Base de dados : MEDLINE
Pesquisa : D08.811.913.555.500.800.800 [Categoria DeCS]
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[PMID]:27862816
[Au] Autor:Härtl K; Kalinowski G; Hoffmann T; Preuss A; Schwab W
[Ad] Endereço:Biotechnology of Natural Products, Technische Universität München, Freising, Germany.
[Ti] Título:RNAi-mediated endogene silencing in strawberry fruit: detection of primary and secondary siRNAs by deep sequencing.
[So] Source:Plant Biotechnol J;15(5):658-668, 2017 May.
[Is] ISSN:1467-7652
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:RNA interference (RNAi) has been exploited as a reverse genetic tool for functional genomics in the nonmodel species strawberry (Fragaria × ananassa) since 2006. Here, we analysed for the first time different but overlapping nucleotide sections (>200 nt) of two endogenous genes, FaCHS (chalcone synthase) and FaOMT (O-methyltransferase), as inducer sequences and a transitive vector system to compare their gene silencing efficiencies. In total, ten vectors were assembled each containing the nucleotide sequence of one fragment in sense and corresponding antisense orientation separated by an intron (inverted hairpin construct, ihp). All sequence fragments along the full lengths of both target genes resulted in a significant down-regulation of the respective gene expression and related metabolite levels. Quantitative PCR data and successful application of a transitive vector system coinciding with a phenotypic change suggested propagation of the silencing signal. The spreading of the signal in strawberry fruit in the 3' direction was shown for the first time by the detection of secondary small interfering RNAs (siRNAs) outside of the primary targets by deep sequencing. Down-regulation of endogenes by the transitive method was less effective than silencing by ihp constructs probably because the numbers of primary siRNAs exceeded the quantity of secondary siRNAs by three orders of magnitude. Besides, we observed consistent hotspots of primary and secondary siRNA formation along the target sequence which fall within a distance of less than 200 nt. Thus, ihp vectors seem to be superior over the transitive vector system for functional genomics in strawberry fruit.
[Mh] Termos MeSH primário: Fragaria/genética
Frutas/genética
Interferência de RNA
RNA Interferente Pequeno
[Mh] Termos MeSH secundário: Aciltransferases/genética
Fragaria/metabolismo
Inativação Gênica
Genes de Plantas
Sequenciamento de Nucleotídeos em Larga Escala
Proteínas de Plantas/genética
Proteína O-Metiltransferase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Plant Proteins); 0 (RNA, Small Interfering); EC 2.1.1.- (Protein O-Methyltransferase); EC 2.3.- (Acyltransferases); EC 2.3.1.74 (flavanone synthetase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171005
[Lr] Data última revisão:
171005
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE
[do] DOI:10.1111/pbi.12664


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[PMID]:27589033
[Au] Autor:van Wijlick L; Swidergall M; Brandt P; Ernst JF
[Ad] Endereço:Department Biologie, Molekulare Mykologie, Heinrich-Heine-Universität, 40225, Düsseldorf, Germany.
[Ti] Título:Candida albicans responds to glycostructure damage by Ace2-mediated feedback regulation of Cek1 signaling.
[So] Source:Mol Microbiol;102(5):827-849, 2016 Dec.
