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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]:28204983
[Au] Autor:Jeon JM; Kim HJ; Bhatia SK; Sung C; Seo HM; Kim JH; Park HY; Lee D; Brigham CJ; Yang YH
[Ad] Endereço:Department of Bioengineering, College of Engineering, Konkuk University, Seoul, South Korea.
[Ti] Título:Application of acetyl-CoA acetyltransferase (AtoAD) in Escherichia coli to increase 3-hydroxyvalerate fraction in poly(3-hydroxybutyrate-co-3-hydroxyvalerate).
[So] Source:Bioprocess Biosyst Eng;40(5):781-789, 2017 May.
[Is] ISSN:1615-7605
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Polyhydroxyalkanoate (PHA) is a family of biodegradable polymers, and incorporation of different monomers can alter its physical properties. To produce the copolymer poly(3-hydroxybutyrate-co-3-hydroxyvalerate) (P(3HB-co-3HV)) containing a high level of 3-hydroxyvalerate (3HV) by altering acetyl-CoA pool levels, we overexpressed an acetyl-CoA acetyltransferase (atoAD) in an engineered E. coli strain, YH090, carrying PHA synthetic genes bktB, phaB, and phaC. It was found that, with introduction of atoAD and with propionate as a co-substrate, 3HV fraction in PHA was increased up to 7.3-fold higher than a strain without atoAD expressed in trans (67.9 mol%). By the analysis of CoA pool concentrations in vivo and in vitro using HPLC and LC-MS, overexpression of AtoAD was shown to decrease the amount of acetyl-CoA and increase the propionyl-CoA/acetyl-CoA ratio, ultimately resulting in an increased 3HV fraction in PHA. Finally, synthesis of P(3HB-co-3HV) containing 57.9 mol% of 3HV was achieved by fed-batch fermentation of YJ101 with propionate.
[Mh] Termos MeSH primário: Acetil-CoA C-Acetiltransferase/biossíntese
Proteínas de Escherichia coli/biossíntese
Escherichia coli/metabolismo
Ácidos Pentanoicos/metabolismo
Poliésteres/metabolismo
[Mh] Termos MeSH secundário: Acetil-CoA C-Acetiltransferase/genética
Escherichia coli/genética
Proteínas de Escherichia coli/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Escherichia coli Proteins); 0 (Pentanoic Acids); 0 (Polyesters); 0 (poly(3-hydroxybutyrate)-co-(3-hydroxyvalerate)); 10237-77-1 (beta-hydroxyvaleric acid); EC 2.3.1.9 (Acetyl-CoA C-Acetyltransferase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170501
[Lr] Data última revisão:
170501
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170217
[St] Status:MEDLINE
[do] DOI:10.1007/s00449-017-1743-9


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[PMID]:28062645
[Au] Autor:Harijan RK; Kiema TR; Syed SM; Qadir I; Mazet M; Bringaud F; Michels PAM; Wierenga RK
[Ad] Endereço:Faculty of Biochemistry and Molecular Medicine, Biocenter Oulu, University of Oulu, FIN-90014, Finland.
[Ti] Título:Crystallographic substrate binding studies of Leishmania mexicana SCP2-thiolase (type-2): unique features of oxyanion hole-1.
[So] Source:Protein Eng Des Sel;30(3):225-233, 2017 Mar 01.
[Is] ISSN:1741-0134
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:C: Structures of the C123A variant of the dimeric Leishmania mexicana SCP2-thiolase (type-2) (Lm-thiolase), complexed with acetyl-CoA and acetoacetyl-CoA, respectively, are reported. The catalytic site of thiolase contains two oxyanion holes, OAH1 and OAH2, which are important for catalysis. The two structures reveal for the first time the hydrogen bond interactions of the CoA-thioester oxygen atom of the substrate with the hydrogen bond donors of OAH1 of a CHH-thiolase. The amino acid sequence fingerprints ( xS, EAF, G P) of three catalytic loops identify the active site geometry of the well-studied CNH-thiolases, whereas SCP2-thiolases (type-1, type-2) are classified as CHH-thiolases, having as corresponding fingerprints xS, DCF and G P. In all thiolases, OAH2 is formed by the main chain NH groups of two catalytic loops. In the well-studied CNH-thiolases, OAH1 is formed by a water (of the Wat-Asn(NEAF) dyad) and NE2 (of the GHP-histidine). In the two described liganded Lm-thiolase structures, it is seen that in this CHH-thiolase, OAH1 is formed by NE2 of His338 (HDCF) and His388 (GHP). Analysis of the OAH1 hydrogen bond networks suggests that the GHP-histidine is doubly protonated and positively charged in these complexes, whereas the HDCF histidine is neutral and singly protonated.
