Base de dados : MEDLINE
Pesquisa : D12.776.543.512.249.500.750.500 [Categoria DeCS]
Referências encontradas : 1496 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 150 ir para página                         

  1 / 1496 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28450105
[Au] Autor:Rosen O; Feldberg L; Dor E; Gura S; Zichel R
[Ad] Endereço:Department of Biotechnology, Israel Institute for Biological Research, Israel.
[Ti] Título:Optimization of SNAP-25-derived peptide substrate for improved detection of botulinum A in the Endopep-MS assay.
[So] Source:Anal Biochem;528:34-37, 2017 07 01.
[Is] ISSN:1096-0309
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Botulinum neurotoxins (BoNTs) are the most toxic proteins in nature. Endopeptidase-mass-spectrometry (Endopep-MS) is used as a specific and rapid in-vitro assay to detect BoNTs. In this assay, immunocaptured toxin cleaves a serotype-specific-peptide-substrate, and the cleavage products are then detected by MS. Here we describe the design of a new peptide substrate for improved detection of BoNT type A (BoNT/A). Our strategy was based on reported BoNT/A-SNAP-25 interactions integrated with analysis method efficiency considerations. Integration of the newly designed substrate led to a 10-fold increase in the assay sensitivity both in buffer and in clinically relevant samples.
[Mh] Termos MeSH primário: Toxinas Botulínicas Tipo A/análise
Espectrometria de Massas/métodos
Peptídeos/análise
Proteína 25 Associada a Sinaptossoma/química
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Toxinas Botulínicas Tipo A/imunologia
Endopeptidases/metabolismo
Seres Humanos
Peptídeos/química
Ligação Proteica
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Peptides); 0 (Synaptosomal-Associated Protein 25); EC 3.4.- (Endopeptidases); EC 3.4.24.69 (Botulinum Toxins, Type A)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:180207
[Lr] Data última revisão:
180207
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170429
[St] Status:MEDLINE


  2 / 1496 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28456331
[Au] Autor:Zdanowicz R; Kreutzberger A; Liang B; Kiessling V; Tamm LK; Cafiso DS
[Ad] Endereço:Department of Chemistry, University of Virginia, Charlottesville, Virginia; Center for Membrane and Cell Physiology, University of Virginia, Charlottesville, Virginia.
[Ti] Título:Complexin Binding to Membranes and Acceptor t-SNAREs Explains Its Clamping Effect on Fusion.
[So] Source:Biophys J;113(6):1235-1250, 2017 Sep 19.
[Is] ISSN:1542-0086
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Complexin-1 is a SNARE effector protein that decreases spontaneous neurotransmitter release and enhances evoked release. Complexin binds to the fully assembled four-helical neuronal SNARE core complex as revealed in competing molecular models derived from x-ray crystallography. Presently, it is unclear how complexin binding to the postfusion complex accounts for its effects upon spontaneous and evoked release in vivo. Using a combination of spectroscopic and imaging methods, we characterize in molecular detail how complexin binds to the 1:1 plasma membrane t-SNARE complex of syntaxin-1a and SNAP-25 while simultaneously binding the lipid bilayer at both its N- and C-terminal ends. These interactions are cooperative, and binding to the prefusion acceptor t-SNARE complex is stronger than to the postfusion core complex. This complexin interaction reduces the affinity of synaptobrevin-2 for the 1:1 complex, thereby retarding SNARE assembly and vesicle docking in vitro. The results provide the basis for molecular models that account for the observed clamping effect of complexin beginning with the acceptor t-SNARE complex and the subsequent activation of the clamped complex by Ca and synaptotagmin.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transporte Vesicular/metabolismo
Bicamadas Lipídicas/metabolismo
Proteínas do Tecido Nervoso/metabolismo
Proteína 25 Associada a Sinaptossoma/metabolismo
Sintaxina 1/metabolismo
Proteína 2 Associada à Membrana da Vesícula/metabolismo
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transporte Vesicular/química
