg) and nonsense mutation c.331C>T (p.Arg111*), and both of them were heterozygotes. The mutation c.304G>A (p.Gly102Arg) had not been reported in the world. Their father carried the missense mutation c.304G>A (p.Gly102Arg), and their mother carried the nonsense mutation c.331C>T (p.Arg111*). CONCLUSIONS: The c.331C>T (p.Arg111*) heterozygous mutation in BCKDHB gene is the pathogenic mutation in these twin neonates and provides a genetic and molecular basis for the clinical features of children with MSUD.
[Mh] Termos MeSH primário: 3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida)/genética
Doenças em Gêmeos
Doença da Urina de Xarope de Bordo/genética
Mutação
[Mh] Termos MeSH secundário: Feminino
Seres Humanos
Recém-Nascido
Masculino
[Pt] Tipo de publicação:CASE REPORTS; JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.2.4.4 (3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide))
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170601
[Lr] Data última revisão:
170601
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161216
[St] Status:MEDLINE


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[PMID]:27677863
[Au] Autor:Kleber A; Maurer F; Lorenz D; Wolf B; Albrecht F; Shopova T; Sessler DI; Volk T; Kreuer S; Fink T
[Ad] Endereço:Department of Anaesthesiology, Center of Breath Research, Intensive Care and Pain Therapy, Saarland University Medical Center, Homburg (Saar), Germany. Both authors contributed equally to the manuscript.
[Ti] Título:Metabolism of 3-pentanone under inflammatory conditions.
[So] Source:J Breath Res;10(4):047101, 2016 09 28.
[Is] ISSN:1752-7163
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Breath analysis of rats using multi-capillary column ion-mobility spectrometry (MCC-IMS) revealed alterations in acetone and other ketones, including 3-pentanone, during inflammation. The alterations seem likely to result from oxidative branched-chain keto acid (BCKA) catabolism. We therefore tested the hypothesis that 3-pentanone arises during inflammation from increased BCKA oxidation in the liver with consequent accumulation of propionyl-CoA and its condensation products. Male Sprague-Dawley rats were anaesthetised and ventilated for 24 h or until death. Exhaled breath was analysed by MCC-IMS while rats were injected with low and high doses of lipopolysaccharide (LPS), tumour necrosis factor α (TNFα), or vehicle. The exhaled 3-pentanone peak was identified by pure substance measurements. Blood was collected 12 h after treatment for the determination of cytokine concentrations; transcription enzymes for BCKA catabolism and the activity of the BCKA dehydrogenase were analysed in liver tissue by quantitative real-time PCR and western blotting. Exhaled 3-pentanone decreased in all groups, but minimum concentrations with high-dose LPS (0.24 ± 0.31 volts; mean ± SD), low-dose TNFα (0.17 ± 0.10 volts) and high-dose TNFα (0.13 ± 0.04 volts) were lower than in vehicle animals (0.27 ± 0.12 volts). At 60% and 85% survival times (svt) concentrations of exhaled 3-pentanone increased significantly in all animals treated with low-dose LPS, (svt 0.38 ± 0.18 volts, svt 0.62 ± 0.15 volts) and high-dose LPS (0.26 ± 0.28 volts, 0.40 ± 0.22 volts), as well as low-dose TNFα, (0.20 ± 0.09 volts, 0.39 ± 0.17 volts) and high-dose TNFα (0.18 ± 0.06 volts, 0.34 ± 0.08 volts), but not in vehicle rats (0.27 ± 0.12 volts, 0.30 ± 0.09 volts). BCKA catabolism was seen in the liver, with increased expression and activity of the branched-chain alpha-keto acid dehydrogenase (BCKD), lower expression of the propionyl-CoA carboxylase (PCC) subunits, and altered expression levels of BCKD regulating enzymes. Exhaled 3-pentanone may arise from altered BCKA catabolism. Our results suggest that excessive propionyl-CoA is possibly generated from BCKAs via increased activity of BCKD, but may undergo unusual condensation reactions rather than being physiologically processed to methylmalonyl-CoA by PCC. The pattern of 3-pentanone during early and prolonged inflammation suggests that reuse of BCKAs for the synthesis of new proteins might be initially favoured. As inflammatory conditions persist, substrates for cellular energy supply are required which activate irreversible degradation of excessive BCKA to propionyl-CoA yielding increased levels of exhaled 3-pentanone.
