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Pesquisa : D08.811.464.267.500.200 [Categoria DeCS]
Referências encontradas : 478 [refinar]
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[PMID]:29281714
[Au] Autor:Chen R; Xu M; Nagati J; Garcia JA
[Ad] Endereço:Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, Texas, United States of America.
[Ti] Título:Coordinate regulation of stress signaling and epigenetic events by Acss2 and HIF-2 in cancer cells.
[So] Source:PLoS One;12(12):e0190241, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Survival of cancer cells in the harsh tumor microenvironment, characterized by oxygen and glucose deprivation, requires rapid initiation of cytoprotective measures. Metabolites whose levels change during stress are ideal signaling cues, particularly if used in post-translational modifications of stress-responsive signal transducers. In cancer cells exposed to oxygen or glucose deprivation, there is an increase in cellular levels of acetate, a substrate for acetate-dependent acetyl CoA synthetase 2 (Acss2) that also stimulates translocation of Acss2 from the cytosol to the nucleus. Nuclear, but not cytosolic, Acss2 promotes acetylation of the stress-responsive Hypoxia Inducible Factor 2α (HIF-2α) subunit by the acetyltransferase/coactivator Creb binding protein (Cbp), a process that facilitates stable Cbp/HIF-2α complex formation. In addition to promoting de novo transcription, Cbp and HIF-2α act in concert to regulate local histone 3 epigenetic marks. Exogenous acetate augments Acss2/HIF-2 dependent cancer growth and metastasis in cell culture and mouse models. Thus, an acetate switch in mammals links nutrient intake and stress signaling with tumor growth and metastasis.
[Mh] Termos MeSH primário: Acetato-CoA Ligase/metabolismo
Fatores de Transcrição Hélice-Alça-Hélice Básicos/metabolismo
Epigênese Genética
Neoplasias/metabolismo
Estresse Oxidativo
Transdução de Sinais
[Mh] Termos MeSH secundário: Acetilcoenzima A/metabolismo
Animais
Fatores de Transcrição Hélice-Alça-Hélice Básicos/química
Linhagem Celular Tumoral
Células HEK293
Seres Humanos
Lisina/metabolismo
Camundongos
Camundongos Nus
Neoplasias/genética
Neoplasias/patologia
Reação em Cadeia da Polimerase em Tempo Real
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.
[Nm] Nome de substância:
0 (Basic Helix-Loop-Helix Transcription Factors); 0 (endothelial PAS domain-containing protein 1); 72-89-9 (Acetyl Coenzyme A); EC 6.2.1.1 (ACSS2 protein, human); EC 6.2.1.1 (Acetate-CoA Ligase); K3Z4F929H6 (Lysine)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180206
[Lr] Data última revisão:
180206
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171228
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190241


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[PMID]:28407230
[Au] Autor:Xu H; Luo J; Ma G; Zhang X; Yao D; Li M; Loor JJ
[Ad] Endereço:Shaanxi Key Laboratory of Molecular Biology for Agriculture, College of Animal Science and Technology, Northwest A&F University, Yangling, Shaanxi, P. R. China.
[Ti] Título:Acyl-CoA synthetase short-chain family member 2 (ACSS2) is regulated by SREBP-1 and plays a role in fatty acid synthesis in caprine mammary epithelial cells.
[So] Source:J Cell Physiol;233(2):1005-1016, 2018 Feb.