Proteínas Adaptadoras de Transporte Vesicular/genética
Animais
Escherichia coli
Bicamadas Lipídicas/química
Lipossomos/química
Lipossomos/metabolismo
Mutação
Proteínas do Tecido Nervoso/química
Proteínas do Tecido Nervoso/genética
Fosfatidilcolinas/química
Fosfatidilserinas/química
Ligação Proteica
Ratos
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
Propriedades de Superfície
Proteína 25 Associada a Sinaptossoma/química
Sintaxina 1/química
Proteína 2 Associada à Membrana da Vesícula/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Vesicular Transport); 0 (Lipid Bilayers); 0 (Liposomes); 0 (Nerve Tissue Proteins); 0 (Phosphatidylcholines); 0 (Phosphatidylserines); 0 (Recombinant Proteins); 0 (Snap25 protein, rat); 0 (Synaptosomal-Associated Protein 25); 0 (Syntaxin 1); 0 (Vamp2 protein, rat); 0 (Vesicle-Associated Membrane Protein 2); 0 (complexin I); 40290-44-6 (1-palmitoyl-2-oleoylglycero-3-phosphoserine); TE895536Y5 (1-palmitoyl-2-oleoylphosphatidylcholine)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171212
[Lr] Data última revisão:
171212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170501
[St] Status:MEDLINE


  3 / 1496 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28972123
[Au] Autor:Houenou J; Boisgontier J; Henrion A; d'Albis MA; Dumaine A; Linke J; Wessa M; Daban C; Hamdani N; Delavest M; Llorca PM; Lançon C; Schürhoff F; Szöke A; Le Corvoisier P; Barau C; Poupon C; Etain B; Leboyer M; Jamain S
[Ad] Endereço:INSERM U955, Institut Mondor de Recherches Biomédicales, Psychiatrie Translationnelle, F-94000 Créteil, France.
[Ti] Título:A Multilevel Functional Study of a At-Risk Variant for Bipolar Disorder and Schizophrenia.
[So] Source:J Neurosci;37(43):10389-10397, 2017 Oct 25.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The synaptosomal-associated protein SNAP25 is a key player in synaptic vesicle docking and fusion and has been associated with multiple psychiatric conditions, including schizophrenia, bipolar disorder, and attention-deficit/hyperactivity disorder. We recently identified a promoter variant in , , that is associated with early-onset bipolar disorder and a higher gene expression level in human prefrontal cortex. In the current study, we showed that this variant was associated both in males and females with schizophrenia in two independent cohorts. We then combined and approaches in humans to understand the functional impact of the at-risk allele. Thus, we showed that the C allele was sufficient to increase the transcription level. In a postmortem expression analysis of 33 individuals affected with schizophrenia and 30 unaffected control subjects, we showed that the / ratio was increased in schizophrenic patients carrying the at-risk allele. Last, using genetics imaging in a cohort of 71 subjects, we showed that male risk carriers had an increased amygdala-ventromedial prefrontal cortex functional connectivity and a larger amygdala than non-risk carriers. The latter association has been replicated in an independent cohort of 121 independent subjects. Altogether, results from these multilevel functional studies are bringing strong evidence for the functional consequences of this allelic variation of on modulating the development and plasticity of the prefrontal-limbic network, which therefore may increase the vulnerability to both early-onset bipolar disorder and schizophrenia. Functional characterization of disease-associated variants is a key challenge in understanding neuropsychiatric disorders and will open an avenue in the development of personalized treatments. Recent studies have accumulated evidence that the SNARE complex, and more specifically the SNAP25 protein, may be involved in psychiatric disorders. Here, our multilevel functional studies are bringing strong evidence for the functional consequences of an allelic variation of on modulating the development and plasticity of the prefrontal-limbic network. These results demonstrate a common genetically driven functional alteration of a synaptic mechanism both in schizophrenia and early-onset bipolar disorder and confirm the shared genetic vulnerability between these two disorders.