[Mh] Termos MeSH primário: Inflamação/metabolismo
Pentanonas/metabolismo
[Mh] Termos MeSH secundário: 3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida)/metabolismo
Aminoácidos de Cadeia Ramificada/metabolismo
Animais
Calibragem
Expiração/efeitos dos fármacos
Regulação da Expressão Gênica/efeitos dos fármacos
Interleucina-10/sangue
Interleucina-6/sangue
Lipopolissacarídeos/administração & dosagem
Lipopolissacarídeos/farmacologia
Fígado/efeitos dos fármacos
Fígado/metabolismo
Masculino
Fosforilação/efeitos dos fármacos
Ratos Sprague-Dawley
Reprodutibilidade dos Testes
Fatores de Tempo
Fator de Necrose Tumoral alfa/administração & dosagem
Fator de Necrose Tumoral alfa/farmacologia
Compostos Orgânicos Voláteis/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Amino Acids, Branched-Chain); 0 (Interleukin-6); 0 (Lipopolysaccharides); 0 (Pentanones); 0 (Tumor Necrosis Factor-alpha); 0 (Volatile Organic Compounds); 130068-27-8 (Interleukin-10); 9SLZ98M9NK (diethyl ketone); EC 1.2.4.4 (3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide))
[Em] Mês de entrada:1704
[Cu] Atualização por classe:170417
[Lr] Data última revisão:
170417
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160929
[St] Status:MEDLINE
[do] DOI:10.1088/1752-7155/10/4/047101


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[PMID]:27642608
[Au] Autor:Zhao X; Han Q; Liu Y; Sun C; Gang X; Wang G
[Ad] Endereço:Department of Endocrinology and Metabolism, The First Hospital of Jilin University, Changchun 130021, China.
[Ti] Título:The Relationship between Branched-Chain Amino Acid Related Metabolomic Signature and Insulin Resistance: A Systematic Review.
[So] Source:J Diabetes Res;2016:2794591, 2016.
[Is] ISSN:2314-6753
[Cp] País de publicação:Egypt
[La] Idioma:eng
[Ab] Resumo:Recent studies have shown the positive association between increased circulating BCAAs (valine, leucine, and isoleucine) and insulin resistance (IR) in obese or diabetic patients. However, results seem to be controversial in different races, diets, and distinct tissues. Our aims were to evaluate the relationship between BCAA and IR as well as later diabetes risk and explore the phenotypic and genetic factors influencing BCAA level based on available studies. We performed systematic review, searching MEDLINE, EMASE, ClinicalTrials.gov, the Cochrane Library, and Web of Science from inception to March 2016. After selection, 23 studies including 20,091 participants were included. Based on current evidence, we found that BCAA is a useful biomarker for early detection of IR and later diabetic risk. Factors influencing BCAA level can be divided into four parts: race, gender, dietary patterns, and gene variants. These factors might not only contribute to the elevated BCAA level but also show obvious associations with insulin resistance. Genes related to BCAA catabolism might serve as potential targets for the treatment of IR associated metabolic disorders. Moreover, these factors should be controlled properly during study design and data analysis. In the future, more large-scale studies with elaborate design addressing BCAA and IR are required.