[Mh] Termos MeSH primário: Acetil-CoA C-Acetiltransferase/química
Leishmania mexicana/enzimologia
Proteínas de Protozoários/química
[Mh] Termos MeSH secundário: Domínio Catalítico
Cristalografia por Raios X
Estrutura Secundária de Proteína
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Protozoan Proteins); EC 2.3.1.9 (Acetyl-CoA C-Acetyltransferase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170605
[Lr] Data última revisão:
170605
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170108
[St] Status:MEDLINE
[do] DOI:10.1093/protein/gzw080


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[PMID]:28045448
[Au] Autor:Chen Q; Yan J; Meng X; Xu F; Zhang W; Liao Y; Qu J
[Ad] Endereço:College of Horticulture and Gardening, Yangtze University, Jingzhou 434025, Hubei, China. chenqwx@foxmail.com.
[Ti] Título:Molecular Cloning, Characterization, and Functional Analysis of Acetyl-CoA C-Acetyltransferase and Mevalonate Kinase Genes Involved in Terpene Trilactone Biosynthesis from Ginkgo biloba.
[So] Source:Molecules;22(1), 2017 Jan 02.
[Is] ISSN:1420-3049
[Cp] País de publicação:Switzerland
[La] Idioma:eng
[Ab] Resumo:Ginkgolides and bilobalide, collectively termed terpene trilactones (TTLs), are terpenoids that form the main active substance of . Terpenoids in the mevalonate (MVA) biosynthetic pathway include acetyl-CoA -acetyltransferase (AACT) and mevalonate kinase (MVK) as core enzymes. In this study, two full-length (cDNAs) encoding AACT ( , GenBank Accession No. KX904942) and MVK ( , GenBank Accession No. KX904944) were cloned from . The deduced GbAACT and GbMVK proteins contain 404 and 396 amino acids with the corresponding open-reading frame (ORF) sizes of 1215 bp and 1194 bp, respectively. Tissue expression pattern analysis revealed that was highly expressed in ginkgo fruits and leaves, and was highly expressed in leaves and roots. The functional complementation of in AACT-deficient strain and in MVK-deficient strain confirmed that mediated the conversion of mevalonate acetyl-CoA to acetoacetyl-CoA and mediated the conversion of mevalonate to mevalonate phosphate. This observation indicated that and are functional genes in the cytosolic mevalonate (MVA) biosynthesis pathway. After seedlings were treated with methyl jasmonate and salicylic acid, the expression levels of and increased, and TTL production was enhanced. The cloning, characterization, expression and functional analysis of and will be helpful to understand more about the role of these two genes involved in TTL biosynthesis.
[Mh] Termos MeSH primário: Acetil-CoA C-Acetiltransferase/genética
Acetil-CoA C-Acetiltransferase/metabolismo
Ginkgo biloba/enzimologia
Lactonas/metabolismo
Fosfotransferases (Aceptor do Grupo Álcool)/genética
Fosfotransferases (Aceptor do Grupo Álcool)/metabolismo
[Mh] Termos MeSH secundário: Acetatos/farmacologia
Vias Biossintéticas
Clonagem Molecular
Ciclopentanos/farmacologia
Regulação Enzimológica da Expressão Gênica
Regulação da Expressão Gênica de Plantas/efeitos dos fármacos
Ginkgo biloba/química
Ginkgo biloba/genética
Ácido Mevalônico/metabolismo
Fases de Leitura Aberta
Especificidade de Órgãos
Oxilipinas/farmacologia
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Ácido Salicílico/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acetates); 0 (Cyclopentanes); 0 (Lactones); 0 (Oxylipins); 0 (Plant Proteins); 0 (trilactone); 900N171A0F (methyl jasmonate); EC 2.3.1.9 (Acetyl-CoA C-Acetyltransferase); EC 2.7.1.- (Phosphotransferases (Alcohol Group Acceptor)); EC 2.7.1.36 (mevalonate kinase); O414PZ4LPZ (Salicylic Acid); S5UOB36OCZ (Mevalonic Acid)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170505
[Lr] Data última revisão:
170505
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170104
[St] Status:MEDLINE


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[PMID]:27678191
[Au] Autor:Wang B; He PP; Zeng GF; Zhang T; Ou Yang XP
[Ad] Endereço:Department of Cardiovascular Medicine, The Second Affiliated Hospital, University of South China, Hengyang, Hunan 421001, China.
