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Pesquisa : D12.776.543.512.249.500.875 [Categoria DeCS]
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[PMID]:29227074
[Au] Autor:Minchenko OH; Tsymbal DO; Minchenko DO; Riabovol OO; Ratushna OO; Karbovskyi LL
[Ti] Título:Hypoxic regulation of the expression of cell proliferation related genes in U87 glioma cells upon inhibition of ire1 signaling enzyme
[So] Source:Ukr Biochem J;88(1):11-21, 2016 Ja-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:We have studied the effect of inhibition of IRE1 (inositol requiring enzyme 1), which is a central mediator of endoplasmic reticulum stress and a controller of cell proliferation and tumor growth, on hypoxic regulation of the expression of different proliferation related genes in U87 glioma cells. It was shown that hypoxia leads to up-regulation of the expression of IL13RA2, CD24, ING1, ING2, ENDOG, and POLG genes and to down-regulation ­ of KRT18, TRAPPC3, TSFM, and MTIF2 genes at the mRNA level in control glioma cells. Changes for ING1 and CD24 genes were more significant. At the same time, inhibition of IRE1 modifies the effect of hypoxia on the expression of all studied genes. In particular, it increases sensitivity to hypoxia of the expression of IL13RA2, TRAPPC3, ENDOG, and PLOG genes and suppresses the effect of hypoxia on the expression of ING1 gene. Additionally, it eliminates hypoxic regulation of KRT18, CD24, ING2, TSFM, and MTIF2 genes expressions and introduces sensitivity to hypoxia of the expression of BET1 gene in glioma cells. The present study demonstrates that hypoxia, which often contributes to tumor growth, affects the expression of almost all studied genes. Additionally, inhibition of IRE1 can both enhance and suppress the hypoxic regulation of these gene expressions in a gene specific manner and thus possibly contributes to slower glioma growth, but several aspects of this regulation must be further clarified.
[Mh] Termos MeSH primário: Estresse do Retículo Endoplasmático/genética
Endorribonucleases/genética
Regulação Neoplásica da Expressão Gênica
Neuroglia/metabolismo
Proteínas Serina-Treonina Quinases/genética
RNA Mensageiro/genética
Transdução de Sinais/genética
[Mh] Termos MeSH secundário: Antígeno CD24/genética
Antígeno CD24/metabolismo
Hipóxia Celular
Linhagem Celular Tumoral
Proliferação Celular
DNA Polimerase gama/genética
DNA Polimerase gama/metabolismo
Endodesoxirribonucleases/genética
Endodesoxirribonucleases/metabolismo
Endorribonucleases/antagonistas & inibidores
Endorribonucleases/metabolismo
Fatores de Iniciação em Eucariotos/genética
Fatores de Iniciação em Eucariotos/metabolismo
Proteínas de Homeodomínio/genética
Proteínas de Homeodomínio/metabolismo
Seres Humanos
Proteína 1 Inibidora do Crescimento/genética
Proteína 1 Inibidora do Crescimento/metabolismo
Subunidade alfa2 de Receptor de Interleucina-13/genética
Subunidade alfa2 de Receptor de Interleucina-13/metabolismo
Queratina-18/genética
Queratina-18/metabolismo
Proteínas Mitocondriais/genética
Proteínas Mitocondriais/metabolismo
Neuroglia/patologia
Fatores de Alongamento de Peptídeos/genética
Fatores de Alongamento de Peptídeos/metabolismo
Proteínas Serina-Treonina Quinases/antagonistas & inibidores
Proteínas Serina-Treonina Quinases/metabolismo
Proteínas Qc-SNARE/genética
Proteínas Qc-SNARE/metabolismo
RNA Mensageiro/metabolismo