[Mh] Termos MeSH primário: Aminoácidos de Cadeia Ramificada/metabolismo
Grupos de Populações Continentais
Diabetes Mellitus/metabolismo
Dieta
Resistência à Insulina
Metaboloma
Obesidade/metabolismo
[Mh] Termos MeSH secundário: 3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida)/genética
Proteínas Adaptadoras de Transdução de Sinal/genética
Genótipo
Seres Humanos
Antígenos de Histocompatibilidade Menor/genética
Fenótipo
Proteínas da Gravidez/genética
Proteína Fosfatase 2C/genética
Fatores Sexuais
Transaminases/genética
Perda de Peso
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Amino Acids, Branched-Chain); 0 (GCKR protein, human); 0 (Minor Histocompatibility Antigens); 0 (Pregnancy Proteins); EC 1.2.4.4 (3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)); EC 2.6.1. (BCAT1 protein, human); EC 2.6.1.- (Transaminases); EC 2.6.1.42 (BCAT2 protein, human); EC 3.1.3.16 (PPM1K protein, human); EC 3.1.3.16 (Protein Phosphatase 2C)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170609
[Lr] Data última revisão:
170609
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160920
[St] Status:MEDLINE
[do] DOI:10.1155/2016/2794591


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[PMID]:27542406
[Au] Autor:Wang W; Zhang F; Xia Y; Zhao S; Yan W; Wang H; Lee Y; Li C; Zhang L; Lian K; Gao E; Cheng H; Tao L
[Ad] Endereço:Department of Cardiology, Xijing Hospital, Fourth Military Medical University, Xi'an, China; and.
[Ti] Título:Defective branched chain amino acid catabolism contributes to cardiac dysfunction and remodeling following myocardial infarction.
[So] Source:Am J Physiol Heart Circ Physiol;311(5):H1160-H1169, 2016 Nov 01.
[Is] ISSN:1522-1539
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cardiac metabolic remodeling is a central event during heart failure (HF) development following myocardial infarction (MI). It is well known that myocardial glucose and fatty acid dysmetabolism contribute to post-MI cardiac dysfunction and remodeling. However, the role of amino acid metabolism in post-MI HF remains elusive. Branched chain amino acids (BCAAs) are an important group of essential amino acids and function as crucial nutrient signaling in mammalian animals. The present study aimed to determine the role of cardiac BCAA metabolism in post-MI HF progression. Utilizing coronary artery ligation-induced murine MI models, we found that myocardial BCAA catabolism was significantly impaired in response to permanent MI, therefore leading to an obvious elevation of myocardial BCAA abundance. In MI-operated mice, oral BCAA administration further increased cardiac BCAA levels, activated the mammalian target of rapamycin (mTOR) signaling, and exacerbated cardiac dysfunction and remodeling. These data demonstrate that BCAAs act as a direct contributor to post-MI cardiac pathologies. Furthermore, these BCAA-mediated deleterious effects were improved by rapamycin cotreatment, revealing an indispensable role of mTOR in BCAA-mediated adverse effects on cardiac function/structure post-MI. Of note, pharmacological inhibition of branched chain ketoacid dehydrogenase kinase (BDK), a negative regulator of myocardial BCAA catabolism, significantly improved cardiac BCAA catabolic disorders, reduced myocardial BCAA levels, and ameliorated post-MI cardiac dysfunction and remodeling. In conclusion, our data provide the evidence that impaired cardiac BCAA catabolism directly contributes to post-MI cardiac dysfunction and remodeling. Moreover, improving cardiac BCAA catabolic defects may be a promising therapeutic strategy against post-MI HF.