[Is] ISSN:1365-2958
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Candida albicans uses the Cek1 MAPK pathway to restore cells from damage of its cell wall glycostructures. Defective protein N- or O-glycosylation activates Cek1 and the transcription factor Ace2 as its downstream target, to upregulate genes encoding protein O-mannosyltransferases (Pmt proteins). In unstressed cells, Cek1-Ace2 activity blocks expression of PMT1, which is de-repressed by tunicamycin. Genomic binding targets of Ace2 included ZCF21, which was upregulated by Ace2 and found to repress PMT1 transcription in unstressed cells. Surprisingly, genes encoding components of the Cek1 pathway including MSB2, CST20, HST7, CEK1 and ACE2 were also identified as Ace2 targets indicating Ace2-mediated transcriptional amplification of pathway genes under N-glycosylation stress. In this condition, physical interaction of the Ace2 protein with the upstream MAPKKK Cst20 was detected. Cst20-GFP showed stress-induced import from the cytoplasm into the nucleus and phosphorylation of Ace2. Interestingly, forced nuclear localization of Cst20 inhibited Cek1-Ace2 signaling, while forced cytoplasmic localization of Cst20 retained full signaling activity, suggesting that nuclear Cst20 downregulates the Cek1 pathway. Collectively, the results indicate that Ace2 is a versatile multifunctional transcriptional regulator, which activates glycostress responses of C. albicans by both positive forward and negative feedback regulation of Cek1 signaling.
[Mh] Termos MeSH primário: Candida albicans/metabolismo
Proteínas Fúngicas/metabolismo
Proteína Quinase 3 Ativada por Mitógeno/metabolismo
[Mh] Termos MeSH secundário: Candida albicans/genética
Parede Celular/metabolismo
Proteínas Fúngicas/genética
Manosiltransferases/genética
Manosiltransferases/metabolismo
Proteína Quinase 3 Ativada por Mitógeno/genética
Proteínas Quinases Ativadas por Mitógeno/metabolismo
Fosforilação
Proteína O-Metiltransferase/genética
Proteína O-Metiltransferase/metabolismo
Transdução de Sinais
Fatores de Transcrição/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ACE2 protein, Candida glabrata); 0 (Fungal Proteins); 0 (Transcription Factors); 148971-42-0 (CEK1 protein, Candida albicans); EC 2.1.1.- (Protein O-Methyltransferase); EC 2.4.1.- (Mannosyltransferases); EC 2.4.1.109 (protein O-mannosyltransferase); EC 2.7.11.24 (Mitogen-Activated Protein Kinase 3); EC 2.7.11.24 (Mitogen-Activated Protein Kinases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170811
[Lr] Data última revisão:
170811
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160903
[St] Status:MEDLINE
[do] DOI:10.1111/mmi.13494


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[PMID]:27507813
[Au] Autor:Hwang J; Lee JA; Pallas DC
[Ad] Endereço:From the Department of Biochemistry, Winship Cancer Center, and the Biochemistry, Cell, and Developmental Graduate Program, Emory University School of Medicine, Atlanta, Georgia 30322.
[Ti] Título:Leucine Carboxyl Methyltransferase 1 (LCMT-1) Methylates Protein Phosphatase 4 (PP4) and Protein Phosphatase 6 (PP6) and Differentially Regulates the Stable Formation of Different PP4 Holoenzymes.
[So] Source:J Biol Chem;291(40):21008-21019, 2016 Sep 30.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The protein phosphatase 2A (PP2A) subfamily of phosphatases, PP2A, PP4, and PP6, are multifunctional serine/threonine protein phosphatases involved in many cellular processes. Carboxyl methylation of the PP2A catalytic subunit (PP2Ac) C-terminal leucine is regulated by the opposing activities of leucine carboxyl methyltransferase 1 (LCMT-1) and protein phosphatase methylesterase 1 (PME-1) and regulates PP2A holoenzyme formation. The site of methylation on PP2Ac is conserved in the catalytic subunits of PP4 and PP6, and PP4 is also methylated on that site, but the identities of the methyltransferase enzyme for PP4 are not known. Whether PP6 is methylated is also not known. Here we use antibodies specific for the unmethylated phosphatases to show that PP6 is carboxyl-methylated and that LCMT-1 is the major methyltransferase for PP2A, PP4, and PP6 in mouse embryonic fibroblasts (MEFs). Analysis of PP2A and PP4 complexes by blue native polyacrylamide gel electrophoresis (BN-PAGE) indicates that PP4 holoenzyme complexes, like those of PP2A, are differentially regulated by LCMT-1, with the PP4 regulatory subunit 1 (PP4R1)-containing PP4 complex being the most dramatically affected by the LCMT-1 loss. MEFs derived from LCMT-1 knock-out mouse embryos have reduced levels of PP2A B regulatory subunit and PP4R1 relative to control MEFs, indicating that LCMT-1 is important for maintaining normal levels of these subunits. Finally, LCMT-1 homozygous knock-out MEFs exhibited hyperphosphorylation of HDAC3, a reported target of the methylation-dependent PP4R1-PP4c complex. Collectively, our data suggest that LCMT-1 coordinately regulates the carboxyl methylation of PP2A-related phosphatases and, consequently, their holoenzyme assembly and function.
