Base de dados : MEDLINE
Pesquisa : G02.111.570.080.689.330.240 [Categoria DeCS]
Referências encontradas : 398 [refinar]
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[PMID]:29307818
[Au] Autor:Wei D; Feng L; Zhang W; Ma X; Cheng G; Li S; Wang L; Zhang S; Hong J; Guo H; Wang Y; Ning Y; Zan L
[Ad] Endereço:College of Animal Science and Technology, Northwest A&F University, Yangling, Shaanxi, 712100, China.
[Ti] Título:Characterization of the promoter region of bovine SIX4: Roles of E-box and MyoD in the regulation of basal transcription.
[So] Source:Biochem Biophys Res Commun;496(1):44-50, 2018 01 29.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The sine oculis homeobox 4 (SIX4) gene belongs to the Six gene family and encodes an evolutionarily conserved transcription factor. Previous studies have demonstrated that SIX4 plays an essential role in proper muscle regeneration. However, the mechanisms regulating SIX4 transcription remain elusive. In the present study, we determined that bovine SIX4 was highly expressed in the longissimus thoracis and in undifferentiated Qinchuan cattle muscle cells (QCMCs) and that its protein localizes to both the cytoplasm and the nucleus. To elucidate the bovine the molecular mechanisms of SIX4 regulation, 1.3 kb of the 5'-regulatory region was obtained. MyoD and Ebox recognition sites were identified in the core promoter region at -522/-193 of the bovine SIX4 using a series of 5' deletion promoter plasmids in luciferase reporter assays. An electrophoretic mobility shift assay (EMSA) and chromatin immunoprecipitation (ChIP) assay in combination with site-directed mutation and siRNA interference demonstrated that MyoD binding occurs at MyoD and Ebox recognition sites through direct and indirect mechanisms and play important roles in the transcriptional regulation of the bovine SIX4 promoter. Taken together, these interactions provide insight into the regulatory mechanisms of SIX4 transcription in mediating skeletal muscle growth in cattle.
[Mh] Termos MeSH primário: Bovinos/genética
Elementos E-Box/genética
Proteínas de Homeodomínio/genética
Proteína MyoD/genética
Regiões Promotoras Genéticas/genética
Elementos Reguladores de Transcrição/genética
Ativação Transcricional/genética
[Mh] Termos MeSH secundário: Animais
Regulação da Expressão Gênica/genética
Transativadores/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Homeodomain Proteins); 0 (MyoD Protein); 0 (Trans-Activators)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE


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[PMID]:27771283
[Au] Autor:Coria-Lucero CD; Golini RS; Ponce IT; Deyurka N; Anzulovich AC; Delgado SM; Navigatore-Fonzo LS
[Ad] Endereço:Laboratory of Chronobiology, Multidisciplinary Institute of Biological Research-San Luis (IMIBIO-SL), National Council of Science and Technology (CONICET), National University of San Luis (UNSL)., Av Ejército de los Andes N° 950, D5700HHW, San Luis, Argentina.
[Ti] Título:Rhythmic Bdnf and TrkB expression patterns in the prefrontal cortex are lost in aged rats.
[So] Source:Brain Res;1653:51-58, 2016 12 15.
[Is] ISSN:1872-6240
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Aging brain undergoes several changes leading to a decline in cognitive functions. Memory and learning-related genes such as Creb, Bdnf and its receptor TrkB, are expressed in different brain regions including prefrontal cortex. Those genes' proteins regulate a wide range of functions such as synaptic plasticity and long-term potentiation. In this work, our objectives were: 1) to investigate whether Creb1, Bdnf and TrkB genes display endogenous circadian expression rhythms, in the prefrontal cortex of rats maintained under constant darkness conditions; 2) to study the synchronization of those temporal patterns to the local cellular clock and 3) to evaluate the aging consequences on both cognition-related genes and activating clock transcription factor, BMAL1, rhythms. A bioinformatics analysis revealed clock-responsive (E-box) sites in regulatory regions of Creb1, Bdnf and TrkB genes. Additionally, cAMP response elements (CRE) were found in Bdnf and TrkB promoters. We observed those key cognition-related factors expression oscillates in the rat prefrontal cortex. Creb1 and TrkB mRNAs display a circadian rhythm with their highest levels occurring at the second half of the 24h period. Interestingly, the cosinor analysis revealed a 12-h rhythm of Bdnf transcript levels, with peaks occurring at the second half of the subjective day and night, respectively. As expected, the BMAL1 rhythm's acrophase precedes Creb1 and first Bdnf expression peaks. Noteworthy, Creb1, Bdnf and TrkB expression rhythms are lost in the prefrontal cortex of aged rats, probably, as consequence of the loss of BMAL1 protein circadian rhythm and altered function of the local cellular clock.