[Ti] Título:miR-467b regulates the cholesterol ester formation via targeting ACAT1 gene in RAW 264.7 macrophages.
[So] Source:Biochimie;132:38-44, 2017 Jan.
[Is] ISSN:1638-6183
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Previous studies have shown that miR-467b plays a central role in the progression of atherosclerosis via regulating LPL expression. However, the regulatory mechanism of miR-467b in regulateing the CE and FC formation is still unclear. Interestingly, computational analysis demonstrated that ACAT1 which converts intracellular FC into the storage form of CE, and ABCA1 which promotes cellular FC efflux may be target gene of miR-467b. Here, we examined whether miR-467b could target ACAT1 and ABCA1, thereby affecting the CE and FC formation in oxLDL-treatment RAW 264.7 cells. We found that miR-467b regulates the CE:FC ratio in oxLDL-treatment RAW 264.7 macrophages, and the luciferase activity of ACAT1 is regulated by the miR-467b, but the luciferase activity of ABCA1 has no effect. Furthermore, our data suggested that miR-467b highly regulates the endogenous levels of ACAT1 expression, thereby affecting the CE formation in oxLDL-treatment RAW 264.7 macrophages. Taken together, our findings demonstrate that ACAT1 is a target gene of miR-467b, and miR-467b regulated the CE and FC formation via directly target the ACAT1 3'UTR.
[Mh] Termos MeSH primário: Acetil-CoA C-Acetiltransferase/genética
Ésteres do Colesterol/metabolismo
Regulação da Expressão Gênica
Macrófagos/metabolismo
MicroRNAs/genética
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas/genética
Transportador 1 de Cassete de Ligação de ATP/genética
Transportador 1 de Cassete de Ligação de ATP/metabolismo
Acetil-CoA C-Acetiltransferase/metabolismo
Animais
Western Blotting
Linhagem Celular
Colesterol/metabolismo
Lipoproteínas LDL/farmacologia
Macrófagos/efeitos dos fármacos
Camundongos
Interferência de RNA
Reação em Cadeia da Polimerase Via Transcriptase Reversa
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (ABCA1 protein, mouse); 0 (ATP Binding Cassette Transporter 1); 0 (Cholesterol Esters); 0 (Lipoproteins, LDL); 0 (MIRN467 microRNA, mouse); 0 (MicroRNAs); 0 (oxidized low density lipoprotein); 97C5T2UQ7J (Cholesterol); EC 2.3.1.9 (Acat1 protein, mouse); EC 2.3.1.9 (Acetyl-CoA C-Acetyltransferase)
[Em] Mês de entrada:1701
[Cu] Atualização por classe:170130
[Lr] Data última revisão:
170130
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160929
[St] Status:MEDLINE


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[PMID]:27611366
[Au] Autor:Kern RJ; Zarek CM; Lindholm-Perry AK; Kuehn LA; Snelling WM; Freetly HC; Cunningham HC; Meyer AM
[Ad] Endereço:University of Wyoming, Laramie, WY, USA.
[Ti] Título:Ruminal expression of the NQO1, RGS5, and ACAT1 genes may be indicators of feed efficiency in beef steers.
[So] Source:Anim Genet;48(1):90-92, 2017 Feb.
[Is] ISSN:1365-2052
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Ruminal genes differentially expressed in crossbred beef steers from USMARC with variation in gain and feed intake were identified in a previous study. Several of the genes identified with expression patterns differing between animals with high gain-low feed intake and low gain-high feed intake were evaluated in a separate, unrelated population of Angus × Hereford beef steers from the University of Wyoming that was classified to differ in residual feed intake (RFI). Of the 17 genes tested, two were differentially expressed by RFI class in the Angus × Hereford animals. These genes included NAD(P)H dehydrogenase, quinone 1 (NQO1; P = 0.0009) and regulator of G-protein signaling 5 (RGS5; P = 0.01). A third gene, acetyl-CoA acetyltransferase 1 (ACAT1; P = 0.06), displayed a trend toward association with RFI. These data suggest that some of the genes identified in a previous rumen transcriptome discovery study may have utility for identifying or selecting for animals with superior feed efficiency phenotypes across cattle breeds and populations.