[Is] ISSN:1097-4652
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Sterol regulatory element binding protein 1 (SREBP-1) is well-known as the master regulator of lipogenesis in rodents. Acyl-CoA synthetase short-chain family member 2 (ACSS2) plays a key role in lipogenesis by synthesizing acetyl-CoA from acetate for lipogenesis. ATP citrate lyase (ACLY) catalyzes the conversion of citrate and coenzyme A to acetyl-CoA, hence, it is also important for lipogenesis. Although ACSS2 function in cancer cells has been elucidated, its essentiality in ruminant mammary lipogenesis is unknown. Furthermore, ACSS2 gene promoter and its regulatory mechanisms have not known. Expression of ACSS2 was high in lipid synthesizing tissues, and its expression increased during lactation compared with non-lactating period. Simultaneous knockdown of both ACSS2 and ACLY by siRNA in primary goat mammary epithelial cells decreased (p < 0.05) the mRNA abundance of genes associated with de novo fatty acid synthesis (FASN, ACACA, SCD1) and triacylglycerol (TAG) synthesis (DGAT1, DGAT2, GPAM, and AGPAT6). Genes responsible for lipid droplet formation and secretion (PLIN2 and PLIN3) and fatty acid oxidation (ATGL, HSL, ACOX, and CPT1A) all decreased (p < 0.05) after ACSS2 and ACLY knockdown. Total cellular TAG content and lipid droplet formation also decreased. Use of a luciferase reporter assay revealed a direct regulation of ACSS2 by SREBP-1. Furthermore, SREBP-1 interacted with an SRE (SREBP response element) spanning at -475 to -483 bp on the ACSS2 promoter. Taken together, our results revealed a novel pathway that SREBP-1 may regulate fatty acid and TAG synthesis by regulating the expression of ACSS2.
[Mh] Termos MeSH primário: Acetato-CoA Ligase/metabolismo
Células Epiteliais/enzimologia
Ácidos Graxos/biossíntese
Lactação
Glândulas Mamárias Animais/enzimologia
Proteína de Ligação a Elemento Regulador de Esterol 1/metabolismo
[Mh] Termos MeSH secundário: ATP Citrato (pro-S)-Liase/genética
ATP Citrato (pro-S)-Liase/metabolismo
Acetato-CoA Ligase/genética
Animais
Células Cultivadas
Feminino
Regulação Enzimológica da Expressão Gênica
Cabras
Gotículas Lipídicas/metabolismo
Lipogênese/genética
Glândulas Mamárias Animais/citologia
Mutagênese Sítio-Dirigida
Mutação
Regiões Promotoras Genéticas
Interferência de RNA
Elemento de Resposta Sérica
Proteína de Ligação a Elemento Regulador de Esterol 1/genética
Transfecção
Triglicerídeos/biossíntese
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fatty Acids); 0 (Sterol Regulatory Element Binding Protein 1); 0 (Triglycerides); EC 2.3.3.8 (ATP Citrate (pro-S)-Lyase); EC 6.2.1.1 (Acetate-CoA Ligase)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171128
[Lr] Data última revisão:
171128
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170414
[St] Status:MEDLINE
[do] DOI:10.1002/jcp.25954


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[PMID]:28562591
[Au] Autor:Mews P; Donahue G; Drake AM; Luczak V; Abel T; Berger SL
[Ad] Endereço:Epigenetics Institute, Departments of Cell and Developmental Biology, Biology, Genetics, University of Pennsylvania Perelman School of Medicine, Philadelphia, Pennsylvania 19104, USA.
[Ti] Título:Acetyl-CoA synthetase regulates histone acetylation and hippocampal memory.
[So] Source:Nature;546(7658):381-386, 2017 06 15.
[Is] ISSN:1476-4687
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Metabolic production of acetyl coenzyme A (acetyl-CoA) is linked to histone acetylation and gene regulation, but the precise mechanisms of this process are largely unknown. Here we show that the metabolic enzyme acetyl-CoA synthetase 2 (ACSS2) directly regulates histone acetylation in neurons and spatial memory in mammals. In a neuronal cell culture model, ACSS2 increases in the nuclei of differentiating neurons and localizes to upregulated neuronal genes near sites of elevated histone acetylation. A decrease in ACSS2 lowers nuclear acetyl-CoA levels, histone acetylation, and responsive expression of the cohort of neuronal genes. In adult mice, attenuation of hippocampal ACSS2 expression impairs long-term spatial memory, a cognitive process that relies on histone acetylation. A decrease in ACSS2 in the hippocampus also leads to defective upregulation of memory-related neuronal genes that are pre-bound by ACSS2. These results reveal a connection between cellular metabolism, gene regulation, and neural plasticity and establish a link between acetyl-CoA generation 'on-site' at chromatin for histone acetylation and the transcription of key neuronal genes.