Receptores Citoplasmáticos e Nucleares/genética
Receptores Citoplasmáticos e Nucleares/metabolismo
Proteínas Supressoras de Tumor/genética
Proteínas Supressoras de Tumor/metabolismo
Proteínas de Transporte Vesicular/genética
Proteínas de Transporte Vesicular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BET1L protein, human); 0 (CD24 Antigen); 0 (Eukaryotic Initiation Factors); 0 (Homeodomain Proteins); 0 (ING1 protein, human); 0 (ING2 protein, human); 0 (Inhibitor of Growth Protein 1); 0 (Interleukin-13 Receptor alpha2 Subunit); 0 (KRT18 protein, human); 0 (Keratin-18); 0 (MTIF2 protein, human); 0 (Mitochondrial Proteins); 0 (Peptide Elongation Factors); 0 (Qc-SNARE Proteins); 0 (RNA, Messenger); 0 (Receptors, Cytoplasmic and Nuclear); 0 (TRAPPC3 protein, human); 0 (TSFM protein, human); 0 (Tumor Suppressor Proteins); 0 (Vesicular Transport Proteins); EC 2.7.11.1 (ERN1 protein, human); EC 2.7.11.1 (Protein-Serine-Threonine Kinases); EC 2.7.7.7 (DNA Polymerase gamma); EC 2.7.7.7 (POLG protein, human); EC 3.1.- (Endodeoxyribonucleases); EC 3.1.- (Endoribonucleases); EC 3.1.21.- (endonuclease G)
[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:171212
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.01.011


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[PMID]:28798239
[Au] Autor:Brasher MI; Martynowicz DM; Grafinger OR; Hucik A; Shanks-Skinner E; Uniacke J; Coppolino MG
[Ad] Endereço:From the Department of Molecular and Cellular Biology, University of Guelph, Guelph, Ontario N1G 2W1, Canada.
[Ti] Título:Interaction of Munc18c and syntaxin4 facilitates invadopodium formation and extracellular matrix invasion of tumor cells.
[So] Source:J Biol Chem;292(39):16199-16210, 2017 Sep 29.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Tumor cell invasion involves targeted localization of proteins required for interactions with the extracellular matrix and for proteolysis. The localization of many proteins during these cell-extracellular matrix interactions relies on membrane trafficking mediated in part by SNAREs. The SNARE protein syntaxin4 (Stx4) is involved in the formation of invasive structures called invadopodia; however, it is unclear how Stx4 function is regulated during tumor cell invasion. Munc18c is known to regulate Stx4 activity, and here we show that Munc18c is required for Stx4-mediated invadopodium formation and cell invasion. Biochemical and microscopic analyses revealed a physical association between Munc18c and Stx4, which was enhanced during invadopodium formation, and that a reduction in Munc18c expression decreases invadopodium formation. We also found that an N-terminal Stx4-derived peptide associates with Munc18c and inhibits endogenous interactions of Stx4 with synaptosome-associated protein 23 (SNAP23) and vesicle-associated membrane protein 2 (VAMP2). Furthermore, expression of the Stx4 N-terminal peptide decreased invadopodium formation and cell invasion Of note, cells expressing the Stx4 N-terminal peptide exhibited impaired trafficking of membrane type 1 matrix metalloproteinase (MT1-MMP) and EGF receptor (EGFR) to the cell surface during invadopodium formation. Our findings implicate Munc18c as a regulator of Stx4-mediated trafficking of MT1-MMP and EGFR, advancing our understanding of the role of SNARE function in the localization of proteins that drive tumor cell invasion.