[Mh] Termos MeSH primário: Embrião de Mamíferos/enzimologia
Fibroblastos/enzimologia
Fosfoproteínas Fosfatases/metabolismo
Proteína O-Metiltransferase/metabolismo
[Mh] Termos MeSH secundário: Animais
Células Cultivadas
Histona Desacetilases/genética
Histona Desacetilases/metabolismo
Holoenzimas/genética
Holoenzimas/metabolismo
Metilação
Camundongos
Camundongos Knockout
Fosfoproteínas Fosfatases/genética
Fosforilação/genética
Proteína O-Metiltransferase/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Holoenzymes); EC 2.1.1.- (Lcmt1 protein, mouse); EC 2.1.1.- (Protein O-Methyltransferase); EC 3.1.3.16 (Phosphoprotein Phosphatases); EC 3.1.3.16 (protein phosphatase 4); EC 3.1.3.16 (protein phosphatase 6); EC 3.5.1.98 (Histone Deacetylases); EC 3.5.1.98 (histone deacetylase 3)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170930
[Lr] Data última revisão:
170930
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160811
[St] Status:MEDLINE


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[PMID]:27459928
[Au] Autor:Liu CD; Wang Q; Zong DK; Pei SC; Yan Y; Yan ML; Sun LL; Hao YY; Mao M; Xing WJ; Ren H; Ai J
[Ad] Endereço:Department of Pharmacology, College of Pharmacy of Harbin Medical University, Harbin, Heilongjiang Province, China.
[Ti] Título:Knockdown of microRNA-195 contributes to protein phosphatase-2A inactivation in rats with chronic brain hypoperfusion.
[So] Source:Neurobiol Aging;45:76-87, 2016 Sep.
[Is] ISSN:1558-1497
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Reduction of protein phosphatase-2A (PP2A) activity is a common clinical feature of Alzheimer's disease and vascular dementia. In this study, we observed that chronic brain hypoperfusion induced by bilateral common carotid artery occlusion of rats led to PP2A inactivation based on the increase in tyrosine-307 phosphorylation and leucine-309 demethylation of PP2AC and the depression in PP2ABα. Knockdown of miR-195 using overexpression of its antisense molecule oligonucleotide (pre-AMO-miR-195) delivered by a lentivirus (lenti-pre-AMO-miR-195) increased tyrosine-307 phosphorylation and decreased both PP2ABα expression and leucine-309 methylation; these effects were prevented by the overexpression of miR-195 using lenti-pre-miR-195 and controlled by an increase in methylesterase (PME-1) and a decrease in leucine carboxyl methyltransferase-1. In vitro studies demonstrated that miR-195 regulated PME-1 expression by binding to the Ppme1 gene 3'-untranslated region (3'UTR) domain. Masking the miR-195 binding sites in the amyloid precursor protein (APP) and ß-site APP cleaving enzyme 1 genes prevented miR-195-induced leucine carboxyl methyltransferase-1 elevation. We concluded that the miR-195 downregulation in chronic brain hypoperfusion involved PP2A inactivity, which was mediated by the post-transcriptional regulation PME-1, APP, and ß-site APP cleaving enzyme 1 expression.