[Mh] Termos MeSH primário: Acetato-CoA Ligase/metabolismo
Hipocampo/enzimologia
Hipocampo/fisiologia
Histonas/metabolismo
Memória/fisiologia
Plasticidade Neuronal/genética
Ativação Transcricional
[Mh] Termos MeSH secundário: Acetato-CoA Ligase/deficiência
Acetato-CoA Ligase/genética
Acetilcoenzima A/metabolismo
Acetilação
Animais
Diferenciação Celular
Núcleo Celular/metabolismo
Células Cultivadas
Cromatina/enzimologia
Cromatina/genética
Cromatina/metabolismo
Regulação Enzimológica da Expressão Gênica
Hipocampo/metabolismo
Histonas/química
Consolidação da Memória/fisiologia
Camundongos
Plasticidade Neuronal/fisiologia
Neurônios/citologia
Neurônios/metabolismo
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Chromatin); 0 (Histones); 72-89-9 (Acetyl Coenzyme A); EC 6.2.1.1 (ACSS2 protein, mouse); EC 6.2.1.1 (Acetate-CoA Ligase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170601
[St] Status:MEDLINE
[do] DOI:10.1038/nature22405


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[PMID]:28552616
[Au] Autor:Li X; Yu W; Qian X; Xia Y; Zheng Y; Lee JH; Li W; Lyu J; Rao G; Zhang X; Qian CN; Rozen SG; Jiang T; Lu Z
[Ad] Endereço:Brain Tumor Center, Department of Neuro-Oncology, The University of Texas MD Anderson Cancer Center, Houston, TX 77030, USA.
[Ti] Título:Nucleus-Translocated ACSS2 Promotes Gene Transcription for Lysosomal Biogenesis and Autophagy.
[So] Source:Mol Cell;66(5):684-697.e9, 2017 Jun 01.
[Is] ISSN:1097-4164
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Overcoming metabolic stress is a critical step in tumor growth. Acetyl coenzyme A (acetyl-CoA) generated from glucose and acetate uptake is important for histone acetylation and gene expression. However, how acetyl-CoA is produced under nutritional stress is unclear. We demonstrate here that glucose deprivation results in AMP-activated protein kinase (AMPK)-mediated acetyl-CoA synthetase 2 (ACSS2) phosphorylation at S659, which exposed the nuclear localization signal of ACSS2 for importin α5 binding and nuclear translocation. In the nucleus, ACSS2 binds to transcription factor EB and translocates to lysosomal and autophagy gene promoter regions, where ACSS2 incorporates acetate generated from histone acetylation turnover to locally produce acetyl-CoA for histone H3 acetylation in these regions and promote lysosomal biogenesis, autophagy, cell survival, and brain tumorigenesis. In addition, ACSS2 S659 phosphorylation positively correlates with AMPK activity in glioma specimens and grades of glioma malignancy. These results underscore the significance of nuclear ACSS2-mediated histone acetylation in maintaining cell homeostasis and tumor development.
[Mh] Termos MeSH primário: Acetato-CoA Ligase/metabolismo
Autofagia
Neoplasias Encefálicas/enzimologia
Núcleo Celular/enzimologia
Glioblastoma/enzimologia
Histonas/metabolismo
Lisossomos/metabolismo
Biogênese de Organelas
Transcrição Genética
[Mh] Termos MeSH secundário: Proteínas Quinases Ativadas por AMP/metabolismo
Acetato-CoA Ligase/genética
Acetilcoenzima A/metabolismo
Acetilação
Transporte Ativo do Núcleo Celular
Animais
Fatores de Transcrição de Zíper de Leucina e Hélice-Alça-Hélix Básicos/genética
Fatores de Transcrição de Zíper de Leucina e Hélice-Alça-Hélix Básicos/metabolismo
Sítios de Ligação
Neoplasias Encefálicas/genética
Neoplasias Encefálicas/patologia
Linhagem Celular Tumoral
Núcleo Celular/patologia
Sobrevivência Celular
Metabolismo Energético
Regulação Neoplásica da Expressão Gênica
Glioblastoma/genética
Glioblastoma/patologia
Seres Humanos
Masculino
Camundongos Endogâmicos BALB C
Camundongos Nus
Fosforilação
Regiões Promotoras Genéticas
Ligação Proteica
Processamento de Proteína Pós-Traducional
Interferência de RNA
Estresse Fisiológico
Transfecção
alfa Carioferinas/genética
alfa Carioferinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Basic Helix-Loop-Helix Leucine Zipper Transcription Factors); 0 (Histones); 0 (KPNA1 protein, human); 0 (TFEB protein, human); 0 (alpha Karyopherins); 72-89-9 (Acetyl Coenzyme A); EC 2.7.11.31 (AMP-Activated Protein Kinases); EC 6.2.1.1 (ACSS2 protein, human); EC 6.2.1.1 (Acetate-CoA Ligase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170530
[St] Status:MEDLINE


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[PMID]:28543373
[Au] Autor:Dodhia S; Celis K; Aylward A; Cai Y; Fontana ME; Trespalacios A; Hoffman DC; Alfonso HO; Eisig SB; Su GH; Chung WK; Haddad J
[Ad] Endereço:Department of Otolaryngology-Head and Neck Surgery, Columbia University Medical Center, New York, New York, U.S.A.