[Mh] Termos MeSH primário: Envelhecimento/metabolismo
Fator Neurotrófico Derivado do Encéfalo/metabolismo
Ritmo Circadiano/fisiologia
Proteína de Ligação ao Elemento de Resposta ao AMP Cíclico/metabolismo
Córtex Pré-Frontal/metabolismo
Receptor trkB/metabolismo
[Mh] Termos MeSH secundário: Fatores de Transcrição ARNTL/metabolismo
Animais
Fator Neurotrófico Derivado do Encéfalo/genética
Proteína de Ligação ao Elemento de Resposta ao AMP Cíclico/genética
Elementos E-Box
Regulação da Expressão Gênica/fisiologia
Immunoblotting
Masculino
Fotoperíodo
RNA Mensageiro/metabolismo
Ratos Sprague-Dawley
Receptor trkB/genética
Reação em Cadeia da Polimerase Via Transcriptase Reversa
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (ARNTL Transcription Factors); 0 (Bmal1 protein, rat); 0 (Brain-Derived Neurotrophic Factor); 0 (CREB1 protein, rat); 0 (Cyclic AMP Response Element-Binding Protein); 0 (RNA, Messenger); EC 2.7.10.1 (Receptor, trkB)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171205
[Lr] Data última revisão:
171205
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


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[PMID]:29036192
[Au] Autor:Chen YT; Lin CF; Chen YM; Lo CE; Chen WE; Chen TY
[Ad] Endereço:Laboratory of Molecular Genetics, Department of Biotechnology and Bioindustry Sciences, College of Bioscience and Biotechnology, National Cheng Kung University, Tainan, Taiwan.
[Ti] Título:Viral infection upregulates myostatin promoter activity in orange-spotted grouper (Epinephelus coioides).
[So] Source:PLoS One;12(10):e0186506, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Myostatin is a negative regulator of myogenesis and has been suggested to be an important factor in the development of muscle wasting during viral infection. The objective of this study was to characterize the main regulatory element of the grouper myostatin promoter and to study changes in promoter activity due to viral stimulation. In vitro and in vivo experiments indicated that the E-box E6 is a positive cis-and trans-regulation motif, and an essential binding site for MyoD. In contrast, the E-box E5 is a dominant negative cis-regulatory. The characteristics of grouper myostatin promoter are similar in regulation of muscle growth to that of other species, but mainly through specific regulatory elements. According to these results, we conducted a study to investigate the effect of viral infection on myostatin promoter activity and its regulation. The nervous necrosis virus (NNV) treatment significantly induced myostatin promoter activity. The present study is the first report describing that specific myostatin motifs regulate promoter activity and response to viral infection.
[Mh] Termos MeSH primário: Bass/genética
Bass/virologia
Proteínas de Peixes/genética
Miostatina/genética
Regiões Promotoras Genéticas/genética
[Mh] Termos MeSH secundário: Animais
Sequência de Bases
Bass/imunologia
Elementos E-Box/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Fish Proteins); 0 (Myostatin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171106
[Lr] Data última revisão:
171106
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171017
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0186506


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[PMID]:28683467
[Au] Autor:Wu J; Zhou XJ; Sun X; Xia TS; Li XX; Shi L; Zhu L; Zhou WB; Wei JF; Ding Q
[Ad] Endereço:Jiangsu Breast Disease Center, The First Affiliated Hospital with Nanjing Medical University, 300 Guangzhou Road, Nanjing 210029, China.