[Mh] Termos MeSH primário: Isquemia Encefálica/enzimologia
Ativação Enzimática/genética
Técnicas de Silenciamento de Genes
MicroRNAs/genética
Proteína Fosfatase 2/metabolismo
[Mh] Termos MeSH secundário: Animais
Hidrolases de Éster Carboxílico/metabolismo
Doença Crônica
Regulação para Baixo
Masculino
Proteína O-Metiltransferase/metabolismo
Ratos Sprague-Dawley
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (MIRN195 microRNA, rat); 0 (MicroRNAs); EC 2.1.1.- (Protein O-Methyltransferase); EC 2.1.1.- (leucine carboxyl methyltransferase-1, human); EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.- (protein phosphatase methylesterase-1); EC 3.1.3.16 (Protein Phosphatase 2)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171017
[Lr] Data última revisão:
171017
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160728
[St] Status:MEDLINE


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[PMID]:27373689
[Au] Autor:Kuwana S; Senoo H; Sawai S; Fukuzawa M
[Ad] Endereço:Department of Biology, Faculty of Agriculture and Life Science, Hirosaki University, Hirosaki 036-8561, Japan.
[Ti] Título:A novel, lineage-primed prestalk cell subtype involved in the morphogenesis of D. discoideum.
[So] Source:Dev Biol;416(2):286-99, 2016 Aug 15.
[Is] ISSN:1095-564X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dictyostelium morphogenesis requires the tip, which acts as an organizer and conducts orchestrated cell movement and cell differentiation. At the slug stage the tip region contains prestalk A (pstA) cells, which are usually recognized by their expression of reporter constructs that utilize a fragment of the promoter of the ecmA gene. Here, using the promoter region of the o-methyl transferase 12 gene (omt12) to drive reporter expression, we demonstrate the presence, also within the pstA region, of a novel prestalk cell subtype: the pstV(A) cells. Surprisingly, a sub-population of the vegetative cells express a pstV(A): GFP marker and, sort out to the tip, both when developing alone and when co-developed with an excess of unmarked cells. The development of such a purified GFP-marked population is greatly accelerated: by precocious cell aggregation and tip formation with accompanying precocious elevation of developmental gene transcription. We therefore suggest that the tip contains at least two prestalk cell subtypes: the developmentally-specified pstA cells and the lineage-primed pstV(A) cells. It is presumably the pstV(A) cells that play the dominant role in morphogenesis during the earlier stages of development. The basis for the lineage priming is, however, unclear because we can find no correlation between pstV(A) differentiation and nutrient status during growth or cell cycle position at the time of starvation, the two known determinants of probable cell fate.
[Mh] Termos MeSH primário: Dictyostelium/citologia
[Mh] Termos MeSH secundário: Agregação Celular
Linhagem da Célula
Movimento Celular
Dictyostelium/crescimento & desenvolvimento
Citometria de Fluxo
Genes de Protozoários
Genes Reporter
Proteínas de Fluorescência Verde/análise
Proteínas de Fluorescência Verde/genética
Microscopia Confocal
Microscopia de Fluorescência
Morfogênese
Regiões Promotoras Genéticas
Proteína O-Metiltransferase/genética
Proteínas de Protozoários/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; VIDEO-AUDIO MEDIA
[Nm] Nome de substância:
0 (Protozoan Proteins); 147336-22-9 (Green Fluorescent Proteins); EC 2.1.1.- (Protein O-Methyltransferase)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:170530
[Lr] Data última revisão:
170530
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160705
[St] Status:MEDLINE


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[PMID]:27312813
[Au] Autor:Khaliullin B; Aggarwal P; Bubas M; Eaton GR; Eaton SS; Latham JA
[Ad] Endereço:Department of Chemistry and Biochemistry, University of Denver, CO, USA.
[Ti] Título:Mycofactocin biosynthesis: modification of the peptide MftA by the radical S-adenosylmethionine protein MftC.