[Mh] Termos MeSH primário: Transtorno Bipolar/genética
Predisposição Genética para Doença/genética
Variação Genética/genética
Esquizofrenia/genética
Proteína 25 Associada a Sinaptossoma/genética
[Mh] Termos MeSH secundário: Adulto
Animais
Transtorno Bipolar/diagnóstico por imagem
Linhagem Celular Tumoral
Feminino
Seres Humanos
Sistema Límbico/diagnóstico por imagem
Imagem por Ressonância Magnética/métodos
Masculino
Camundongos
Meia-Idade
Rede Nervosa/diagnóstico por imagem
Córtex Pré-Frontal/diagnóstico por imagem
Esquizofrenia/diagnóstico por imagem
Adulto Jovem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (SNAP25 protein, human); 0 (Synaptosomal-Associated Protein 25)
[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:171004
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.1040-17.2017


  4 / 1496 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28882895
[Au] Autor:Lemonidis K; MacLeod R; Baillie GS; Chamberlain LH
[Ad] Endereço:From The Strathclyde Institute of Pharmacy and Biomedical Sciences, 161 Cathedral Street, University of Strathclyde, Glasgow G4 0RE and kimon.lemonidis@strath.ac.uk.
[Ti] Título:Peptide array-based screening reveals a large number of proteins interacting with the ankyrin-repeat domain of the zDHHC17 -acyltransferase.
[So] Source:J Biol Chem;292(42):17190-17202, 2017 Oct 20.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:zDHHC -acyltransferases are enzymes catalyzing protein -acylation, a common post-translational modification on proteins frequently affecting their membrane targeting and trafficking. The ankyrin repeat (AR) domain of zDHHC17 (HIP14) and zDHHC13 (HIP14L) -acyltransferases, which is involved in both substrate recruitment and -acylation-independent functions, was recently shown to bind at least six proteins, by specific recognition of a consensus sequence in them. To further refine the rules governing binding to the AR of zDHHC17, we employed peptide arrays based on zDHHC AR-binding motif (zDABM) sequences of synaptosomal-associated protein 25 (SNAP25) and cysteine string protein α (CSPα). Quantitative comparisons of the binding preferences of 400 peptides allowed us to construct a position-specific scoring matrix (PSSM) for zDHHC17 AR binding, with which we predicted and subsequently validated many putative zDHHC17 interactors. We identified 95 human zDABM sequences with unexpected versatility in amino acid usage; these sequences were distributed among 90 proteins, of which 62 have not been previously implicated in zDHHC17/13 binding. These zDABM-containing proteins included all family members of the SNAP25, sprouty, cornifelin, ankyrin, and SLAIN-motif containing families; seven endogenous Gag polyproteins sharing the same binding sequence; and several proteins involved in cytoskeletal organization, cell communication, and regulation of signaling. A dozen of the zDABM-containing proteins had more than one zDABM sequence, whereas isoform-specific binding to the AR of zDHHC17 was identified for the Ena/VASP-like protein. The large number of zDABM sequences within the human proteome suggests that zDHHC17 may be an interaction hub regulating many cellular processes.
[Mh] Termos MeSH primário: Aciltransferases/metabolismo
Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Proteínas do Tecido Nervoso/metabolismo
Proteoma/metabolismo
[Mh] Termos MeSH secundário: Aciltransferases/química
Proteínas Adaptadoras de Transdução de Sinal/química
Repetição de Anquirina
Linhagem Celular
Proteínas de Choque Térmico HSP40/química
Proteínas de Choque Térmico HSP40/metabolismo
Seres Humanos
Proteínas de Membrana/química
Proteínas de Membrana/metabolismo
Proteínas do Tecido Nervoso/química
Peptídeos/química
Peptídeos/metabolismo
Análise Serial de Proteínas/métodos
Ligação Proteica
Proteoma/química
Proteína 25 Associada a Sinaptossoma/química
Proteína 25 Associada a Sinaptossoma/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (HSP40 Heat-Shock Proteins); 0 (Membrane Proteins); 0 (Nerve Tissue Proteins); 0 (Peptides); 0 (Proteome); 0 (SNAP25 protein, human); 0 (Synaptosomal-Associated Protein 25); 0 (cysteine string protein); EC 2.3.- (Acyltransferases); EC 2.3.1.- (ZDHHC17 protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171027
[Lr] Data última revisão:
171027
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170909
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.799650


  5 / 1496 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28827281
[Au] Autor:Arnold MG; Adhikari P; Kang B; Xu 徐昊 H
[Ad] Endereço:Department of Biological Sciences, University of Southern Mississippi, 118 College Drive, #5018, Hattiesburg, Mississippi 39406, U.S.A.