[Mh] Termos MeSH primário: Adenocarcinoma/metabolismo
Matriz Extracelular/metabolismo
Fibrossarcoma/metabolismo
Proteínas Munc18/metabolismo
Proteínas de Neoplasias/metabolismo
Podossomos/metabolismo
Proteínas Qa-SNARE/metabolismo
[Mh] Termos MeSH secundário: Adenocarcinoma/patologia
Ligação Competitiva
Linhagem Celular Tumoral
Matriz Extracelular/patologia
Fibrossarcoma/patologia
Proteínas de Fluorescência Verde/genética
Proteínas de Fluorescência Verde/metabolismo
Seres Humanos
Metaloproteinase 14 da Matriz/metabolismo
Proteínas Munc18/antagonistas & inibidores
Proteínas Munc18/química
Proteínas Munc18/genética
Invasividade Neoplásica
Proteínas de Neoplasias/antagonistas & inibidores
Proteínas de Neoplasias/química
Proteínas de Neoplasias/genética
Fragmentos de Peptídeos/química
Fragmentos de Peptídeos/genética
Fragmentos de Peptídeos/metabolismo
Podossomos/patologia
Domínios e Motivos de Interação entre Proteínas
Multimerização Proteica
Transporte Proteico
Proteínas Qa-SNARE/química
Proteínas Qa-SNARE/genética
Proteínas Qb-SNARE/antagonistas & inibidores
Proteínas Qb-SNARE/química
Proteínas Qb-SNARE/metabolismo
Proteínas Qc-SNARE/antagonistas & inibidores
Proteínas Qc-SNARE/química
Proteínas Qc-SNARE/metabolismo
Interferência de RNA
Receptor do Fator de Crescimento Epidérmico/metabolismo
Proteínas Recombinantes de Fusão/química
Proteínas Recombinantes de Fusão/metabolismo
Proteína 2 Associada à Membrana da Vesícula/antagonistas & inibidores
Proteína 2 Associada à Membrana da Vesícula/química
Proteína 2 Associada à Membrana da Vesícula/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Munc18 Proteins); 0 (Neoplasm Proteins); 0 (Peptide Fragments); 0 (Qa-SNARE Proteins); 0 (Qb-SNARE Proteins); 0 (Qc-SNARE Proteins); 0 (Recombinant Fusion Proteins); 0 (SNAP23 protein, human); 0 (VAMP2 protein, human); 0 (Vesicle-Associated Membrane Protein 2); 0 (syntaxin 4, human); 147336-22-9 (Green Fluorescent Proteins); EC 2.7.10.1 (EGFR protein, human); EC 2.7.10.1 (Receptor, Epidermal Growth Factor); EC 3.4.24.80 (MMP14 protein, human); EC 3.4.24.80 (Matrix Metalloproteinase 14)
[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:170812
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.807438


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[PMID]:28654152
[Au] Autor:Bateman NW; Dubil EA; Wang G; Hood BL; Oliver JM; Litzi TA; Gist GD; Mitchell DA; Blanton B; Phippen NT; Tian C; Zahn CM; Cohn DE; Havrilesky LJ; Berchuck A; Shriver CD; Darcy KM; Hamilton CA; Conrads TP; Maxwell GL
[Ad] Endereço:Gynecologic Cancer Center of Excellence, Department of Obstetrics and Gynecology, Uniformed Services University and Walter Reed National Military Medical Center, Bethesda, Maryland.
[Ti] Título:Race-specific molecular alterations correlate with differential outcomes for black and white endometrioid endometrial cancer patients.
[So] Source:Cancer;123(20):4004-4012, 2017 Oct 15.
[Is] ISSN:1097-0142
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The objective of this study was to identify molecular alterations associated with disease outcomes for white and black patients with endometrioid endometrial cancer (EEC). METHODS: EEC samples from black (n = 17) and white patients (n = 13) were analyzed by proteomics (liquid chromatography-tandem mass spectrometry) and transcriptomics (RNA-seq). Coordinate alterations were validated with RNA-seq data from black (n = 49) and white patients (n = 216). Concordantly altered candidates were further tested for associations with race-specific progression-free survival (PFS) in black (n = 64) or white patients (n = 267) via univariate and multivariate Cox regression modeling and log-rank testing. RESULTS: Discovery analyses revealed significantly altered candidate proteins and transcripts between black and white patients, suggesting modulation of tumor cell viability in black patients and cell death signaling in black and white patients. Eighty-nine candidates were validated as altered between these patient cohorts, and a subset significantly correlated with differential PFS. White-specific PFS candidates included serpin family A member 4 (SERPINA4; hazard ratio [HR], 0.89; Wald P value = .02), integrin subunit α3 (ITGA3; HR, 0.76; P = .03), and Bet1 Golgi vesicular membrane trafficking protein like (BET1L; HR, 0.48; P = .04). Black-specific PFS candidates included family with sequence similarity 228 member B (FAM228B; HR, 0.13; P = .001) and HEAT repeat containing 6 (HEATR6; HR, 4.94; P = .047). Several candidates were also associated with overall survival (SERPINA4 and ITGA3) as well as PFS independent of disease stage, grade and myometrial invasion (SERPINA4, BET1L and FAM228B). CONCLUSIONS: This study has identified and validated molecular alterations in tumors from black and white EEC patients, including candidates significantly associated with altered disease outcomes within these patient cohorts. Cancer 2017;123:4004-12. © 2017 American Cancer Society.