[Ti] Título:ACSS2 gene variant associated with cleft lip and palate in two independent Hispanic populations.
[So] Source:Laryngoscope;127(10):E336-E339, 2017 Oct.
[Is] ISSN:1531-4995
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:OBJECTIVES/HYPOTHESIS: A candidate variant (p.Val496Ala) of the ACSS2 gene (T > C missense, rs59088485 variant at chr20: bp37 33509608) was previously found to consistently segregate with nonsyndromic cleft lip and/or palate (NSCLP) in three Honduran families. Objectives of this study were 1) to investigate the frequency of this ACSS2 variant in Honduran unrelated NSCLP patients and unrelated unaffected controls and 2) to investigate the frequency of this variant in Colombian unrelated affected NSCLP patients and unrelated unaffected controls. STUDY DESIGN: Case-control studies. METHODS: Sanger sequencing of 99 unrelated Honduran NSCLP patients and 215 unrelated unaffected controls for the p.Val496Ala ACSS2 variant was used to determine the carrier frequency in NSCLP patients and controls. Sanger sequencing of 230 unrelated Colombian NSCLP patients and 146 unrelated unaffected controls for the p.Val496Ala ACSS2 variant was used to determine the carrier frequency in NSCLP patients and controls. RESULTS: In the Honduran population, the odds ratio of having NSCLP among carriers of the p.Val496Ala ACSS2 variant was 4.0 (P = .03), with a carrier frequency of seven of 99 (7.1%) in unrelated affected and four of 215 (1.9%) in unrelated unaffected individuals. In the Colombian population, the odds ratio of having NSCLP among carriers of the p.Val496Ala ACSS2 variant was 2.6 (P = .04), with a carrier frequency of 23 of 230 (10.0%) in unrelated affected and six of 146 (4.1%) in unrelated unaffected individuals. CONCLUSIONS: These findings support the role of ACSS2 in NSCLP in two independent Hispanic populations from Honduras and Colombia. LEVEL OF EVIDENCE: NA Laryngoscope, 127:E336-E339, 2017.
[Mh] Termos MeSH primário: Acetato-CoA Ligase/genética
Encéfalo/anormalidades
Fenda Labial/genética
Fissura Palatina/genética
[Mh] Termos MeSH secundário: Acetato-CoA Ligase/sangue
Estudos de Casos e Controles
Pré-Escolar
Fenda Labial/sangue
Fissura Palatina/sangue
Colômbia
Feminino
Frequência do Gene
Estudos de Associação Genética
Predisposição Genética para Doença
Honduras
Seres Humanos
Masculino
Razão de Chances
Polimorfismo de Nucleotídeo Único
Análise de Sequência de DNA/métodos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 6.2.1.1 (ACSS2 protein, human); EC 6.2.1.1 (Acetate-CoA Ligase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170929
[Lr] Data última revisão:
170929
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.1002/lary.26637


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[PMID]:28542616
[Au] Autor:Jacob K; Rasmussen A; Tyler P; Servos MM; Sylla M; Prado C; Daniele E; Sharp JS; Purdy AE
[Ad] Endereço:Department of Biology, Northern Michigan University, Marquette, Michigan, United States of America.
[Ti] Título:Regulation of acetyl-CoA synthetase transcription by the CrbS/R two-component system is conserved in genetically diverse environmental pathogens.