[So] Source:FEBS Lett;590(16):2538-48, 2016 Aug.
[Is] ISSN:1873-3468
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Mycofactocin is a putative, peptide derived, cofactor that is associated primarily with the Mycobacterium genera including the pathogen M. tuberculosis. The pathway consists of the three genes mftA, mftB, and mftC that encode for the peptide substrate, peptide chaperone, and a radical S-adenosylmethionine protein (RS), respectively. Here, we show that the MftB acts as a peptide chaperone, binding MftA with a submicromolar KD (~ 100 nm) and MftC with a low micromolar KD (~ 2 µm). Moreover, we demonstrate that MftC is a radical S-adenosylmethionine (SAM) enzyme. Finally, we show that MftC catalyzes the oxidative decarboxylation of the peptide MftA.
[Mh] Termos MeSH primário: Proteínas com Ferro-Enxofre/genética
Mycobacterium ulcerans/enzimologia
Proteína O-Metiltransferase/genética
S-Adenosilmetionina/metabolismo
[Mh] Termos MeSH secundário: Catálise
Seres Humanos
Proteínas com Ferro-Enxofre/química
Chaperonas Moleculares/química
Chaperonas Moleculares/genética
Mycobacterium tuberculosis/genética
Mycobacterium tuberculosis/patogenicidade
Mycobacterium ulcerans/química
Mycobacterium ulcerans/genética
Peptídeos/química
Peptídeos/genética
Ligação Proteica
Proteína O-Metiltransferase/química
S-Adenosilmetionina/química
Especificidade por Substrato
[Pt] Tipo de publicação:LETTER
[Nm] Nome de substância:
0 (Iron-Sulfur Proteins); 0 (Molecular Chaperones); 0 (Peptides); 7LP2MPO46S (S-Adenosylmethionine); EC 2.1.1.- (Protein O-Methyltransferase)
[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:160618
[St] Status:MEDLINE
[do] DOI:10.1002/1873-3468.12249


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[PMID]:26779826
[Au] Autor:Deng H; Gao R; Liao X; Cai Y
[Ad] Endereço:The Key Laboratory of Industrial Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, 1800 LihuRoad, Wuxi, Jiangsu 214122, China.
[Ti] Título:Reference genes selection and relative expression analysis from Shiraia sp. SUPER-H168 productive of hypocrellin.
[So] Source:Gene;580(1):67-72, 2016 Apr 10.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Shiraia bambusicola is an essential pharmaceutical fungus due to its production of hypocrellin with antiviral, antidepressant, and antiretroviral properties. Based on suitable reference gene (RG) normalization, gene expression analysis enables the exploitation of significant genes relative to hypocrellin biosynthesis by quantitative real-time polymerase chain reaction. We selected and assessed nine candidate RGs in the presence and absence of hypocrellin biosynthesis using GeNorm and NormFinder algorithms. After stepwise exclusion of unstable genes, GeNorm analysis identified glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and cytochrome oxidase (CyO) as the most stable expression, while NormFinder determined 18S ribosomal RNA (18S rRNA) as the most appropriate candidate gene for normalization. Tubulin (Tub) was observed to be the least stable gene and should be avoided for relative expression analysis. We further analyzed relative expression levels of essential proteins correlative with hypocrellin biosynthesis, including polyketide synthase (PKS), O-methyltransferase (Omef), FAD/FMN-dependent oxidoreductase (FAD), and monooxygenase (Mono). Compared to PKS, Mono kept a similar expression pattern and simulated PKS expression, while FAD remained constantly expressed. Omef presented lower transcript levels and had no relation to PKS expression. These relative expression analyses will pave the way for further interpretation of the hypocrellin biosynthesis pathway.