[Ti] Título:RBM38 is involved in TGF-ß-induced epithelial-to-mesenchymal transition by stabilising zonula occludens-1 mRNA in breast cancer.
[So] Source:Br J Cancer;117(5):675-684, 2017 Aug 22.
[Is] ISSN:1532-1827
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The transforming growth factor-ß (TGF-ß) pathway plays a vital role in driving cancer cell epithelial-mesenchymal transition (EMT). Zonula occludens-1 (ZO-1), which is downregulated in response to TGF-ß, is able to control endothelial cell-cell tension, cell migration, and barrier formation. However, the molecular mechanism of how TGF-ß regulates ZO-1 expression remains unclear. METHODS: Breast cancer cells were treated with TGF-ß to induce an EMT progress. Chromatin immunoprecipitation and dual-luciferase reporter assay were performed to investigate direct relationship between Snail and RNA binding motif protein 38 (RBM38). The RNA immunoprecipitation combined with RNA electrophoretic mobility shift assay and dual-luciferase reporter assay were conducted to testify direct relationship between RBM38 and ZO-1. The ZO-1 siRNA was transfected to breast cancer cells that overexpress RBM38 and the control, followed by transwell and Matrigel invasion assays to examine cell migratory and invasive ability. RESULTS: Transforming growth factor-ß induced a remarkable downregulation of RBM38 in breast cancer that was directly regulated by transcription repressor Snail targeting the E-box elements in promoter region of RBM38 gene. Additionally, RBM38 positively regulated ZO-1 transcript via directly binding to AU/U-rich elements in its mRNA 3'-UTR. Moreover, by magnifying RBM38 expression, cell migration and invasion mediated by knockdown of ZO-1 in breast cancer were reversed. CONCLUSIONS: All the results clarified a linear regulation relationship among Snail, RBM38, and ZO-1, implicating RBM38 as a pivotal mediator in TGF-ß-induced EMT in breast cancer.
[Mh] Termos MeSH primário: Transição Epitelial-Mesenquimal
RNA Mensageiro/metabolismo
Proteínas de Ligação a RNA/genética
Proteínas de Ligação a RNA/metabolismo
Proteína da Zônula de Oclusão-1/genética
Proteína da Zônula de Oclusão-1/metabolismo
[Mh] Termos MeSH secundário: Regiões 3' não Traduzidas
Benzamidas/farmacologia
Neoplasias da Mama/química
Movimento Celular/efeitos dos fármacos
Movimento Celular/genética
Dioxóis/farmacologia
Regulação para Baixo
Elementos E-Box/genética
Transição Epitelial-Mesenquimal/efeitos dos fármacos
Feminino
Expressão Gênica
Seres Humanos
Células MCF-7
Regiões Promotoras Genéticas
Proteínas Serina-Treonina Quinases/antagonistas & inibidores
RNA Interferente Pequeno/genética
Proteínas de Ligação a RNA/análise
Receptores de Fatores de Crescimento Transformadores beta/antagonistas & inibidores
Fatores de Transcrição da Família Snail/genética
Transfecção
Fator de Crescimento Transformador beta/farmacologia
Proteína da Zônula de Oclusão-1/análise
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (3' Untranslated Regions); 0 (4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1H-imidazol-2-yl)benzamide); 0 (Benzamides); 0 (Dioxoles); 0 (RBM38 protein, human); 0 (RNA, Messenger); 0 (RNA, Small Interfering); 0 (RNA-Binding Proteins); 0 (Receptors, Transforming Growth Factor beta); 0 (SNAI1 protein, human); 0 (Snail Family Transcription Factors); 0 (Transforming Growth Factor beta); 0 (Zonula Occludens-1 Protein); EC 2.7.1.11 (TGF-beta type I receptor); EC 2.7.11.1 (Protein-Serine-Threonine Kinases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170918
[Lr] Data última revisão:
170918
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170707
[St] Status:MEDLINE
[do] DOI:10.1038/bjc.2017.204


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[PMID]:28350847
[Au] Autor:Maltais L; Montagne M; Bédard M; Tremblay C; Soucek L; Lavigne P
[Ad] Endereço:Département de Biochimie, Faculté de Médecine et des Sciences de la Santé, Institut de Pharmacologie de Sherbrooke, Université de Sherbrooke, Sherbrooke, Québec, Canada.