[So] Source:PLoS One;12(5):e0177825, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The CrbS/R two-component signal transduction system is a conserved regulatory mechanism through which specific Gram-negative bacteria control acetate flux into primary metabolic pathways. CrbS/R governs expression of acetyl-CoA synthase (acsA), an enzyme that converts acetate to acetyl-CoA, a metabolite at the nexus of the cell's most important energy-harvesting and biosynthetic reactions. During infection, bacteria can utilize this system to hijack host acetate metabolism and alter the course of colonization and pathogenesis. In toxigenic strains of Vibrio cholerae, CrbS/R-dependent expression of acsA is required for virulence in an arthropod model. Here, we investigate the function of the CrbS/R system in Pseudomonas aeruginosa, Pseudomonas entomophila, and non-toxigenic V. cholerae strains. We demonstrate that its role in acetate metabolism is conserved; this system regulates expression of the acsA gene and is required for growth on acetate as a sole carbon source. As a first step towards describing the mechanism of signaling through this pathway, we identify residues and domains that may be critical for phosphotransfer. We further demonstrate that although CrbS, the putative hybrid sensor kinase, carries both a histidine kinase domain and a receiver domain, the latter is not required for acsA transcription. In order to determine whether our findings are relevant to pathogenesis, we tested our strains in a Drosophila model of oral infection previously employed for the study of acetate-dependent virulence by V. cholerae. We show that non-toxigenic V. cholerae strains lacking CrbS or CrbR are significantly less virulent than are wild-type strains, while P. aeruginosa and P. entomophila lacking CrbS or CrbR are fully pathogenic. Together, the data suggest that the CrbS/R system plays a central role in acetate metabolism in V. cholerae, P. aeruginosa, and P. entomophila. However, each microbe's unique environmental adaptations and pathogenesis strategies may dictate conditions under which CrbS/R-mediated acs expression is most critical.
[Mh] Termos MeSH primário: Acetato-CoA Ligase/genética
Proteínas de Bactérias/metabolismo
Meio Ambiente
Variação Genética
Transcrição Genética
[Mh] Termos MeSH secundário: Acetatos/metabolismo
Animais
Proteínas de Bactérias/química
Proteínas de Bactérias/genética
Sequência Conservada
Regulação Bacteriana da Expressão Gênica
Proteínas Hemolisinas/metabolismo
Domínios Proteicos
Pseudomonas aeruginosa/citologia
Pseudomonas aeruginosa/genética
Pseudomonas aeruginosa/metabolismo
Pseudomonas aeruginosa/patogenicidade
Deleção de Sequência
Homologia de Sequência do Ácido Nucleico
Transdução de Sinais
Vibrio cholerae/citologia
Vibrio cholerae/genética
Vibrio cholerae/metabolismo
Vibrio cholerae/patogenicidade
Virulência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acetates); 0 (Bacterial Proteins); 0 (Hemolysin Proteins); EC 6.2.1.1 (Acetate-CoA Ligase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170912
[Lr] Data última revisão:
170912
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0177825


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[PMID]:28431246
[Au] Autor:Tang H; Han M
[Ad] Endereço:Howard Hughes Medical Institute and Department of MCDB of the University of Colorado at Boulder, Boulder, CO 80309, USA.
[Ti] Título:Fatty Acids Regulate Germline Sex Determination through ACS-4-Dependent Myristoylation.
[So] Source:Cell;169(3):457-469.e13, 2017 Apr 20.
[Is] ISSN:1097-4172
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Fat metabolism has been linked to fertility and reproductive adaptation in animals and humans, and environmental sex determination potentially plays a role in the process. To investigate the impact of fatty acids (FA) on sex determination and reproductive development, we examined and observed an impact of FA synthesis and mobilization by lipolysis in somatic tissues on oocyte fate in Caenorhabditis elegans. The subsequent genetic analysis identified ACS-4, an acyl-CoA synthetase and its FA-CoA product, as key germline factors that mediate the role of FA in promoting oocyte fate through protein myristoylation. Further tests indicated that ACS-4-dependent protein myristoylation perceives and translates the FA level into regulatory cues that modulate the activities of MPK-1/MAPK and key factors in the germline sex-determination pathway. These findings, including a similar role of ACS-4 in a male/female species, uncover a likely conserved mechanism by which FA, an environmental factor, regulates sex determination and reproductive development.