[Mh] Termos MeSH primário: Acetil-CoA C-Acetiltransferase/genética
Fenômenos Fisiológicos da Nutrição Animal/genética
NAD(P)H Desidrogenase (Quinona)/genética
Proteínas RGS/genética
Rúmen/metabolismo
[Mh] Termos MeSH secundário: Ração Animal
Animais
Cruzamento
Bovinos
Ingestão de Alimentos/genética
Masculino
Carne Vermelha
Transcriptoma
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RGS Proteins); EC 1.6.5.2 (NAD(P)H Dehydrogenase (Quinone)); EC 2.3.1.9 (Acetyl-CoA C-Acetyltransferase)
[Em] Mês de entrada:1702
[Cu] Atualização por classe:170228
[Lr] Data última revisão:
170228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160910
[St] Status:MEDLINE
[do] DOI:10.1111/age.12490


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[PMID]:28082803
[Au] Autor:Zhang CY; Yuan WG; He P; Lei JH; Wang CX
[Ad] Endereço:Chong-Yang Zhang, Jia-Hui Lei, Department of Pathogenic Biology, School of Basic Medicine, Tongji Medical College, Huazhong University of Science and Technology, Wuhan 430030, Hubei Province, China.
[Ti] Título:Liver fibrosis and hepatic stellate cells: Etiology, pathological hallmarks and therapeutic targets.
[So] Source:World J Gastroenterol;22(48):10512-10522, 2016 Dec 28.
[Is] ISSN:2219-2840
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Liver fibrosis is a reversible wound-healing process aimed at maintaining organ integrity, and presents as the critical pre-stage of liver cirrhosis, which will eventually progress to hepatocellular carcinoma in the absence of liver transplantation. Fibrosis generally results from chronic hepatic injury caused by various factors, mainly viral infection, schistosomiasis, and alcoholism; however, the exact pathological mechanisms are still unknown. Although numerous drugs have been shown to have antifibrotic activity and in animal models, none of these drugs have been shown to be efficacious in the clinic. Importantly, hepatic stellate cells (HSCs) play a key role in the initiation, progression, and regression of liver fibrosis by secreting fibrogenic factors that encourage portal fibrocytes, fibroblasts, and bone marrow-derived myofibroblasts to produce collagen and thereby propagate fibrosis. These cells are subject to intricate cross-talk with adjacent cells, resulting in scarring and subsequent liver damage. Thus, an understanding of the molecular mechanisms of liver fibrosis and their relationships with HSCs is essential for the discovery of new therapeutic targets. This comprehensive review outlines the role of HSCs in liver fibrosis and details novel strategies to suppress HSC activity, thereby providing new insights into potential treatments for liver fibrosis.
[Mh] Termos MeSH primário: Células Estreladas do Fígado/efeitos dos fármacos
Células Estreladas do Fígado/patologia
Cirrose Hepática/tratamento farmacológico
Cirrose Hepática/etiologia
Terapia de Alvo Molecular/métodos
[Mh] Termos MeSH secundário: Acetil-CoA C-Acetiltransferase/metabolismo
Animais
Linfócitos T CD4-Positivos/metabolismo
Progressão da Doença
Fígado Gorduroso Alcoólico/complicações
Seres Humanos
Interleucinas/metabolismo
Peptídeos e Proteínas de Sinalização Intracelular/metabolismo
Proteínas com Domínio LIM/metabolismo
Cirrose Hepática/patologia
Macrófagos/metabolismo
MicroRNAs/metabolismo
Hepatopatia Gordurosa não Alcoólica/complicações
Esquistossomose/complicações
Transdução de Sinais
Estilbenos/uso terapêutico
Linfócitos T Reguladores/metabolismo
Triterpenos/uso terapêutico
Ácido Ursodesoxicólico/análogos & derivados
Ácido Ursodesoxicólico/uso terapêutico
Viroses/complicações
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (IL27 protein, human); 0 (Interleukins); 0 (Intracellular Signaling Peptides and Proteins); 0 (LIM Domain Proteins); 0 (MicroRNAs); 0 (Stilbenes); 0 (TGFB1I1 protein, human); 0 (Triterpenes); 724L30Y2QR (Ursodeoxycholic Acid); 99697-24-2 (24-norursodeoxycholic acid); EC 2.3.1.9 (ACAT1 protein, human); EC 2.3.1.9 (Acetyl-CoA C-Acetyltransferase); P3M2575F3F (ursolic acid); Q369O8926L (resveratrol)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170606
[Lr] Data última revisão:
170606
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170114
[St] Status:MEDLINE
[do] DOI:10.3748/wjg.v22.i48.10512


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[PMID]:27912096
[Au] Autor:Garcia-Bermudez J; Birsoy K
[Ad] Endereço:Laboratory of Metabolic Regulation and Genetics, The Rockefeller University, 1230 York Avenue, New York, NY 10065, USA.