[Ti] Título:Biophysical characterization of the b-HLH-LZ of ΔMax, an alternatively spliced isoform of Max found in tumor cells: Towards the validation of a tumor suppressor role for the Max homodimers.
[So] Source:PLoS One;12(3):e0174413, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:It is classically recognized that the physiological and oncogenic functions of Myc proteins depend on specific DNA binding enabled by the dimerization of its C-terminal basic-region-Helix-Loop-Helix-Leucine Zipper (b-HLH-LZ) domain with that of Max. However, a new paradigm is emerging, where the binding of the c-Myc/Max heterodimer to non-specific sequences in enhancers and promoters drives the transcription of genes involved in diverse oncogenic programs. Importantly, Max can form a stable homodimer even in the presence of c-Myc and bind DNA (specific and non-specific) with comparable affinity to the c-Myc/Max heterodimer. Intriguingly, alterations in the Max gene by germline and somatic mutations or changes in the gene product by alternative splicing (e.g. ΔMax) were recently associated with pheochromocytoma and glioblastoma, respectively. This has led to the proposition that Max is, by itself, a tumor suppressor. However, the actual mechanism through which it exerts such an activity remains to be elucidated. Here, we show that contrary to the WT motif, the b-HLH-LZ of ΔMax does not homodimerize in the absence of DNA. In addition, although ΔMax can still bind the E-box sequence as a homodimer, it cannot bind non-specific DNA in that form, while it can heterodimerize with c-Myc and bind E-box and non-specific DNA as a heterodimer with high affinity. Taken together, our results suggest that the WT Max homodimer is important for attenuating the binding of c-Myc to specific and non-specific DNA, whereas ΔMax is unable to do so. Conversely, the splicing of Max into ΔMax could provoke an increase in overall chromatin bound c-Myc. According to the new emerging paradigm, the splicing event and the stark reduction in homodimer stability and DNA binding should promote tumorigenesis impairing the tumor suppressor activity of the WT homodimer of Max.
[Mh] Termos MeSH primário: Processamento Alternativo
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
DNA/metabolismo
Neoplasias/genética
Proteínas Proto-Oncogênicas c-myc/metabolismo
Proteínas Repressoras/genética
Proteínas Repressoras/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Fatores de Transcrição de Zíper de Leucina e Hélice-Alça-Hélix Básicos/química
DNA/química
Elementos E-Box
Seres Humanos
Modelos Moleculares
Neoplasias/metabolismo
Multimerização Proteica
Proteínas Repressoras/química
Proteínas Supressoras de Tumor/química
Proteínas Supressoras de Tumor/genética
Proteínas Supressoras de Tumor/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Basic Helix-Loop-Helix Leucine Zipper Transcription Factors); 0 (MXD1 protein, human); 0 (Proto-Oncogene Proteins c-myc); 0 (Repressor Proteins); 0 (Tumor Suppressor Proteins); 9007-49-2 (DNA)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170906
[Lr] Data última revisão:
170906
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170329
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0174413


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[PMID]:28161523
[Au] Autor:Zhang W; Roy S
[Ad] Endereço:Institute of Molecular and Cell Biology, Proteos, 61 Biopolis Drive, Singapore 138673, Singapore.
[Ti] Título:Myomaker is required for the fusion of fast-twitch myocytes in the zebrafish embryo.
[So] Source:Dev Biol;423(1):24-33, 2017 03 01.