[Mh] Termos MeSH primário: Acetato-CoA Ligase/metabolismo
Proteínas de Caenorhabditis elegans/metabolismo
Caenorhabditis elegans/fisiologia
Ácidos Graxos/metabolismo
Ácido Mirístico/metabolismo
Processamento de Proteína Pós-Traducional
Processos de Determinação Sexual
[Mh] Termos MeSH secundário: Acetato-CoA Ligase/genética
Animais
Proteínas de Caenorhabditis elegans/genética
Mutação
Oócitos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caenorhabditis elegans Proteins); 0 (Fatty Acids); 0I3V7S25AW (Myristic Acid); EC 6.2.1.1 (Acetate-CoA Ligase)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170623
[Lr] Data última revisão:
170623
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170422
[St] Status:MEDLINE


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[PMID]:28387999
[Au] Autor:Sun L; Kong Y; Cao M; Zhou H; Li H; Cui Y; Fang F; Zhang W; Li J; Zhu X; Li Q; Song T; Zhang T
[Ad] Endereço:Tianjin Medical University Cancer Institute and Hospital, National Clinical Research Center for Cancer, Key Laboratory of Cancer Prevention and Therapy, Tianjin's Clinical Research Center for Cancer, Tianjin, China.
[Ti] Título:Decreased expression of acetyl-CoA synthase 2 promotes metastasis and predicts poor prognosis in hepatocellular carcinoma.
[So] Source:Cancer Sci;108(7):1338-1346, 2017 Jul.
[Is] ISSN:1349-7006
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Metastasis is a serious risk that may occur during the treatment of hepatocellular carcinoma (HCC), preventing many patients from being surgical candidates and contributing to poor prognosis. Hypoxia has been proved an important factor of metastasis through the epithelial-mesenchymal transition (EMT) pathway. Acetyl-CoA synthase 2 (ACSS2) provides an acetyl group for the acetylation of hypoxia-inducible factor (HIF)-2α, and this epigenetic modification affects the activity of HIF-2α and the subsequent EMT process. Here, we showed that ACSS2 expression was negatively correlated with HCC malignancy. Knockdown of ACSS2 increased the invasion and migration ability of HCC cells and promoted EMT without increasing the total protein level of HIF-2α, even in hypoxic conditions. The immunoprecipitation assay revealed downregulated acetylation levels of HIF-2α after ACSS2 knockdown in hypoxic conditions, which resulted in enhanced HIF-2α activity. Finally, decreased expression of ACSS2 was found to be related to advanced stage and poor overall survival and disease-free survival rates in a cohort of patients with HCC. In conclusion, ACSS2 plays an important role in the acetylation process of HIF-2α, which effectively modifies the activity of HIF-2α under hypoxic conditions and greatly impacts on the prognosis of patients with HCC.
[Mh] Termos MeSH primário: Acetato-CoA Ligase/metabolismo
Fatores de Transcrição Hélice-Alça-Hélice Básicos/metabolismo
Carcinoma Hepatocelular/patologia
Neoplasias Hepáticas/patologia
[Mh] Termos MeSH secundário: Acetilação
Western Blotting
Carcinoma Hepatocelular/mortalidade
Intervalo Livre de Doença
Transição Epitelial-Mesenquimal/fisiologia
Feminino
Seres Humanos
Imuno-Histoquímica
Imunoprecipitação
Estimativa de Kaplan-Meier
Neoplasias Hepáticas/mortalidade
Masculino
Meia-Idade
Invasividade Neoplásica/patologia
Prognóstico
Reação em Cadeia da Polimerase em Tempo Real
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Basic Helix-Loop-Helix Transcription Factors); 0 (endothelial PAS domain-containing protein 1); EC 6.2.1.1 (ACSS2 protein, human); EC 6.2.1.1 (Acetate-CoA Ligase)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170408
[St] Status:MEDLINE
[do] DOI:10.1111/cas.13252


  9 / 478 MEDLINE  
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[PMID]:28178309
[Au] Autor:Schrapers P; Ilina J; Gregg CM; Mebs S; Jeoung JH; Dau H; Dobbek H; Haumann M
[Ad] Endereço:Department of Physics, Freie Universität Berlin, Berlin, Germany.
