Base de dados : MEDLINE
Pesquisa : D08.811.277.352.650 [Categoria DeCS]
Referências encontradas : 15102 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 1511 ir para página                         

  1 / 15102 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28461450
[Au] Autor:Rothstein DM; Lazinski D; Osburne MS; Sonenshein AL
[Ad] Endereço:Graduate Program in Molecular Biology, Tufts University School of Medicine, Boston, Massachusetts, USA.
[Ti] Título:A Mutation in the Bacillus subtilis rsbU Gene That Limits RNA Synthesis during Sporulation.
[So] Source:J Bacteriol;199(14), 2017 07 15.
[Is] ISSN:1098-5530
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mutants of that are temperature sensitive for RNA synthesis during sporulation were isolated after selection with a P suicide agent. Whole-genome sequencing revealed that two of the mutants carried an identical lesion in the gene, which encodes a phosphatase that indirectly activates SigB, the stress-responsive RNA polymerase sigma factor. The mutation appeared to cause RsbU to be hyperactive, because the mutants were more resistant than the parent strain to ethanol stress. In support of this hypothesis, pseudorevertants that regained wild-type levels of sporulation at high temperature had secondary mutations that prevented expression of the mutant gene. The properties of these RsbU mutants support the idea that activation of SigB diminishes the bacterium's ability to sporulate. Most bacterial species encode multiple RNA polymerase promoter recognition subunits (sigma factors). Each sigma factor directs RNA polymerase to different sets of genes; each gene set typically encodes proteins important for responses to specific environmental conditions, such as changes in temperature, salt concentration, and nutrient availability. A selection for mutants of that are temperature sensitive for RNA synthesis during sporulation unexpectedly yielded strains with a point mutation in , a gene that encodes a protein that normally activates sigma factor B (SigB) under conditions of salt stress. The mutation appears to cause RsbU, and therefore SigB, to be active inappropriately, thereby inhibiting, directly or indirectly, the ability of the cells to transcribe sporulation genes.
[Mh] Termos MeSH primário: Bacillus subtilis/metabolismo
Proteínas de Bactérias/metabolismo
Regulação Bacteriana da Expressão Gênica/fisiologia
Monoéster Fosfórico Hidrolases/metabolismo
RNA Bacteriano/biossíntese
Esporos Bacterianos/fisiologia
[Mh] Termos MeSH secundário: Bacillus subtilis/genética
Proteínas de Bactérias/genética
Etanol/farmacologia
Genoma Bacteriano
Temperatura Alta
Mutação
Fosfatos/metabolismo
Monoéster Fosfórico Hidrolases/genética
Radioisótopos de Fósforo
Estresse Fisiológico/efeitos dos fármacos
Estresse Fisiológico/efeitos da radiação
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Phosphates); 0 (Phosphorus Radioisotopes); 0 (RNA, Bacterial); 3K9958V90M (Ethanol); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.1.3.3 (RsbU protein, Bacillus subtilis)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:180306
[Lr] Data última revisão:
180306
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170503
[St] Status:MEDLINE


  2 / 15102 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29360855
[Au] Autor:Carrillo JB; Gomez-Casati DF; Martín M; Busi MV
[Ad] Endereço:Centro de Estudios Fotosintéticos y Bioquímicos (CEFOBI-CONICET), Universidad Nacional de Rosario, Rosario, Santa Fe, Argentina.
[Ti] Título:Identification and analysis of OsttaDSP, a phosphoglucan phosphatase from Ostreococcus tauri.
[So] Source:PLoS One;13(1):e0191621, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ostreococcus tauri, the smallest free-living (non-symbiotic) eukaryote yet described, is a unicellular green alga of the Prasinophyceae family. It has a very simple cellular organization and presents a unique starch granule and chloroplast. However, its starch metabolism exhibits a complexity comparable to higher plants, with multiple enzyme forms for each metabolic reaction. Glucan phosphatases, a family of enzymes functionally conserved in animals and plants, are essential for normal starch or glycogen degradation in plants and mammals, respectively. Despite the importance of O. tauri microalgae in evolution, there is no information available concerning the enzymes involved in reversible phosphorylation of starch. Here, we report the molecular cloning and heterologous expression of the gene coding for a dual specific phosphatase from O. tauri (OsttaDSP), homologous to Arabidopsis thaliana LSF2. The recombinant enzyme was purified to electrophoretic homogeneity to characterize its oligomeric and kinetic properties accurately. OsttaDSP is a homodimer of 54.5 kDa that binds and dephosphorylates amylopectin. Also, we also determined that residue C162 is involved in catalysis and possibly also in structural stability of the enzyme. Our results could contribute to better understand the role of glucan phosphatases in the metabolism of starch in green algae.
[Mh] Termos MeSH primário: Clorófitas/enzimologia
Glucanos/metabolismo
Monoéster Fosfórico Hidrolases/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Clonagem Molecular
Dimerização
Cinética
Monoéster Fosfórico Hidrolases/química
Monoéster Fosfórico Hidrolases/genética
Fosforilação
Conformação Proteica
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Glucans); 0 (Recombinant Proteins); EC 3.1.3.2 (Phosphoric Monoester Hydrolases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180226
[Lr] Data última revisão:
180226
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180124
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191621