[Mh] Termos MeSH primário: Antivirais/metabolismo
Ascomicetos/genética
Perfilação da Expressão Gênica
Perileno/análogos & derivados
Quinonas/metabolismo
[Mh] Termos MeSH secundário: Complexo IV da Cadeia de Transporte de Elétrons/genética
Gliceraldeído-3-Fosfato Desidrogenases/genética
Oxigenases de Função Mista/genética
Perileno/metabolismo
Policetídeo Sintases/genética
Proteína O-Metiltransferase/genética
RNA Ribossômico 18S/genética
Reação em Cadeia da Polimerase em Tempo Real/métodos
Tubulina (Proteína)/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Antiviral Agents); 0 (Quinones); 0 (RNA, Ribosomal, 18S); 0 (Tubulin); 5QD5427UN7 (Perylene); 79956-01-7 (Polyketide Synthases); EC 1.- (Mixed Function Oxygenases); EC 1.2.1.- (Glyceraldehyde-3-Phosphate Dehydrogenases); EC 1.9.3.1 (Electron Transport Complex IV); EC 2.1.1.- (Protein O-Methyltransferase); V86371B0XS (hypocrellin A)
[Em] Mês de entrada:1606
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160119
[St] Status:MEDLINE


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[PMID]:26484916
[Au] Autor:Chu D; Tan J; Xie S; Jin N; Yin X; Gong CX; Iqbal K; Liu F
[Ad] Endereço:Jiangsu Key Laboratory of Neuroregeneration, Nantong University, Co-innovation Center of Neuroregeneration, Nantong, PR China.
[Ti] Título:GSK-3ß is Dephosphorylated by PP2A in a Leu309 Methylation-Independent Manner.
[So] Source:J Alzheimers Dis;49(2):365-75, 2016.
[Is] ISSN:1875-8908
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Hyperphosphorylation of tau is pivotally involved in the pathogenesis of Alzheimer's disease (AD) and related tauopathies. Glycogen synthase kinase-3ß (GSK-3ß) and protein phosphate 2A (PP2A) are crucial enzymes to regulate tau phosphorylation. GSK-3ß activity is regulated by its inhibitory phosphorylation at Ser9. We previously reported the cross-talk between GSK-3ß and PP2A signaling and showed that PP2A could dephosphorylate GSK-3ß at Ser9. Here, we investigated the dephosphorylation of GSK-3ß in brain extracts in the presence of phosphatase inhibitors and found that a PP2A-like phosphatase activity was required for dephosphorylation of GSK-3ß at Ser9. PP2A interacted with GSK-3ß and suppressed its Ser9 phosphorylation in vitro and in HEK-293FT cells. Activity of PP2A negatively correlated to the level of phosphorylated GSK-3ß in kainic acid-induced excitotoxic mouse brain. Alteration of methylation of the catalytic subunit of PP2A (PP2Ac) at Leu309 did not affect GSK-3ß phosphorylation. These findings suggest that Leu309 methylation is not required for PP2A to dephosphorylate GSK-3ß at Ser9.