[Mh] Termos MeSH primário: Carcinoma Endometrioide/genética
Neoplasias do Endométrio/genética
[Mh] Termos MeSH secundário: Afroamericanos
Carcinoma Endometrioide/etnologia
Carcinoma Endometrioide/metabolismo
Carcinoma Endometrioide/patologia
Cromatografia Líquida
Intervalo Livre de Doença
Neoplasias do Endométrio/etnologia
Neoplasias do Endométrio/metabolismo
Neoplasias do Endométrio/patologia
Grupo com Ancestrais do Continente Europeu
Feminino
Perfilação da Expressão Gênica
Disparidades nos Níveis de Saúde
Seres Humanos
Integrina alfa3
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
Análise Multivariada
Gradação de Tumores
Estadiamento de Neoplasias
Prognóstico
Modelos de Riscos Proporcionais
Proteínas Qc-SNARE
Serpinas
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (BET1L protein, human); 0 (ITGA3 protein, human); 0 (Integrin alpha3); 0 (Membrane Proteins); 0 (Qc-SNARE Proteins); 0 (Serpins); 0 (kallistatin)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171011
[Lr] Data última revisão:
171011
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170628
[St] Status:MEDLINE
[do] DOI:10.1002/cncr.30813


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[PMID]:28575006
[Au] Autor:Wang P; Zhang X; Ma X; Sun Y; Liu N; Li F; Hou Y
[Ad] Endereço:College of Science, China Agricultural University, Beijing, China.
[Ti] Título:Identification of CkSNAP33, a gene encoding synaptosomal-associated protein from Cynanchum komarovii, that enhances Arabidopsis resistance to Verticillium dahliae.
[So] Source:PLoS One;12(6):e0178101, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:SNARE proteins are essential to vesicle trafficking and membrane fusion in eukaryotic cells. In addition, the SNARE-mediated secretory pathway can deliver diverse defense products to infection sites during exocytosis-associated immune responses in plants. In this study, a novel gene (CkSNAP33) encoding a synaptosomal-associated protein was isolated from Cynanchum komarovii and characterized. CkSNAP33 contains Qb- and Qc-SNARE domains in the N- and C-terminal regions, respectively, and shares high sequence identity with AtSNAP33 from Arabidopsis. CkSNAP33 expression was induced by H2O2, salicylic acid (SA), Verticillium dahliae, and wounding. Arabidopsis lines overexpressing CkSNAP33 had longer primary roots and larger seedlings than the wild type (WT). Transgenic Arabidopsis lines showed significantly enhanced resistance to V. dahliae, and displayed reductions in disease index and fungal biomass, and also showed elevated expression of PR1 and PR5. The leaves of transgenic plants infected with V. dahliae showed strong callose deposition and cell death that hindered the penetration and spread of the fungus at the infection site. Taken together, these results suggest that CkSNAP33 is involved in the defense response against V. dahliae and enhanced disease resistance in Arabidopsis.
[Mh] Termos MeSH primário: Proteínas de Arabidopsis/genética
Arabidopsis/genética
Arabidopsis/microbiologia
Cynanchum/genética
Doenças das Plantas/genética
Doenças das Plantas/microbiologia
Proteínas de Plantas/genética
Proteínas Qb-SNARE/genética
Proteínas Qc-SNARE/genética
Verticillium/fisiologia
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Arabidopsis/química
Proteínas de Arabidopsis/química
Cynanchum/química
Cynanchum/microbiologia
Resistência à Doença
Regulação da Expressão Gênica de Plantas
Filogenia
Proteínas de Plantas/química
Plantas Geneticamente Modificadas/química
Plantas Geneticamente Modificadas/genética
Plantas Geneticamente Modificadas/microbiologia
Domínios Proteicos
Proteínas Qb-SNARE/química
Proteínas Qc-SNARE/química
Alinhamento de Sequência
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Arabidopsis Proteins); 0 (Plant Proteins); 0 (Qb-SNARE Proteins); 0 (Qc-SNARE Proteins); 0 (SNAP33 protein, Arabidopsis)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170603
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0178101


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[PMID]:28202687
[Au] Autor:Dingjan I; Linders PT; van den Bekerom L; Baranov MV; Halder P; Ter Beest M; van den Bogaart G
[Ad] Endereço:Department of Tumor Immunology, Radboud Institute for Molecular Life Sciences, Radboud University Medical Center, Nijmegen 6525 GA, The Netherlands.