[Is] ISSN:1095-564X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:During skeletal muscle development, myocytes aggregate and fuse to form multinucleated muscle fibers. Inhibition of myocyte fusion is thought to significantly derail the differentiation of functional muscle fibers. Despite the purported importance of fusion in myogenesis, in vivo studies of this process in vertebrates are rather limited. Myomaker, a multipass transmembrane protein, has been shown to be the first muscle-specific fusion protein essential for myocyte fusion in the mouse. We have generated loss-of-function alleles in zebrafish myomaker, and found that fusion of myocytes into syncytial fast-twitch muscles was significantly compromised. However, mutant myocytes could be recruited to fuse with wild-type myocytes in chimeric embryos, albeit rather inefficiently. Conversely, overexpression of Myomaker was sufficient to induce hyperfusion among fast-twitch myocytes, and it also induced fusion among slow-twitch myocytes that are normally fusion-incompetent. In line with this, Myomaker overexpression also triggered fusion in another myocyte fusion mutant compromised in the function of the junctional cell adhesion molecule, Jam2a. We also provide evidence that Rac, a regulator of actin cytoskeleton, requires Myomaker activity to induce fusion, and that an approximately 3kb of myomaker promoter sequence, with multiple E-box motifs, is sufficient to direct expression within the fast-twitch muscle lineage. Taken together, our findings underscore a conserved role for Myomaker in vertebrate myocyte fusion. Strikingly, and in contrast to the mouse, homozygous myomaker mutants are viable and do not exhibit discernible locomotory defects. Thus, in the zebrafish, myocyte fusion is not an absolute requirement for skeletal muscle morphogenesis and function.
[Mh] Termos MeSH primário: Embrião não Mamífero/citologia
Embrião não Mamífero/metabolismo
Proteínas de Membrana/metabolismo
Células Musculares/citologia
Células Musculares/metabolismo
Fibras Musculares de Contração Rápida/citologia
Proteínas Musculares/metabolismo
Proteínas de Peixe-Zebra/metabolismo
Peixe-Zebra/embriologia
[Mh] Termos MeSH secundário: Animais
Sequência de Bases
Fusão Celular
Linhagem da Célula/genética
Elementos E-Box/genética
Genes Reporter
Locomoção
Proteínas de Membrana/genética
Fibras Musculares de Contração Rápida/metabolismo
Fibras Musculares de Contração Lenta/metabolismo
Proteínas Musculares/genética
Mutação/genética
Fenótipo
Regiões Promotoras Genéticas/genética
Natação
Peixe-Zebra/genética
Proteínas de Peixe-Zebra/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (Muscle Proteins); 0 (Zebrafish Proteins); 0 (myomaker protein, zebrafish)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171110
[Lr] Data última revisão:
171110
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170206
[St] Status:MEDLINE


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[PMID]:28102866
[Au] Autor:Inamoto I; Chen G; Shin JA
[Ad] Endereço:Department of Chemistry, University of Toronto, 3359 Mississauga Road, Mississauga, Ontario, Canada L5L 1C6. jumi.shin@utoronto.ca.
[Ti] Título:The DNA target determines the dimerization partner selected by bHLHZ-like hybrid proteins AhRJun and ArntFos.
[So] Source:Mol Biosyst;13(3):476-488, 2017 Feb 28.
[Is] ISSN:1742-2051
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The molecular basis of protein-partner selection and DNA binding of the basic helix-loop-helix (bHLH) and basic region-leucine zipper (bZIP) superfamilies of dimeric transcription factors is fundamental toward understanding gene regulation. Because these families share structural similarities, we swapped the bHLH and leucine zipper (LZ) modules between families to uncover how individual modules influence protein-partnering and protein:DNA complexation. We previously described ArntFos, a bHLHZ-like hybrid of the bHLH domain from the bHLH/PAS protein Arnt and LZ from the bZIP protein c-Fos, binding to the Arnt E-box site (TCACGTGA) as a homodimer. Herein, we describe a heterodimer between ArntFos and AhRJun, a hybrid of the bHLH domain from AhR and LZ of JunD. We designed AhRJun and ArntFos to heterodimerize, given the strong interaction between native AhR/Arnt and Jun/Fos, but the hybrids showed no preference for hetero- or homo-dimerization in Y2H assays. However, adding a specific DNA target drove the formation of a single dimeric protein species over others. EMSA showed that the AhRJun/ArntFos heterodimer binds to the cognate DNA site XRE1 (TTGCGTG) with K = 337 nM. Unexpectedly, the palindromic Arnt E-box drove the binding of the AhRJun/ArntFos heterodimer (K = 276 nM)-not the ArntFos homodimer-that binds to the Arnt E-box. However, the dimerization preference switched to the ArntFos homodimer when the variant Max E-box (CCACGTGG) was used. We conclude that the DNA sites themselves are the primary determinants of dimerization specificity for AhRJun and ArntFos, not the JunD and c-Fos LZs, a result that sheds light on the dynamics of protein/protein and protein:DNA interactions and the structural modularity of bHLH and bZIP proteins.