[Mh] Termos MeSH primário: Quinase 3 da Glicogênio Sintase/metabolismo
Leucina/metabolismo
Proteína Fosfatase 2/metabolismo
[Mh] Termos MeSH secundário: Animais
Encéfalo/efeitos dos fármacos
Encéfalo/metabolismo
Hidrolases de Éster Carboxílico/metabolismo
Linhagem Celular Transformada
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/farmacologia
Agonistas de Aminoácidos Excitatórios/farmacologia
Quinase 3 da Glicogênio Sintase/genética
Glicogênio Sintase Quinase 3 beta
Seres Humanos
Ácido Caínico/farmacologia
Proteínas Luminescentes/genética
Proteínas Luminescentes/metabolismo
Masculino
Metilação/efeitos dos fármacos
Camundongos
Fosforilação/efeitos dos fármacos
Proteína O-Metiltransferase/metabolismo
Proteína Fosfatase 2/genética
RNA Interferente Pequeno/genética
RNA Interferente Pequeno/metabolismo
Serina/metabolismo
Proteínas tau/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Excitatory Amino Acid Agonists); 0 (Luminescent Proteins); 0 (RNA, Small Interfering); 0 (fluorescent protein 583); 0 (tau Proteins); 452VLY9402 (Serine); EC 2.1.1.- (Lcmt1 protein, mouse); EC 2.1.1.- (Protein O-Methyltransferase); EC 2.7.11.1 (GSK3B protein, human); EC 2.7.11.1 (Glycogen Synthase Kinase 3 beta); EC 2.7.11.1 (Gsk3b protein, mouse); EC 2.7.11.26 (Glycogen Synthase Kinase 3); EC 3.1.1.- (Carboxylic Ester Hydrolases); EC 3.1.1.- (protein phosphatase methylesterase-1); EC 3.1.3.16 (Protein Phosphatase 2); GMW67QNF9C (Leucine); SIV03811UC (Kainic Acid)
[Em] Mês de entrada:1609
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:151021
[St] Status:MEDLINE
[do] DOI:10.3233/JAD-150497


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[PMID]:26407870
[Au] Autor:Liu X; Luo Y; Wu H; Xi W; Yu J; Zhang Q; Zhou Z
[Ad] Endereço:College of Horticulture and Landscape Architecture, Southwest University, Chongqing 400715, China; Key Laboratory of Horticulture Science for Southern Mountainous Regions, Ministry of Education, Chongqing 400715, China; Post-doctoral Station of Horticulture, Southwest University, Chongqing 400715, C
[Ti] Título:Systematic analysis of O-methyltransferase gene family and identification of potential members involved in the formation of O-methylated flavonoids in Citrus.
[So] Source:Gene;575(2 Pt 2):458-472, 2016 Jan 10.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The O-methylation of various secondary metabolites is mainly catalyzed by S-adenosyl-l-methionine (SAM)-dependent O-methyltransferase (OMT) proteins that are encoded by the O-methyltransferase gene family. Citrus fruits are a rich source of O-methylated flavonoids that have a broad spectrum of biological activities, including anti-inflammatory, anticarcinogenic, and antiatherogenic properties. However, little is known about this gene family and its members that are involved in the O-methylation of flavonoids and their regulation in Citrus. In this study, 58 OMT genes were identified from the entire Citrus sinensis genome and compared with those from 3 other representative dicot plants. A comprehensive analysis was performed, including functional/substrate predictions, identification of chromosomal locations, phylogenetic relationships, gene structures, and conserved motifs. Distribution mapping revealed that the 58 OMT genes were unevenly distributed on the 9 citrus chromosomes. Phylogenetic analysis of 164 OMT proteins from C.sinensis, Arabidopsis thaliana, Populus trichocarpa, and Vitis vinifera showed that these proteins were categorized into group I (COMT subfamily) and group II (CCoAOMT subfamily), which were further divided into 10 and 2 subgroups, respectively. Finally, digital gene expression and quantitative real-time polymerase chain reaction analyses revealed that citrus OMT genes had distinct temporal and spatial expression patterns in different tissues and developmental stages. Interestingly, 18 and 11 of the 27 genes predicted to be involved in O-methylation of flavonoids had higher expression in the peel and pulp during fruit development, respectively. The citrus OMT gene family identified in this study might help in the selection of appropriate candidate genes and facilitate functional studies in Citrus.