  3 / 15102 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29248581
[Au] Autor:Zhang T; Hou L; Chen DT; McMahon FJ; Wang JC; Rice JP
[Ad] Endereço:Department of Epidemiology and Biostatistics, School of Public Health, Xi'an Jiaotong University, Shaanxi, China.
[Ti] Título:Exome sequencing of a large family identifies potential candidate genes contributing risk to bipolar disorder.
[So] Source:Gene;645:119-123, 2018 Mar 01.
[Is] ISSN:1879-0038
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Bipolar disorder is a mental illness with lifetime prevalence of about 1%. Previous genetic studies have identified multiple chromosomal linkage regions and candidate genes that might be associated with bipolar disorder. The present study aimed to identify potential susceptibility variants for bipolar disorder using 6 related case samples from a four-generation family. A combination of exome sequencing and linkage analysis was performed to identify potential susceptibility variants for bipolar disorder. Our study identified a list of five potential candidate genes for bipolar disorder. Among these five genes, GRID1(Glutamate Receptor Delta-1 Subunit), which was previously reported to be associated with several psychiatric disorders and brain related traits, is particularly interesting. Variants with functional significance in this gene were identified from two cousins in our bipolar disorder pedigree. Our findings suggest a potential role for these genes and the related rare variants in the onset and development of bipolar disorder in this one family. Additional research is needed to replicate these findings and evaluate their patho-biological significance.
[Mh] Termos MeSH primário: Transtorno Bipolar/genética
Polimorfismo de Nucleotídeo Único
Sequenciamento Completo do Exoma/métodos
[Mh] Termos MeSH secundário: Caderinas/genética
Feminino
Redes Reguladoras de Genes
Ligação Genética
Predisposição Genética para Doença
Seres Humanos
Masculino
Proteínas do Tecido Nervoso/genética
Linhagem
Monoéster Fosfórico Hidrolases/genética
Receptores de Glutamato/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (CDHR1 protein, human); 0 (Cadherins); 0 (Nerve Tissue Proteins); 0 (Receptors, Glutamate); 0 (glutamate receptor delta 1); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.1.3.62 (multiple inositol-polyphosphate phosphatase)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180203
[Lr] Data última revisão:
180203
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171218
[St] Status:MEDLINE


  4 / 15102 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29235319
[Au] Autor:Toptikov VA; Totsky VN; Alieksieieva TG; Kovtun OA
[Ti] Título:Hydrolytic enzymes expressivity in different parts of the Rapana digestive system.
[So] Source:Ukr Biochem J;88(3):5-17, 2016 May-Jun.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:The relevance of comprehensive studies of the Rapana vital functions is determined by its considerab­le negative impact on the ecosystem of the Black Sea. The aim of the work was to find out the polymorphism and activity of the main hydrolases in the different parts of the digestive system of Rapana. Hydrolases (proteases, amylases, esterases, lipases and phosphatases) in glandular structures of the Rapana digestive system were studied by electrophoresis. It was found that different sets of hydrolytic enzymes are functioning in certain parts of the Rapana digestive tract. The gland of Leiblein and hepatopancreas played the most important role in the digestion of food components. The salivary glands had the significant influence on proteolysis.
[Mh] Termos MeSH primário: Mucosa Gástrica/enzimologia
Gastrópodes/enzimologia
Expressão Gênica
Hepatopâncreas/enzimologia
Espécies Introduzidas
Glândulas Salivares/enzimologia
[Mh] Termos MeSH secundário: Amilases/classificação
Amilases/genética
Amilases/metabolismo
Animais
Mar Negro
Ensaios Enzimáticos
Esterases/classificação
Esterases/genética
Esterases/metabolismo
Gastrópodes/genética
Lipase/classificação
Lipase/genética
Lipase/metabolismo
Peptídeo Hidrolases/classificação
Peptídeo Hidrolases/genética
Peptídeo Hidrolases/metabolismo
Monoéster Fosfórico Hidrolases/classificação
Monoéster Fosfórico Hidrolases/genética
Monoéster Fosfórico Hidrolases/metabolismo
Comportamento Predatório/fisiologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.1.- (Esterases); EC 3.1.1.3 (Lipase); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.2.1.- (Amylases); EC 3.4.- (Peptide Hydrolases)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180116
[Lr] Data última revisão:
180116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171214
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.03.005