[Mh] Termos MeSH primário: Fatores de Transcrição Hélice-Alça-Hélice Básicos/química
DNA/química
Multimerização Proteica
Proteínas Recombinantes de Fusão/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Fatores de Transcrição Hélice-Alça-Hélice Básicos/genética
Fatores de Transcrição Hélice-Alça-Hélice Básicos/metabolismo
Sítios de Ligação
Proteínas Estimuladoras de Ligação a CCAAT/metabolismo
DNA/metabolismo
Elementos E-Box
Expressão Gênica
Genes Reporter
Sequências Hélice-Volta-Hélice
Zíper de Leucina
Ligação Proteica
Conformação Proteica
Proteínas Recombinantes de Fusão/genética
Proteínas Recombinantes de Fusão/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Basic Helix-Loop-Helix Transcription Factors); 0 (CCAAT-Enhancer-Binding Proteins); 0 (Recombinant Fusion Proteins); 9007-49-2 (DNA)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170724
[Lr] Data última revisão:
170724
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170120
[St] Status:MEDLINE
[do] DOI:10.1039/c6mb00795c


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[PMID]:27981602
[Au] Autor:Fan W; Yang H; Liu T; Wang J; Li TW; Mavila N; Tang Y; Yang J; Peng H; Tu J; Annamalai A; Noureddin M; Krishnan A; Gores GJ; Martínez-Chantar ML; Mato JM; Lu SC
[Ad] Endereço:Division of Digestive and Liver Diseases, Cedars-Sinai Medical Center, Los Angeles, CA.
[Ti] Título:Prohibitin 1 suppresses liver cancer tumorigenesis in mice and human hepatocellular and cholangiocarcinoma cells.
[So] Source:Hepatology;65(4):1249-1266, 2017 Apr.
[Is] ISSN:1527-3350
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Prohibitin 1 (PHB1) is best known as a mitochondrial chaperone, and its role in cancer is conflicting. Mice lacking methionine adenosyltransferase α1 (MATα1) have lower PHB1 expression, and we reported that c-MYC interacts directly with both proteins. Furthermore, c-MYC and MATα1 exert opposing effects on liver cancer growth, prompting us to examine the interplay between PHB1, MATα1, and c-MYC and PHB1's role in liver tumorigenesis. We found that PHB1 is highly expressed in normal hepatocytes and bile duct epithelial cells and down-regulated in most human hepatocellular carcinoma (HCC) and cholangiocarcinoma (CCA). In HCC and CCA cells, PHB1 expression correlates inversely with growth. PHB1 and MAT1A positively regulate each other's expression, whereas PHB1 negatively regulates the expression of c-MYC, MAFG, and c-MAF. Both PHB1 and MATα1 heterodimerize with MAX, bind to the E-box element, and repress E-box promoter activity. PHB1 promoter contains a repressive E-box element and is occupied mainly by MAX, MNT, and MATα1 in nonmalignant cholangiocytes and noncancerous tissues that switched to c-MYC, c-MAF, and MAFG in cancer cells and human HCC/CCA. All 8-month-old liver-specific Phb1 knockout mice developed HCC, and one developed CCA. Five-month-old Phb1 heterozygotes, but not Phb1 flox mice, developed aberrant bile duct proliferation; and one developed CCA 3.5 months after left and median bile duct ligation. Phb1 heterozygotes had a more profound fall in the expression of glutathione synthetic enzymes and higher hepatic oxidative stress following left and median bile duct ligation. CONCLUSION: We have identified that PHB1, down-regulated in most human HCC and CCA, heterodimerizes with MAX to repress the E-box and positively regulates MAT1A while suppressing c-MYC, MAFG, and c-MAF expression; in mice, reduced PHB1 expression predisposes to the development of cholestasis-induced CCA. (Hepatology 2017;65:1249-1266).