[Ti] Título:Munc18a clusters SNARE-bearing liposomes prior to -SNARE zippering.
[So] Source:Biochem J;474(19):3339-3354, 2017 Sep 24.
[Is] ISSN:1470-8728
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Sec1-Munc18 (SM) proteins co-operate with SNAREs {SNAP [soluble NSF ( -ethylmaleimide-sensitive factor) attachment protein] receptors} to mediate membrane fusion in eukaryotic cells. Studies of Munc18a/Munc18-1/Stxbp1 in neurotransmission suggest that SM proteins accelerate fusion kinetics primarily by activating the partially zippered -SNARE complex. However, accumulating evidence has argued for additional roles for SM proteins in earlier steps in the fusion cascade. Here, we investigate the function of Munc18a in reconstituted exocytic reactions mediated by neuronal and non-neuronal SNAREs. We show that Munc18a plays a direct role in promoting proteoliposome clustering, underlying vesicle docking during exocytosis. In the three different fusion reactions examined, Munc18a-dependent clustering requires an intact N-terminal peptide (N-peptide) motif in syntaxin that mediates the binary interaction between syntaxin and Munc18a. Importantly, clustering is preserved under inhibitory conditions that abolish both -SNARE complex formation and lipid mixing, indicating that Munc18a promotes membrane clustering in a step that is independent of -SNARE zippering and activation.
[Mh] Termos MeSH primário: Lipossomos/metabolismo
Proteínas Munc18/química
Proteínas Munc18/metabolismo
Proteínas SNARE/metabolismo
[Mh] Termos MeSH secundário: Motivos de Aminoácidos
Animais
Exocitose
Lipossomos/química
Fusão de Membrana
Proteínas Munc18/genética
Proteínas Qa-SNARE/química
Proteínas Qa-SNARE/metabolismo
Proteínas R-SNARE/genética
Proteínas R-SNARE/metabolismo
Ratos
Proteínas SNARE/genética
Proteína 25 Associada a Sinaptossoma/genética
Proteína 25 Associada a Sinaptossoma/metabolismo
Proteína 2 Associada à Membrana da Vesícula/genética
Proteína 2 Associada à Membrana da Vesícula/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Liposomes); 0 (Munc18 Proteins); 0 (Qa-SNARE Proteins); 0 (R-SNARE Proteins); 0 (SNARE Proteins); 0 (Snap25 protein, rat); 0 (Synaptosomal-Associated Protein 25); 0 (Vamp2 protein, rat); 0 (Vamp8 protein, rat); 0 (Vesicle-Associated Membrane Protein 2)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171025
[Lr] Data última revisão:
171025
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170823
[St] Status:MEDLINE
[do] DOI:10.1042/BCJ20170494


  6 / 1496 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28800600
[Au] Autor:Zanetti G; Sikorra S; Rummel A; Krez N; Duregotti E; Negro S; Henke T; Rossetto O; Binz T; Pirazzini M
[Ad] Endereço:Department of Biomedical Sciences, University of Padova, Padova, Italy.
[Ti] Título:Botulinum neurotoxin C mutants reveal different effects of syntaxin or SNAP-25 proteolysis on neuromuscular transmission.
[So] Source:PLoS Pathog;13(8):e1006567, 2017 Aug.