  5 / 15102 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28470336
[Au] Autor:Otori K; Tanabe N; Maruyama T; Sato S; Yanagisawa S; Tamoi M; Shigeoka S
[Ad] Endereço:Department of Advanced Bioscience, Faculty of Agriculture, Kindai University, Nakamachi, Nara, 631-8505, Japan.
[Ti] Título:Enhanced photosynthetic capacity increases nitrogen metabolism through the coordinated regulation of carbon and nitrogen assimilation in Arabidopsis thaliana.
[So] Source:J Plant Res;130(5):909-927, 2017 Sep.
[Is] ISSN:1618-0860
[Cp] País de publicação:Japan
[La] Idioma:eng
[Ab] Resumo:Plant growth and productivity depend on interactions between the metabolism of carbon and nitrogen. The sensing ability of internal carbon and nitrogen metabolites (the C/N balance) enables plants to regulate metabolism and development. In order to investigate the effects of an enhanced photosynthetic capacity on the metabolism of carbon and nitrogen in photosynthetically active tissus (source leaves), we herein generated transgenic Arabidopsis thaliana plants (ApFS) that expressed cyanobacterial fructose-1,6-/sedoheptulose-1,7-bisphosphatase in their chloroplasts. The phenotype of ApFS plants was indistinguishable from that of wild-type plants at the immature stage. However, as plants matured, the growth of ApFS plants was superior to that of wild-type plants. Starch levels were higher in ApFS plants than in wild-type plants at 2 and 5 weeks. Sucrose levels were also higher in ApFS plants than in wild-type plants, but only at 5 weeks. On the other hand, the contents of various free amino acids were lower in ApFS plants than in wild-type plants at 2 weeks, but were similar at 5 weeks. The total C/N ratio was the same in ApFS plants and wild-type plants, whereas nitrite levels increased in parallel with elevations in nitrate reductase activity at 5 weeks in ApFS plants. These results suggest that increases in the contents of photosynthetic intermediates at the early growth stage caused a temporary imbalance in the free-C/free-N ratio and, thus, the feedback inhibition of the expression of genes involved in the Calvin cycle and induction of the expression of those involved in nitrogen metabolism due to supply deficient free amino acids for maintenance of the C/N balance in source leaves of ApFS plants.
[Mh] Termos MeSH primário: Arabidopsis/fisiologia
Carbono/metabolismo
Nitrogênio/metabolismo
Fotossíntese
[Mh] Termos MeSH secundário: Arabidopsis/genética
Arabidopsis/crescimento & desenvolvimento
Proteínas de Arabidopsis/genética
Proteínas de Arabidopsis/metabolismo
Cloroplastos/enzimologia
Frutose-Bifosfatase/genética
Frutose-Bifosfatase/metabolismo
Fenótipo
Monoéster Fosfórico Hidrolases/genética
Monoéster Fosfórico Hidrolases/metabolismo
Plantas Geneticamente Modificadas
Amido/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 7440-44-0 (Carbon); 9005-25-8 (Starch); EC 3.1.3.11 (Fructose-Bisphosphatase); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.1.3.37 (sedoheptulose-bisphosphatase); N762921K75 (Nitrogen)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171228
[Lr] Data última revisão:
171228
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1007/s10265-017-0950-4