[Mh] Termos MeSH primário: Neoplasias dos Ductos Biliares/patologia
Carcinoma Hepatocelular/patologia
Colangiocarcinoma/patologia
Neoplasias Hepáticas/patologia
Proteínas Repressoras/genética
Proteínas Repressoras/metabolismo
[Mh] Termos MeSH secundário: Animais
Neoplasias dos Ductos Biliares/metabolismo
Biópsia por Agulha
Western Blotting
Carcinogênese/metabolismo
Carcinoma Hepatocelular/metabolismo
Linhagem Celular Tumoral
Transformação Celular Neoplásica/patologia
Colangiocarcinoma/metabolismo
Modelos Animais de Doenças
Regulação para Baixo
Elementos E-Box/genética
Perfilação da Expressão Gênica
Seres Humanos
Imuno-Histoquímica
Neoplasias Hepáticas/metabolismo
Masculino
Camundongos
Camundongos Knockout
Reação em Cadeia da Polimerase/métodos
RNA Mensageiro/análise
Distribuição Aleatória
Sensibilidade e Especificidade
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); 0 (Repressor Proteins); 0 (prohibitin)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161217
[St] Status:MEDLINE
[do] DOI:10.1002/hep.28964


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[PMID]:27903915
[Au] Autor:Wang D; Hashimoto H; Zhang X; Barwick BG; Lonial S; Boise LH; Vertino PM; Cheng X
[Ad] Endereço:Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA.
[Ti] Título:MAX is an epigenetic sensor of 5-carboxylcytosine and is altered in multiple myeloma.
[So] Source:Nucleic Acids Res;45(5):2396-2407, 2017 Mar 17.
[Is] ISSN:1362-4962
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The oncogenic transcription factor MYC and its binding partner MAX regulate gene expression by binding to DNA at enhancer-box (E-box) elements 5΄-CACGTG-3΄. In mammalian genomes, the central E-box CpG has the potential to be methylated at the 5-position of cytosine (5mC), or to undergo further oxidation to the 5-hydroxymethyl (5hmC), 5-formyl (5fC), or 5-carboxyl (5caC) forms. We find that MAX exhibits the greatest affinity for a 5caC or unmodified C-containing E-box, and much reduced affinities for the corresponding 5mC, 5hmC or 5fC forms. Crystallization of MAX with a 5caC modified E-box oligonucleotide revealed that MAX Arg36 recognizes 5caC using a 5caC-Arg-Guanine triad, with the next nearest residue to the carboxylate group being Arg60. In an analysis of >800 primary multiple myelomas, MAX alterations occurred at a frequency of ∼3%, more than half of which were single nucleotide substitutions affecting a basic clamp-like interface important for DNA interaction. Among these, arginines 35, 36 and 60 were the most frequently altered. In vitro binding studies showed that whereas mutation of Arg36 (R36W) or Arg35 (R35H/L) completely abolished DNA binding, mutation of Arg60 (R60Q) significantly reduced DNA binding, but retained a preference for the 5caC modified E-box. Interestingly, MAX alterations define a subset of myeloma patients with lower MYC expression and a better overall prognosis. Together these data indicate that MAX can act as a direct epigenetic sensor of E-box cytosine modification states and that local CpG modification and MAX variants converge to modulate the MAX-MYC transcriptional network.