[Is] ISSN:1553-7374
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Botulinum neurotoxin serotype C (BoNT/C) is a neuroparalytic toxin associated with outbreaks of animal botulism, particularly in birds, and is the only BoNT known to cleave two different SNARE proteins, SNAP-25 and syntaxin. BoNT/C was shown to be a good substitute for BoNT/A1 in human dystonia therapy because of its long lasting effects and absence of neuromuscular damage. Two triple mutants of BoNT/C, namely BoNT/C S51T/R52N/N53P (BoNT/C α-51) and BoNT/C L200W/M221W/I226W (BoNT/C α-3W), were recently reported to selectively cleave syntaxin and have been used here to evaluate the individual contribution of SNAP-25 and syntaxin cleavage to the effect of BoNT/C in vivo. Although BoNT/C α-51 and BoNT/C α-3W toxins cleave syntaxin with similar efficiency, we unexpectedly found also cleavage of SNAP-25, although to a lesser extent than wild type BoNT/C. Interestingly, the BoNT/C mutants exhibit reduced lethality compared to wild type toxin, a result that correlated with their residual activity against SNAP-25. In spite of this, a local injection of BoNT/C α-51 persistently impairs neuromuscular junction activity. This is due to an initial phase in which SNAP-25 cleavage causes a complete blockade of neurotransmission, and to a second phase of incomplete impairment ascribable to syntaxin cleavage. Together, these results indicate that neuroparalysis of BoNT/C at the neuromuscular junction is due to SNAP-25 cleavage, while the proteolysis of syntaxin provides a substantial, but incomplete, neuromuscular impairment. In light of this evidence, we discuss a possible clinical use of BoNT/C α-51 as a botulinum neurotoxin endowed with a wide safety margin and a long lasting effect.
[Mh] Termos MeSH primário: Toxinas Botulínicas/toxicidade
Proteínas Qa-SNARE/metabolismo
Transmissão Sináptica/efeitos dos fármacos
Proteína 25 Associada a Sinaptossoma/metabolismo
[Mh] Termos MeSH secundário: Animais
Toxinas Botulínicas/genética
Potenciais Evocados/efeitos dos fármacos
Immunoblotting
Imuno-Histoquímica
Camundongos
Mutação
Junção Neuromuscular/efeitos dos fármacos
Técnicas de Patch-Clamp
Proteólise
Ratos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Qa-SNARE Proteins); 0 (Synaptosomal-Associated Protein 25); EC 3.4.24.69 (Botulinum Toxins); FPM7829VMX (botulinum toxin type C)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171002
[Lr] Data última revisão:
171002
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170812
[St] Status:MEDLINE
[do] DOI:10.1371/journal.ppat.1006567


  7 / 1496 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28768838
[Au] Autor:Lozada LE; Desai A; Kevala K; Lee JW; Kim HY
[Ad] Endereço:Department of Pediatrics, Walter Reed National Military Medical Center, Bethesda, MD; and.
[Ti] Título:Perinatal Brain Docosahexaenoic Acid Concentration Has a Lasting Impact on Cognition in Mice.
[So] Source:J Nutr;147(9):1624-1630, 2017 Sep.
[Is] ISSN:1541-6100
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Premature infants are deprived of prenatal accumulation of brain docosahexaenoic acid [DHA (22:6n-3)], an omega-3 fatty acid [ω-3 FA (n-3 FA)] important for proper development of cognitive function. The resulting brain DHA deficit can be reversed by ω-3 FA supplementation. The objective was to test whether there is a critical period for providing ω-3 FA to correct cognitive deficits caused by developmental ω-3 FA deprivation in mice. Twelve timed-pregnant mice [embryonic day 14 (E14), C57/BL6NCr] were fed an ω-3 FA-deficient diet containing 0.04% α-linolenic acid [ALA (18:3n-3)], and their offspring were fed the same deficient diet (Def group) or changed to an ω-3 FA-adequate diet containing 3.1% ALA at 3 wk, 2 mo, or 4 mo of age. In parallel, 3 E14 pregnant mice were fed the adequate diet and their offspring were fed the same diet (Adeq group) throughout the experiment. Brain FA composition, learning and memory, and hippocampal synaptic protein expression were evaluated at 6 mo by gas chromatography, the Morris water maze test, and western blot analysis, respectively. Maternal dietary ω-3 FA deprivation decreased DHA by >50% in the brain of their offspring at 3 wk of age. The Def group showed significantly worse learning and memory at 6 mo than those groups fed the adequate diet. These pups also had decreased hippocampal expression of postsynaptic density protein 95 (43% of Adeq group), Homer protein homolog 1 (21% of Adeq group), and synaptosome-associated protein of 25 kDa (64% of Adeq group). Changing mice to the adequate diet at 3 wk, 2 mo, or 4 mo of age restored brain DHA to the age-matched adequate concentration. However, deficits in hippocampal synaptic protein expression and spatial learning and memory were normalized only when the diet was changed at 3 wk. Developmental deprivation of brain DHA by dietary ω-3 FA depletion in mice may have a lasting impact on cognitive function if not corrected at an early age.