  6 / 15102 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29034772
[Au] Autor:Kim TW; Lee SJ; Park YJ; Park SY; Oh BM; Park YS; Kim BY; Lee YH; Cho HJ; Yoon SR; Choe YK; Lee HG
[Ad] Endereço:1 Immunotherapy Convergence Research Group, Korea Research Institute of Bioscience & Biotechnology, Daejeon, Republic of Korea.
[Ti] Título:Opa-interacting protein 5 modulates docetaxel-induced cell death via regulation of mitophagy in gastric cancer.
[So] Source:Tumour Biol;39(10):1010428317733985, 2017 Oct.
[Is] ISSN:1423-0380
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Damage to mitochondria induces mitophagy, a cellular process that is gaining interest for its therapeutic relevance to a variety of human diseases. However, the mechanism underlying mitochondrial depolarization and clearance in mitophagy remains poorly understood. We previously reported that mitochondria-induced cell death was caused by knockdown of Neisseria gonorrhoeae opacity-associated-interacting protein 5 in gastric cancer. In this study, we show that Neisseria gonorrhoeae opacity-associated-interacting protein 5 loss and gain of function modulates mitophagy induced by treatment with docetaxel, a chemotherapy drug for gastric cancer. The activation of mitophagy by Neisseria gonorrhoeae opacity-associated-interacting protein 5 overexpression promoted cell survival, preventing docetaxel-induced mitochondrial clearance. Conversely, short interfering RNA-mediated knockdown of Neisseria gonorrhoeae opacity-associated-interacting protein 5 accelerated docetaxel-induced apoptosis while increasing mitochondrial depolarization, reactive oxygen species, and endoplasmic reticulum stress and decreasing adenosine triphosphate production. We also found that the mitochondrial outer membrane proteins mitofusin 2 and phosphatase and tensin homolog-induced putative kinase 1 colocalized with Neisseria gonorrhoeae opacity-associated-interacting protein 5 in mitochondria and that mitofusin 2 knockdown altered Neisseria gonorrhoeae opacity-associated-interacting protein 5 expression. These findings indicate that Neisseria gonorrhoeae opacity-associated-interacting protein 5 modulates docetaxel-induced mitophagic cell death and therefore suggest that this protein comprises a potential therapeutic target for gastric cancer treatment.
[Mh] Termos MeSH primário: Morte Celular/efeitos dos fármacos
Proteínas Cromossômicas não Histona/metabolismo
Mitocôndrias/metabolismo
Degradação Mitocondrial/fisiologia
Neoplasias Gástricas/metabolismo
Taxoides/farmacologia
[Mh] Termos MeSH secundário: Apoptose/efeitos dos fármacos
Apoptose/fisiologia
Linhagem Celular Tumoral
Sobrevivência Celular/efeitos dos fármacos
Sobrevivência Celular/fisiologia
GTP Fosfo-Hidrolases/metabolismo
Seres Humanos
Mitocôndrias/efeitos dos fármacos
Degradação Mitocondrial/efeitos dos fármacos
Proteínas Mitocondriais/metabolismo
Neisseria gonorrhoeae/metabolismo
Monoéster Fosfórico Hidrolases/metabolismo
RNA Interferente Pequeno/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Tensinas/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Chromosomal Proteins, Non-Histone); 0 (Mitochondrial Proteins); 0 (OIP5 protein, human); 0 (RNA, Small Interfering); 0 (Reactive Oxygen Species); 0 (Taxoids); 0 (Tensins); 15H5577CQD (docetaxel); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.6.1.- (GTP Phosphohydrolases); EC 3.6.1.- (MFN2 protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171020
[Lr] Data última revisão:
171020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171017
[St] Status:MEDLINE
[do] DOI:10.1177/1010428317733985


  7 / 15102 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:29028801
[Au] Autor:Del Signore SJ; Biber SA; Lehmann KS; Heimler SR; Rosenfeld BH; Eskin TL; Sweeney ST; Rodal AA
[Ad] Endereço:Rosenstiel Basic Medical Sciences Research Center, Department of Biology, Brandeis University, Waltham, Massachusetts, United States of America.
[Ti] Título:dOCRL maintains immune cell quiescence by regulating endosomal traffic.
[So] Source:PLoS Genet;13(10):e1007052, 2017 Oct.
[Is] ISSN:1553-7404
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Lowe Syndrome is a developmental disorder characterized by eye, kidney, and neurological pathologies, and is caused by mutations in the phosphatidylinositol-5-phosphatase OCRL. OCRL plays diverse roles in endocytic and endolysosomal trafficking, cytokinesis, and ciliogenesis, but it is unclear which of these cellular functions underlie specific patient symptoms. Here, we show that mutation of Drosophila OCRL causes cell-autonomous activation of hemocytes, which are macrophage-like cells of the innate immune system. Among many cell biological defects that we identified in docrl mutant hemocytes, we pinpointed the cause of innate immune cell activation to reduced Rab11-dependent recycling traffic and concomitantly increased Rab7-dependent late endosome traffic. Loss of docrl amplifies multiple immune-relevant signals, including Toll, Jun kinase, and STAT, and leads to Rab11-sensitive mis-sorting and excessive secretion of the Toll ligand Spåtzle. Thus, docrl regulation of endosomal traffic maintains hemocytes in a poised, but quiescent state, suggesting mechanisms by which endosomal misregulation of signaling may contribute to symptoms of Lowe syndrome.
[Mh] Termos MeSH primário: Citocinese/genética
Imunidade Inata/genética
Síndrome Oculocerebrorrenal/genética
Monoéster Fosfórico Hidrolases/genética
[Mh] Termos MeSH secundário: Animais
Drosophila
Endossomos/genética
Endossomos/patologia
Hemócitos/metabolismo
Hemócitos/patologia
Seres Humanos
Mutação
Síndrome Oculocerebrorrenal/patologia
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.1.3.36 (OCRL protein, human)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171111
[Lr] Data última revisão:
171111
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171014
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007052