[Mh] Termos MeSH primário: Fatores de Transcrição de Zíper de Leucina e Hélice-Alça-Hélix Básicos/química
Fatores de Transcrição de Zíper de Leucina e Hélice-Alça-Hélix Básicos/genética
Citosina/análogos & derivados
Elementos E-Box
Mieloma Múltiplo/genética
Proteínas Repressoras/química
Proteínas Repressoras/genética
[Mh] Termos MeSH secundário: Arginina/química
Fatores de Transcrição de Zíper de Leucina e Hélice-Alça-Hélix Básicos/metabolismo
Ilhas de CpG
Citosina/química
Citosina/metabolismo
DNA/química
DNA/metabolismo
Epigênese Genética
Mutação
Ligação Proteica
Conformação Proteica
Proteínas Repressoras/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (5-carboxylcytosine); 0 (Basic Helix-Loop-Helix Leucine Zipper Transcription Factors); 0 (MNT protein, human); 0 (Repressor Proteins); 8J337D1HZY (Cytosine); 9007-49-2 (DNA); 94ZLA3W45F (Arginine)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170808
[Lr] Data última revisão:
170808
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161202
[St] Status:MEDLINE
[do] DOI:10.1093/nar/gkw1184


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[PMID]:27941970
[Au] Autor:Weger BD; Weger M; Görling B; Schink A; Gobet C; Keime C; Poschet G; Jost B; Krone N; Hell R; Gachon F; Luy B; Dickmeis T
[Ad] Endereço:Institute of Toxicology and Genetics, Karlsruhe Institute of Technology, Hermann-von-Helmholtz-Platz 1, Eggenstein-Leopoldshafen, Germany.
[Ti] Título:Extensive Regulation of Diurnal Transcription and Metabolism by Glucocorticoids.
[So] Source:PLoS Genet;12(12):e1006512, 2016 Dec.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Altered daily patterns of hormone action are suspected to contribute to metabolic disease. It is poorly understood how the adrenal glucocorticoid hormones contribute to the coordination of daily global patterns of transcription and metabolism. Here, we examined diurnal metabolite and transcriptome patterns in a zebrafish glucocorticoid deficiency model by RNA-Seq, NMR spectroscopy and liquid chromatography-based methods. We observed dysregulation of metabolic pathways including glutaminolysis, the citrate and urea cycles and glyoxylate detoxification. Constant, non-rhythmic glucocorticoid treatment rescued many of these changes, with some notable exceptions among the amino acid related pathways. Surprisingly, the non-rhythmic glucocorticoid treatment rescued almost half of the entire dysregulated diurnal transcriptome patterns. A combination of E-box and glucocorticoid response elements is enriched in the rescued genes. This simple enhancer element combination is sufficient to drive rhythmic circadian reporter gene expression under non-rhythmic glucocorticoid exposure, revealing a permissive function for the hormones in glucocorticoid-dependent circadian transcription. Our work highlights metabolic pathways potentially contributing to morbidity in patients with glucocorticoid deficiency, even under glucocorticoid replacement therapy. Moreover, we provide mechanistic insight into the interaction between the circadian clock and glucocorticoids in the transcriptional regulation of metabolism.
[Mh] Termos MeSH primário: Proteínas CLOCK/biossíntese
Relógios Circadianos/genética
Elementos E-Box/genética
Glucocorticoides/genética
Redes e Vias Metabólicas/genética
[Mh] Termos MeSH secundário: Animais
Proteínas CLOCK/genética
Ritmo Circadiano/genética
Ácido Cítrico/metabolismo
Regulação da Expressão Gênica
Glucocorticoides/biossíntese
Glucocorticoides/deficiência
Sequenciamento de Nucleotídeos em Larga Escala
Hormônios/genética
Hormônios/metabolismo
Seres Humanos
Espectroscopia de Ressonância Magnética
Transcrição Genética
Transcriptoma/genética
Ureia/metabolismo
Peixe-Zebra
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glucocorticoids); 0 (Hormones); 2968PHW8QP (Citric Acid); 8W8T17847W (Urea); EC 2.3.1.48 (CLOCK Proteins)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170509
[Lr] Data última revisão:
170509
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161213
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1006512



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