[Ti] Título:Ligand binding at the A-cluster in full-length or truncated acetyl-CoA synthase studied by X-ray absorption spectroscopy.
[So] Source:PLoS One;12(2):e0171039, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Bacteria integrate CO2 reduction and acetyl coenzyme-A (CoA) synthesis in the Wood-Ljungdal pathway. The acetyl-CoA synthase (ACS) active site is a [4Fe4S]-[NiNi] complex (A-cluster). The dinickel site structure (with proximal, p, and distal, d, ions) was studied by X-ray absorption spectroscopy in ACS variants comprising all three protein domains or only the C-terminal domain with the A-cluster. Both variants showed two square-planar Ni(II) sites and an OH- bound at Ni(II)p in oxidized enzyme and a H2O at Ni(I)p in reduced enzyme; a Ni(I)p-CO species was induced by CO incubation and a Ni(II)-CH3- species with an additional water ligand by a methyl group donor. These findings render a direct effect of the N-terminal and middle domains on the A-cluster structure unlikely.
[Mh] Termos MeSH primário: Acetato-CoA Ligase/química
Ligantes
Espectroscopia por Absorção de Raios X
[Mh] Termos MeSH secundário: Acetato-CoA Ligase/genética
Acetato-CoA Ligase/metabolismo
Domínio Catalítico
Metais/química
Metais/metabolismo
Modelos Moleculares
Conformação Molecular
Mutação
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ligands); 0 (Metals); EC 6.2.1.1 (Acetate-CoA Ligase)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170209
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0171039


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[PMID]:27987242
[Au] Autor:You D; Wang MM; Ye BC
[Ad] Endereço:Lab of Biosystems and Microanalysis, State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, Meilong RD 130, Shanghai, 200237, China.
[Ti] Título:Acetyl-CoA synthetases of Saccharopolyspora erythraea are regulated by the nitrogen response regulator GlnR at both transcriptional and post-translational levels.
[So] Source:Mol Microbiol;103(5):845-859, 2017 Mar.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Saccharopolyspora erythraea has three AMP-forming acetyl-CoA synthetases (Acs) encoded by acsA1, acsA2, and acsA3. In this work, we found that nitrogen response regulator GlnR can directly interact with the promoter regions of all three genes and can activate their transcription in response to nitrogen availability. The typical GlnR-binding boxes were identified in the promoter regions. Moreover, the activities of three Acs enzymes were modulated by the reversible lysine acetylation (RLA) with acetyltransferase AcuA and NAD -dependent deacetylase SrtN. Interestingly, GlnR controlled the RLA by directly activating the expression of acuA and srtN. A glnR-deleted mutant (ΔglnR) caused a growth defect in 10 mM acetate minimal medium, a condition under which RLA function is critical to control Acs activity. Overexpression of acuA reversed the growth defect of ΔglnR mutant. Total activity of Acs in cell-free extracts from ΔglnR strain had a 4-fold increase relative to that of wildtype strain. Western Blotting showed that in vivo acetylation levels of Acs were influenced by nitrogen availability and lack of glnR. These results demonstrated that GlnR regulated acetyl-CoA synthetases at transcriptional and post-translational levels, and mediated the interplay between nitrogen and carbon metabolisms by integrating nitrogen signals to modulate the acetate metabolism.
[Mh] Termos MeSH primário: Acetato-CoA Ligase/genética
Aminoacil-tRNA Sintetases/genética
Regulação Bacteriana da Expressão Gênica
Nitrogênio/metabolismo
Processamento de Proteína Pós-Traducional
Saccharopolyspora/enzimologia
Transcrição Genética
[Mh] Termos MeSH secundário: Acetato-CoA Ligase/metabolismo
Acetilação
Aminoacil-tRNA Sintetases/metabolismo
Proteínas de Bactérias/metabolismo
Carbono/metabolismo
Lisina/metabolismo
Saccharopolyspora/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Bacterial Proteins); 7440-44-0 (Carbon); EC 6.1.1.- (Amino Acyl-tRNA Synthetases); EC 6.1.1.18 (glutaminyl-tRNA synthetase); EC 6.2.1.1 (Acetate-CoA Ligase); K3Z4F929H6 (Lysine); N762921K75 (Nitrogen)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170828
[Lr] Data última revisão:
170828
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161218
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.13595



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