  8 / 15102 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:28982866
[Au] Autor:Sung JY; Na K; Kim HS
[Ad] Endereço:Department of Pathology, Kyung Hee University School of Medicine, Seoul, Republic of Korea.
[Ti] Título:Down-regulation of Inositol Polyphosphate 4-Phosphatase Type II Expression in Colorectal Carcinoma.
[So] Source:Anticancer Res;37(10):5525-5531, 2017 10.
[Is] ISSN:1791-7530
[Cp] País de publicação:Greece
[La] Idioma:eng
[Ab] Resumo:BACKGROUND/AIM: Aberrant expression of survival signaling pathways causes deregulation of cellular proliferation and resistance to apoptosis, and plays a crucial role in the development, progression and metastasis of cancer. Inositol polyphosphate 4-phosphatase type II (INPP4B) negatively regulates phosphatidylinositol 3-kinase signaling and has a tumor-suppressive role in several human malignancies. MATERIALS AND METHODS: We analyzed the expression levels of INPP4B mRNA and protein in colorectal carcinoma (CRC) cell lines and tissue samples using western blot, quantitative real-time reverse-transcriptase polymerase chain reaction, and immunohistochemical staining. RESULTS: Western blot analysis revealed that the CRC cell lines HCT 116, SW620, DLD-1, and WiDr expressed significantly lower levels of INPP4B protein than the normal colonic epithelial cell lines CCD 841 CoTr and FHC. Consistent with these results, INPP4B mRNA expression in the CRC cell lines was significantly lower than in the normal colonic epithelial cells. Immunohistochemical staining revealed that normal colonic mucosa displayed uniform and strong-to-moderate INPP4B immunoreactivity, whereas 60.7% (71/117; p<0.001) and 76.5% (62/81; p<0.001) of the primary and metastatic CRC tissue samples exhibited reduced INPP4B expression, respectively. CONCLUSION: Our results indicate that INPP4B is down-regulated in CRC and that INPP4B is involved in the development and progression of CRC.
[Mh] Termos MeSH primário: Adenocarcinoma/enzimologia
Neoplasias Colorretais/enzimologia
Monoéster Fosfórico Hidrolases/metabolismo
[Mh] Termos MeSH secundário: Adenocarcinoma/genética
Adenocarcinoma/patologia
Neoplasias Colorretais/genética
Neoplasias Colorretais/patologia
Regulação para Baixo
Regulação Enzimológica da Expressão Gênica
Regulação Neoplásica da Expressão Gênica
Células HCT116
Seres Humanos
Monoéster Fosfórico Hidrolases/genética
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (RNA, Messenger); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.1.3.66 (phosphatidylinositol-3,4-bisphosphate 4-phosphatase)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171007
[St] Status:MEDLINE