[Mh] Termos MeSH primário: 3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida)/metabolismo
Aminoácidos de Cadeia Ramificada/metabolismo
Insuficiência Cardíaca/metabolismo
Infarto do Miocárdio/metabolismo
Miocárdio/metabolismo
Disfunção Ventricular Esquerda/metabolismo
Remodelação Ventricular
[Mh] Termos MeSH secundário: Animais
Western Blotting
Vasos Coronários/cirurgia
Ecocardiografia
Ácidos Graxos/metabolismo
Glucose/metabolismo
Insuficiência Cardíaca/etiologia
Marcação In Situ das Extremidades Cortadas
Ligadura
Masculino
Camundongos
Infarto do Miocárdio/complicações
Peptídeo Natriurético Encefálico/metabolismo
Proteínas Quinases/metabolismo
Proteína Fosfatase 2C/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Reação em Cadeia da Polimerase Via Transcriptase Reversa
Transdução de Sinais
Serina-Treonina Quinases TOR/metabolismo
Disfunção Ventricular Esquerda/etiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amino Acids, Branched-Chain); 0 (Fatty Acids); 114471-18-0 (Natriuretic Peptide, Brain); EC 1.2.4.4 (3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)); EC 2.7.- (Protein Kinases); EC 2.7.1.1 (TOR Serine-Threonine Kinases); EC 2.7.1.1 (mTOR protein, mouse); EC 2.7.11.4 ((3-methyl-2-oxobutanoate dehydrogenase (lipoamide)) kinase); EC 3.1.3.16 (PPM1A protein, human); EC 3.1.3.16 (Protein Phosphatase 2C); IY9XDZ35W2 (Glucose)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170630
[Lr] Data última revisão:
170630
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160821
[St] Status:MEDLINE
[do] DOI:10.1152/ajpheart.00114.2016


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[PMID]:27472223
[Au] Autor:Zigler JS; Hodgkinson CA; Wright M; Klise A; Sundin O; Broman KW; Hejtmancik F; Huang H; Patek B; Sergeev Y; Hose S; Brayton C; Xaiodong J; Vasquez D; Maragakis N; Mori S; Goldman D; Hoke A; Sinha D
[Ad] Endereço:Department of Ophthalmology, The Johns Hopkins University School of Medicine, Baltimore, MD, United States of America.
[Ti] Título:A Spontaneous Missense Mutation in Branched Chain Keto Acid Dehydrogenase Kinase in the Rat Affects Both the Central and Peripheral Nervous Systems.
[So] Source:PLoS One;11(7):e0160447, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:A novel mutation, causing a phenotype we named frogleg because its most obvious characteristic is a severe splaying of the hind limbs, arose spontaneously in a colony of Sprague-Dawley rats. Frogleg is a complex phenotype that includes abnormalities in hind limb function, reduced brain weight with dilated ventricles and infertility. Using micro-satellite markers spanning the entire rat genome, the mutation was mapped to a region of rat chromosome 1 between D1Rat131 and D1Rat287. Analysis of whole genome sequencing data within the linkage interval, identified a missense mutation in the branched-chain alpha-keto dehydrogenase kinase (Bckdk) gene. The protein encoded by Bckdk is an integral part of an enzyme complex located in the mitochondrial matrix of many tissues which regulates the levels of the branched-chain amino acids (BCAAs), leucine, isoleucine and valine. BCAAs are essential amino acids (not synthesized by the body), and circulating levels must be tightly regulated; levels that are too high or too low are both deleterious. BCKDK phosphorylates Ser293 of the E1α subunit of the BCKDH protein, which catalyzes the rate-limiting step in the catabolism of the BCAAs, inhibiting BCKDH and thereby, limiting breakdown of the BCAAs. In contrast, when Ser293 is not phosphorylated, BCKDH activity is unchecked and the levels of the BCAAs will decrease dramatically. The mutation is located within the kinase domain of Bckdk and is predicted to be damaging. Consistent with this, we show that in rats homozygous for the mutation, phosphorylation of BCKDH in the brain is markedly decreased relative to wild type or heterozygous littermates. Further, circulating levels of the BCAAs are reduced by 70-80% in animals homozygous for the mutation. The frogleg phenotype shares important characteristics with a previously described Bckdk knockout mouse and with human subjects with Bckdk mutations. In addition, we report novel data regarding peripheral neuropathy of the hind limbs.