[Mh] Termos MeSH primário: Encéfalo/efeitos dos fármacos
Cognição/efeitos dos fármacos
Deficiências Nutricionais/tratamento farmacológico
Ácidos Docosa-Hexaenoicos/administração & dosagem
Recém-Nascido Prematuro
Aprendizagem em Labirinto/efeitos dos fármacos
Memória/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Animais Recém-Nascidos
Encéfalo/crescimento & desenvolvimento
Encéfalo/metabolismo
Deficiências Nutricionais/complicações
Dieta
Gorduras na Dieta/administração & dosagem
Gorduras na Dieta/farmacologia
Gorduras na Dieta/uso terapêutico
Proteína 4 Homóloga a Disks-Large
Ácidos Docosa-Hexaenoicos/deficiência
Ácidos Docosa-Hexaenoicos/farmacologia
Ácidos Docosa-Hexaenoicos/uso terapêutico
Feminino
Guanilato Quinases/metabolismo
Proteínas de Arcabouço Homer/metabolismo
Seres Humanos
Lactente
Recém-Nascido Prematuro/crescimento & desenvolvimento
Recém-Nascido Prematuro/metabolismo
Fenômenos Fisiológicos da Nutrição Materna
Proteínas de Membrana/metabolismo
Camundongos
Gravidez
Proteína 25 Associada a Sinaptossoma/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Dietary Fats); 0 (Disks Large Homolog 4 Protein); 0 (Dlg4 protein, mouse); 0 (Homer Scaffolding Proteins); 0 (Homer1 protein, mouse); 0 (Membrane Proteins); 0 (Snap25 protein, mouse); 0 (Synaptosomal-Associated Protein 25); 25167-62-8 (Docosahexaenoic Acids); EC 2.7.4.8 (Guanylate Kinases)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170804
[St] Status:MEDLINE
[do] DOI:10.3945/jn.117.254607


  8 / 1496 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28593826
[Au] Autor:Mao L; Wang H; Ma F; Guo Z; He H; Zhou H; Wang N
[Ad] Endereço:a Key Laboratory of Industrial Fermentation Microbiology, Ministry of Education and Tianjin, College of Biotechnology , Tianjin University of Science and Technology , Tianjin , P.R. China.
[Ti] Título:Exposure to static magnetic fields increases insulin secretion in rat INS-1 cells by activating the transcription of the insulin gene and up-regulating the expression of vesicle-secreted proteins.
[So] Source:Int J Radiat Biol;93(8):831-840, 2017 Aug.
[Is] ISSN:1362-3095
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:PURPOSE: To evaluate the effect of static magnetic fields (SMFs) on insulin secretion and explore the mechanisms underlying exposure to SMF-induced insulin secretion in rat insulinoma INS-1 cells. MATERIALS AND METHODS: INS-1 cells were exposed to a 400 mT SMF for 72 h, and the proliferation of INS-1 cells was detected by (3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyltetrazolium bromide (MTT) assay. The secretion of insulin was measured with an enzyme linked immunosorbent assays (ELISA), the expression of genes was detected by real-time PCR, and the expression of proteins was measured by Western blotting. RESULTS: Exposure to an SMF increased the expression and secretion of insulin by INS-1 cells but did not affect cell proliferation. Moreover, SMF exposure up-regulated the expression of several pancreas-specific transcriptional factors. Specifically, the activity of the rat insulin promoter was enhanced in INS-1 cells exposed to an SMF, and the expression levels of synaptosomal-associated protein 25 (SNAP-25) and syntaxin-1A were up-regulated after exposure to an SMF. CONCLUSIONS: SMF exposure can promote insulin secretion in rat INS-1 cells by activating the transcription of the insulin gene and up-regulating the expression of vesicle-secreted proteins.