[Mh] Termos MeSH primário: Citrus sinensis/enzimologia
Flavonoides/biossíntese
Proteína O-Metiltransferase/classificação
Proteína O-Metiltransferase/genética
[Mh] Termos MeSH secundário: Citrus sinensis/química
Citrus sinensis/genética
Flavonoides/química
Garcinia cambogia/química
Regulação da Expressão Gênica no Desenvolvimento
Regulação Enzimológica da Expressão Gênica
Genoma de Planta
Metilação
Família Multigênica
Especificidade de Órgãos
Filogenia
Proteínas de Plantas/classificação
Proteínas de Plantas/genética
Proteínas de Plantas/metabolismo
Proteína O-Metiltransferase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Flavonoids); 0 (Plant Proteins); EC 2.1.1.- (Protein O-Methyltransferase)
[Em] Mês de entrada:1603
[Cu] Atualização por classe:170728
[Lr] Data última revisão:
170728
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150927
[St] Status:MEDLINE


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[PMID]:25944273
[Au] Autor:Du Z; Zhou Y; Lu X; Li L; Lu C; Li L; Li B; Bu H; Yang J; Shi Y
[Ad] Endereço:Laboratory of Pathology, West China Hospital, Sichuan University, Chengdu, China.
[Ti] Título:Octreotide prevents liver failure through upregulating 5'-methylthioadenosine in extended hepatectomized rats.
[So] Source:Liver Int;36(2):212-22, 2016 Feb.
[Is] ISSN:1478-3231
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND & AIMS: Insufficient liver regeneration and hepatocyte injury caused by excessive portal perfusion are considered to be responsible for post-hepatectomy liver failure (PLF) or small-for-size syndrome in living-donor liver transplantation. Somatostatin can decrease portal vein pressure (PVP) but simultaneously inhibits liver regeneration. This interesting paradox motivated us to investigate the outcome of PLF in response to somatostatin treatment. METHODS: Rats receiving extended partial hepatectomy (90% PH) were treated with octreotide, a somatostatin analogue, or placebo. Animal survival, serum parameters and hepatic histology were evaluated. Metabolomic analysis was performed to investigate the effect of octreotide on hepatocyte metabolism. RESULTS: Despite significantly inhibiting early regeneration, octreotide application noticeably improved the hepatic histology, liver function and survival after PH but did not decrease the PVP level. Metabolomic analysis exhibited that octreotide profoundly and exclusively altered the levels of five metabolites that participate in or closely associate with the methionine cycle, a biochemical reaction that uniquely produces S-adenosylmethionine (SAMe), an active methyl residual donor for methyltransferase reactions. Among these metabolites, 5'-methylthioadenosine (MTA), a derivate of SAMe, increased three-fold and was found independently improve the hepatic histology and reduce inflammatory cytokines in hepatectomized rats. CONCLUSIONS: Octreotide exclusively regulates the methionine cycle reaction and augments the MTA level in hepatocytes. MTA prominently protects hepatocytes against shear stress injury and reduces the secondary inflammation, thereby protecting rats from PLF.
[Mh] Termos MeSH primário: Hepatectomia/efeitos adversos
Falência Hepática
Regeneração Hepática
Fígado
Octreotida
[Mh] Termos MeSH secundário: Animais
Desoxiadenosinas/metabolismo
Fármacos Gastrointestinais/administração & dosagem
Fármacos Gastrointestinais/farmacocinética
Fígado/metabolismo
Fígado/patologia
Falência Hepática/etiologia
Falência Hepática/metabolismo
Falência Hepática/patologia
Falência Hepática/prevenção & controle
Regeneração Hepática/efeitos dos fármacos
Regeneração Hepática/fisiologia
Masculino
Octreotida/administração & dosagem
Octreotida/farmacocinética
Substâncias Protetoras/administração & dosagem
Substâncias Protetoras/farmacocinética
Proteína O-Metiltransferase/antagonistas & inibidores
Ratos
Tionucleosídeos/metabolismo
Resultado do Tratamento
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Deoxyadenosines); 0 (Gastrointestinal Agents); 0 (Protective Agents); 0 (Thionucleosides); 634Z2VK3UQ (5'-methylthioadenosine); EC 2.1.1.- (Protein O-Methyltransferase); RWM8CCW8GP (Octreotide)
[Em] Mês de entrada:1610
[Cu] Atualização por classe:161230
[Lr] Data última revisão:
161230
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150507
[St] Status:MEDLINE
[do] DOI:10.1111/liv.12863



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