  9 / 15102 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28947610
[Au] Autor:VerPlank JJS; Goldberg AL
[Ad] Endereço:Harvard Medical School, Boston, MA 02115, U.S.A.
[Ti] Título:Regulating protein breakdown through proteasome phosphorylation.
[So] Source:Biochem J;474(19):3355-3371, 2017 Sep 24.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The ubiquitin proteasome system degrades the great majority of proteins in mammalian cells. Countless studies have described how ubiquitination promotes the selective degradation of different cell proteins. However, there is a small but the growing literature that protein half-lives can also be regulated by post-translational modifications of the 26S proteasome. The present study reviews the ability of several kinases to alter proteasome function through subunit phosphorylation. For example, PKA (protein kinase A) and DYRK2 (dual-specificity tyrosine-regulated kinase 2) stimulate the proteasome's ability to degrade ubiquitinated proteins, peptides, and adenosine triphosphate, while one kinase, ASK1 (apoptosis signal-regulating kinase 1), inhibits proteasome function during apoptosis. Proteasome phosphorylation is likely to be important in regulating protein degradation because it occurs downstream from many hormones and neurotransmitters, in conditions that raise cyclic adenosine monophosphate or cyclic guanosine monophosphate levels, after calcium influx following synaptic depolarization, and during phases of the cell cycle. Beyond its physiological importance, pharmacological manipulation of proteasome phosphorylation has the potential to combat various diseases. Inhibitors of phosphodiesterases by activating PKA or PKG (protein kinase G) can stimulate proteasomal degradation of misfolded proteins that cause neurodegenerative or myocardial diseases and even reduce the associated pathology in mouse models. These observations are promising since in many proteotoxic diseases, aggregation-prone proteins impair proteasome function, and disrupt protein homeostasis. Conversely, preventing subunit phosphorylation by DYRK2 slows cell cycle progression and tumor growth. However, further research is essential to determine how phosphorylation of different subunits by these (or other) kinases alters the properties of this complex molecular machine and thus influence protein degradation rates.
[Mh] Termos MeSH primário: Complexo de Endopeptidases do Proteassoma/metabolismo
Proteínas/metabolismo
[Mh] Termos MeSH secundário: Animais
Apoptose
AMP Cíclico/metabolismo
Proteínas Quinases Dependentes de AMP Cíclico/metabolismo
Proteínas Quinases Dependentes de GMP Cíclico/metabolismo
Seres Humanos
Neurônios/metabolismo
Monoéster Fosfórico Hidrolases/metabolismo
Fosforilação
Processamento de Proteína Pós-Traducional
Proteólise
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Proteins); E0399OZS9N (Cyclic AMP); EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases); EC 2.7.11.12 (Cyclic GMP-Dependent Protein Kinases); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.4.25.1 (Proteasome Endopeptidase Complex)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171003
[Lr] Data última revisão:
171003
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170927
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20160809


  10 / 15102 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28942147
[Au] Autor:Angkawijaya AE; Nakamura Y
[Ad] Endereço:Institute of Plant and Microbial Biology, Academia Sinica, 128 sec.2, Academia Rd., Nankang, Taipei 11529, Taiwan.
[Ti] Título:Arabidopsis PECP1 and PS2 are phosphate starvation-inducible phosphocholine phosphatases.
[So] Source:Biochem Biophys Res Commun;494(1-2):397-401, 2017 Dec 09.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Phosphate-starved plants reduce phosphatidylcholine content presumably to provide an internal phosphate source while replacing membrane phospholipids by galactolipids, a process termed membrane lipid remodeling. However, whether the metabolic fate of released phosphocholine is a phosphate source remains elusive because primary phosphocholine phosphatases in vivo are unknown in seed plants. Here, we show that PECP1 and PS2 are the primary phosphocholine phosphatases in Arabidopsis and function redundantly under phosphate starvation. Under phosphate starvation, the double knockout mutant of PECP1 and PS2 showed reduced content of choline but no severe growth phenotype, which suggests that phosphocholine dephosphorylation is not likely a major source of internal phosphate reserve. We identified primary phosphocholine phosphatases, demonstrated their involvement under phosphate starvation, and updated the metabolic map of membrane lipid remodeling.
[Mh] Termos MeSH primário: Arabidopsis/genética
Fosfatos/deficiência
Fosfatidilcolinas/metabolismo
Monoéster Fosfórico Hidrolases/genética
Sementes/genética
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Arabidopsis/enzimologia
Membrana Celular/metabolismo
Deleção de Genes
Regulação da Expressão Gênica de Plantas
Metabolismo dos Lipídeos
Lipídeos de Membrana/metabolismo
Monoéster Fosfórico Hidrolases/metabolismo
Sementes/enzimologia
Alinhamento de Sequência
Homologia de Sequência de Aminoácidos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Lipids); 0 (Phosphates); 0 (Phosphatidylcholines); EC 3.1.3.- (PECP1 protein, Arabidopsis); EC 3.1.3.- (phosphocholine phosphatase); EC 3.1.3.2 (Phosphoric Monoester Hydrolases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171108
[Lr] Data última revisão:
171108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170925
[St] Status:MEDLINE



página 1 de 1511 ir para página                         
   


Refinar a pesquisa
  Base de dados : MEDLINE Formulário avançado   

    Pesquisar no campo  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/OPAS/OMS - Centro Latino-Americano e do Caribe de Informação em Ciências da Saúde