[Mh] Termos MeSH primário: Insulina/genética
Insulina/secreção
Campos Magnéticos
Proteína 25 Associada a Sinaptossoma/metabolismo
Sintaxina 1/metabolismo
Ativação Transcricional
Regulação para Cima
[Mh] Termos MeSH secundário: Animais
Linhagem Celular Tumoral
Células Secretoras de Insulina/secreção
Regiões Promotoras Genéticas/genética
Ratos
Proteína 25 Associada a Sinaptossoma/genética
Sintaxina 1/genética
Fatores de Transcrição/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Insulin); 0 (Synaptosomal-Associated Protein 25); 0 (Syntaxin 1); 0 (Transcription Factors)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:170825
[Lr] Data última revisão:
170825
[Sb] Subgrupo de revista:IM; S
[Da] Data de entrada para processamento:170609
[St] Status:MEDLINE
[do] DOI:10.1080/09553002.2017.1332439


  9 / 1496 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28575017
[Au] Autor:Rasnitsyn A; Doucette L; Seifi M; Footz T; Raymond V; Walter MA
[Ad] Endereço:Department of Medical Genetics, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, Alberta, Canada.
[Ti] Título:FOXC1 modulates MYOC secretion through regulation of the exocytic proteins RAB3GAP1, RAB3GAP2 and SNAP25.
[So] Source:PLoS One;12(6):e0178518, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The neurodegenerative disease glaucoma is one of the leading causes of blindness in the world. Glaucoma is characterized by progressive visual field loss caused by retinal ganglion cell (RGC) death. Both surgical glaucoma treatments and medications are available, however, they only halt glaucoma progression and are unable to reverse damage. Furthermore, many patients do not respond well to treatments. It is therefore important to better understand the mechanisms involved in glaucoma pathogenesis. Patients with Axenfeld-Rieger syndrome (ARS) offer important insight into glaucoma progression. ARS patients are at 50% risk of developing early onset glaucoma and respond poorly to treatments, even when surgical treatments are combined with medications. Mutations in the transcription factor FOXC1 cause ARS. Alterations in FOXC1 levels cause ocular malformations and disrupt stress response in ocular tissues, thereby contributing to glaucoma progression. In this study, using biochemical and molecular techniques, we show that FOXC1 regulates the expression of RAB3GAP1, RAB3GAP2 and SNAP25, three genes with central roles in both exocytosis and endocytosis, responsible for extracellular trafficking. FOXC1 positively regulates RAB3GAP1 and RAB3GAP2, while either increase or decrease in FOXC1 levels beyond its normal range results in decreased SNAP25. In addition, we found that FOXC1 regulation of RAB3GAP1, RAB3GAP2 and SNAP25 affects secretion of Myocilin (MYOC), a protein associated with juvenile onset glaucoma and steroid-induced glaucoma. The present work reveals that FOXC1 is an important regulator of exocytosis and establishes a new link between FOXC1 and MYOC-associated glaucoma.
[Mh] Termos MeSH primário: Proteínas do Citoesqueleto/secreção
Exocitose
Proteínas do Olho/secreção
Fatores de Transcrição Forkhead/fisiologia
Glicoproteínas/secreção
Proteína 25 Associada a Sinaptossoma/fisiologia
Proteínas rab3 de Ligação ao GTP/fisiologia
[Mh] Termos MeSH secundário: Fatores de Transcrição Forkhead/genética
Técnicas de Silenciamento de Genes
Células HeLa
Seres Humanos
Luciferases/genética
RNA Mensageiro/genética
Proteína 25 Associada a Sinaptossoma/genética
Ativação Transcricional
Proteínas rab3 de Ligação ao GTP/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytoskeletal Proteins); 0 (Eye Proteins); 0 (FOXC1 protein, human); 0 (Forkhead Transcription Factors); 0 (Glycoproteins); 0 (RAB3GAP2 protein, human); 0 (RNA, Messenger); 0 (SNAP25 protein, human); 0 (Synaptosomal-Associated Protein 25); 0 (trabecular meshwork-induced glucocorticoid response protein); EC 1.13.12.- (Luciferases); EC 3.6.5.2 (RAB3GAP1 protein, human); EC 3.6.5.2 (rab3 GTP-Binding Proteins)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171009
[Lr] Data última revisão:
171009
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170603
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0178518


  10 / 1496 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28515322
[Au] Autor:Zurawski Z; Page B; Chicka MC; Brindley RL; Wells CA; Preininger AM; Hyde K; Gilbert JA; Cruz-Rodriguez O; Currie KPM; Chapman ER; Alford S; Hamm HE
[Ad] Endereço:From the Department of Pharmacology, Vanderbilt University, Nashville, Tennessee 37232-6600.