[Ti] Título:Drugging ACAT1 for Cancer Therapy.
[So] Source:Mol Cell;64(5):856-857, 2016 Dec 01.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:In this issue, Fan et al. (2016) show that oncogenic tyrosine kinases can promote glycolysis by phosphorylating and stabilizing the tetrameric form of mitochondrial acetyl-coA acetyltransferase 1 (ACAT1). The authors further identify a small molecule ACAT1 inhibitor that displays anti-cancer effects.
[Mh] Termos MeSH primário: Acetil-CoA C-Acetiltransferase
Proteínas Tirosina Quinases
[Mh] Termos MeSH secundário: Glicólise
Seres Humanos
Mitocôndrias
Neoplasias
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 2.3.1.9 (Acetyl-CoA C-Acetyltransferase); EC 2.7.10.1 (Protein-Tyrosine Kinases)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171026
[Lr] Data última revisão:
171026
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161203
[St] Status: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]:27867011
[Au] Autor:Fan J; Lin R; Xia S; Chen D; Elf SE; Liu S; Pan Y; Xu H; Qian Z; Wang M; Shan C; Zhou L; Lei QY; Li Y; Mao H; Lee BH; Sudderth J; DeBerardinis RJ; Zhang G; Owonikoko T; Gaddh M; Arellano ML; Khoury HJ; Khuri FR; Kang S; Doetsch PW; Lonial S; Boggon TJ; Curran WJ; Chen J
[Ad] Endereço:Department of Radiation Oncology, Emory University School of Medicine, Atlanta, GA 30322, USA; Winship Cancer Institute, Emory University School of Medicine, Atlanta, GA 30322, USA. Electronic address: jfan3@emory.edu.
[Ti] Título:Tetrameric Acetyl-CoA Acetyltransferase 1 Is Important for Tumor Growth.
[So] Source:Mol Cell;64(5):859-874, 2016 Dec 01.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mitochondrial acetyl-CoA acetyltransferase 1 (ACAT1) regulates pyruvate dehydrogenase complex (PDC) by acetylating pyruvate dehydrogenase (PDH) and PDH phosphatase. How ACAT1 is "hijacked" to contribute to the Warburg effect in human cancer remains unclear. We found that active, tetrameric ACAT1 is commonly upregulated in cells stimulated by EGF and in diverse human cancer cells, where ACAT1 tetramers, but not monomers, are phosphorylated and stabilized by enhanced Y407 phosphorylation. Moreover, we identified arecoline hydrobromide (AH) as a covalent ACAT1 inhibitor that binds to and disrupts only ACAT1 tetramers. The resultant AH-bound ACAT1 monomers cannot reform tetramers. Inhibition of tetrameric ACAT1 by abolishing Y407 phosphorylation or AH treatment results in decreased ACAT1 activity, leading to increased PDC flux and oxidative phosphorylation with attenuated cancer cell proliferation and tumor growth. These findings provide a mechanistic understanding of how oncogenic events signal through distinct acetyltransferases to regulate cancer metabolism and suggest ACAT1 as an anti-cancer target.
[Mh] Termos MeSH primário: Acetil-CoA C-Acetiltransferase/metabolismo
Mitocôndrias/enzimologia
Complexo Piruvato Desidrogenase/metabolismo
[Mh] Termos MeSH secundário: Acetil-CoA C-Acetiltransferase/genética
Animais
Linhagem Celular Tumoral
Proliferação Celular
Fator de Crescimento Epidérmico/metabolismo
Regulação Enzimológica da Expressão Gênica
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Camundongos
Camundongos Nus
Células NIH 3T3
Neoplasias/enzimologia
Neoplasias/patologia
Oligopeptídeos/genética
Oligopeptídeos/metabolismo
Fosforilação
Proteínas Tirosina Quinases/metabolismo
Receptor Tipo 1 de Fator de Crescimento de Fibroblastos/genética
Receptor Tipo 1 de Fator de Crescimento de Fibroblastos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Oligopeptides); 0 (Pyruvate Dehydrogenase Complex); 62229-50-9 (Epidermal Growth Factor); 98849-88-8 (FLAG peptide); EC 2.3.1.9 (ACAT1 protein, human); EC 2.3.1.9 (Acetyl-CoA C-Acetyltransferase); EC 2.7.10.1 (FGFR1 protein, human); EC 2.7.10.1 (Protein-Tyrosine Kinases); EC 2.7.10.1 (Receptor, Fibroblast Growth Factor, Type 1)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170904
[Lr] Data última revisão:
170904
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161122
[St] Status:MEDLINE



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