[Mh] Termos MeSH primário: 3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida)/genética
Sistema Nervoso Central/enzimologia
Mutação de Sentido Incorreto
Sistema Nervoso Periférico/enzimologia
[Mh] Termos MeSH secundário: Animais
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.2.4.4 (3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide))
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170804
[Lr] Data última revisão:
170804
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160730
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0160447


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[PMID]:27320015
[Au] Autor:Sirobhushanam S; Galva C; Sen S; Wilkinson BJ; Gatto C
[Ad] Endereço:School of Biological Sciences, Illinois State University, Normal, IL 61790, USA.
[Ti] Título:Broad substrate specificity of phosphotransbutyrylase from Listeria monocytogenes: A potential participant in an alternative pathway for provision of acyl CoA precursors for fatty acid biosynthesis.
[So] Source:Biochim Biophys Acta;1861(9 Pt A):1102-1110, 2016 09.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Listeria monocytogenes, the causative organism of the serious food-borne disease listeriosis, has a membrane abundant in branched-chain fatty acids (BCFAs). BCFAs are normally biosynthesized from branched-chain amino acids via the activity of branched chain α-keto acid dehydrogenase (Bkd), and disruption of this pathway results in reduced BCFA content in the membrane. Short branched-chain carboxylic acids (BCCAs) added as media supplements result in incorporation of BCFAs arising from the supplemented BCCAs in the membrane of L. monocytogenes bkd mutant MOR401. High concentrations of the supplements also effect similar changes in the membrane of the wild type organism with intact bkd. Such carboxylic acids clearly act as fatty acid precursors, and there must be an alternative pathway resulting in the formation of their CoA thioester derivatives. Candidates for this are the enzymes phosphotransbutyrylase (Ptb) and butyrate kinase (Buk), the products of the first two genes of the bkd operon. Ptb from L. monocytogenes exhibited broad substrate specificity, a strong preference for branched-chain substrates, a lack of activity with acetyl CoA and hexanoyl CoA, and strict chain length preference (C3-C5). Ptb catalysis involved ternary complex formation. Additionally, Ptb could utilize unnatural branched-chain substrates such as 2-ethylbutyryl CoA, albeit with lower efficiency, consistent with a potential involvement of this enzyme in the conversion of the carboxylic acid additives into CoA primers for BCFA biosynthesis.
[Mh] Termos MeSH primário: 3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida)/genética
Aminoácidos de Cadeia Ramificada/biossíntese
Ácidos Graxos/biossíntese
Fosfato Acetiltransferase/metabolismo
Fosfotransferases (Aceptor do Grupo Carboxila)/genética
[Mh] Termos MeSH secundário: 3-Metil-2-Oxobutanoato Desidrogenase (Lipoamida)/metabolismo
Acil Coenzima A/metabolismo
Aminoácidos de Cadeia Ramificada/metabolismo
Ácidos Graxos/metabolismo
Seres Humanos
Lipogênese/genética
Listeria monocytogenes/genética
Listeria monocytogenes/patogenicidade
Listeriose/genética
Listeriose/microbiologia
Listeriose/patologia
Redes e Vias Metabólicas
Fosfato Acetiltransferase/genética
Fosfotransferases (Aceptor do Grupo Carboxila)/metabolismo
Especificidade por Substrato
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Acyl Coenzyme A); 0 (Amino Acids, Branched-Chain); 0 (Fatty Acids); 5060-32-2 (hexanoyl-coenzyme A); EC 1.2.4.4 (3-Methyl-2-Oxobutanoate Dehydrogenase (Lipoamide)); EC 2.3.1.8 (Phosphate Acetyltransferase); EC 2.7.2.- (Phosphotransferases (Carboxyl Group Acceptor)); EC 2.7.2.7 (butyrate kinase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170902
[Lr] Data última revisão:
170902
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160621
[St] Status:MEDLINE



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