[Ti] Título:Gßγ directly modulates vesicle fusion by competing with synaptotagmin for binding to neuronal SNARE proteins embedded in membranes.
[So] Source:J Biol Chem;292(29):12165-12177, 2017 Jul 21.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:G -coupled G protein-coupled receptors can inhibit neurotransmitter release at synapses via multiple mechanisms. In addition to Gßγ-mediated modulation of voltage-gated calcium channels (VGCC), inhibition can also be mediated through the direct interaction of Gßγ subunits with the soluble -ethylmaleimide attachment protein receptor (SNARE) complex of the vesicle fusion apparatus. Binding studies with soluble SNARE complexes have shown that Gßγ binds to both ternary SNARE complexes, t-SNARE heterodimers, and monomeric SNAREs, competing with synaptotagmin 1(syt1) for binding sites on t-SNARE. However, in secretory cells, Gßγ, SNAREs, and synaptotagmin interact in the lipid environment of a vesicle at the plasma membrane. To approximate this environment, we show that fluorescently labeled Gßγ interacts specifically with lipid-embedded t-SNAREs consisting of full-length syntaxin 1 and SNAP-25B at the membrane, as measured by fluorescence polarization. Fluorescently labeled syt1 undergoes competition with Gßγ for SNARE-binding sites in lipid environments. Mutant Gßγ subunits that were previously shown to be more efficacious at inhibiting Ca -triggered exocytotic release than wild-type Gßγ were also shown to bind SNAREs at a higher affinity than wild type in a lipid environment. These mutant Gßγ subunits were unable to inhibit VGCC currents. Specific peptides corresponding to regions on Gß and Gγ shown to be important for the interaction disrupt the interaction in a concentration-dependent manner. In fusion assays using full-length t- and v-SNAREs embedded in liposomes, Gßγ inhibited Ca /synaptotagmin-dependent fusion. Together, these studies demonstrate the importance of these regions for the Gßγ-SNARE interaction and show that the target of Gßγ, downstream of VGCC, is the membrane-embedded SNARE complex.
[Mh] Termos MeSH primário: Subunidades beta da Proteína de Ligação ao GTP/metabolismo
Subunidades gama da Proteína de Ligação ao GTP/metabolismo
Bicamadas Lipídicas
Modelos Moleculares
Proteína 25 Associada a Sinaptossoma/metabolismo
Sinaptotagmina I/metabolismo
Sintaxina 1/metabolismo
[Mh] Termos MeSH secundário: Animais
Ligação Competitiva
Sinalização do Cálcio
Bovinos
Linhagem Celular
Subunidades beta da Proteína de Ligação ao GTP/química
Subunidades beta da Proteína de Ligação ao GTP/genética
Subunidades gama da Proteína de Ligação ao GTP/química
Subunidades gama da Proteína de Ligação ao GTP/genética
Seres Humanos
Lipossomos
Fusão de Membrana
Mutação
Proteínas do Tecido Nervoso/química
Proteínas do Tecido Nervoso/metabolismo
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Conformação Proteica
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Ratos
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteínas Recombinantes/química
Proteínas Recombinantes/metabolismo
Proteína 25 Associada a Sinaptossoma/química
Sinaptotagmina I/química
Sinaptotagmina I/genética
Sintaxina 1/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (GTP-Binding Protein beta Subunits); 0 (GTP-Binding Protein gamma Subunits); 0 (Lipid Bilayers); 0 (Liposomes); 0 (Nerve Tissue Proteins); 0 (Peptide Fragments); 0 (Recombinant Fusion Proteins); 0 (Recombinant Proteins); 0 (Snap25 protein, rat); 0 (Stx1a protein, rat); 0 (Synaptosomal-Associated Protein 25); 0 (Synaptotagmin I); 0 (Syntaxin 1); 0 (Syt1 protein, rat)
[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:170519
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M116.773523



página 1 de 150 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