[Ti] Título:Oxidized phagosomal NOX2 complex is replenished from lysosomes.
[So] Source:J Cell Sci;130(7):1285-1298, 2017 Apr 01.
[Is] ISSN:1477-9137
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:In dendritic cells, the NADPH oxidase 2 complex (NOX2) is recruited to the phagosomal membrane during antigen uptake. NOX2 produces reactive oxygen species (ROS) in the lumen of the phagosome that kill ingested pathogens, delay antigen breakdown and alter the peptide repertoire for presentation to T cells. How the integral membrane component of NOX2, cytochrome (which comprises CYBB and CYBA), traffics to phagosomes is incompletely understood. In this study, we show in dendritic cells derived from human blood-isolated monocytes that cytochrome is initially recruited to the phagosome from the plasma membrane during phagosome formation. Cytochrome also traffics from a lysosomal pool to phagosomes and this is required to replenish oxidatively damaged NOX2. We identified syntaxin-7, SNAP23 and VAMP8 as the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins mediating this process. Our data describe a key mechanism of how dendritic cells sustain ROS production after antigen uptake that is required to initiate T cell responses.
[Mh] Termos MeSH primário: Lisossomos/metabolismo
Glicoproteínas de Membrana/metabolismo
NADPH Oxidases/metabolismo
Fagossomos/metabolismo
[Mh] Termos MeSH secundário: Compartimento Celular
Membrana Celular/metabolismo
Grupo dos Citocromos b/metabolismo
Endossomos/metabolismo
Técnicas de Silenciamento de Genes
Seres Humanos
Membranas Intracelulares/metabolismo
Proteína 1 de Membrana Associada ao Lisossomo/metabolismo
Modelos Biológicos
NADPH Oxidase 2
Oxirredução
Fosfatidilinositóis/metabolismo
Proteínas Qa-SNARE
Proteínas Qb-SNARE/metabolismo
Proteínas Qc-SNARE/metabolismo
Proteínas R-SNARE/metabolismo
RNA Interferente Pequeno/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Proteínas de Ligação a Fator Solúvel Sensível a N-Etilmaleimida/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytochrome b Group); 0 (Lysosomal-Associated Membrane Protein 1); 0 (Membrane Glycoproteins); 0 (Phosphatidylinositols); 0 (Qa-SNARE Proteins); 0 (Qb-SNARE Proteins); 0 (Qc-SNARE Proteins); 0 (R-SNARE Proteins); 0 (RNA, Small Interfering); 0 (Reactive Oxygen Species); 0 (SNAP23 protein, human); 0 (Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins); 0 (VAMP8 protein, human); 9064-78-2 (cytochrome b558); EC 1.6.3.- (CYBB protein, human); EC 1.6.3.- (NADPH Oxidase 2); EC 1.6.3.- (NADPH Oxidases)
[Em] Mês de entrada:1708
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170217
[St] Status:MEDLINE
[do] DOI:10.1242/jcs.196931


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[PMID]:27932448
[Au] Autor:Kimura T; Jia J; Kumar S; Choi SW; Gu Y; Mudd M; Dupont N; Jiang S; Peters R; Farzam F; Jain A; Lidke KA; Adams CM; Johansen T; Deretic V
[Ad] Endereço:Department of Molecular Genetics and Microbiology, University of New Mexico Health Sciences Center, Albuquerque, NM, USA.
[Ti] Título:Dedicated SNAREs and specialized TRIM cargo receptors mediate secretory autophagy.
[So] Source:EMBO J;36(1):42-60, 2017 Jan 04.
[Is] ISSN:1460-2075
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Autophagy is a process delivering cytoplasmic components to lysosomes for degradation. Autophagy may, however, play a role in unconventional secretion of leaderless cytosolic proteins. How secretory autophagy diverges from degradative autophagy remains unclear. Here we show that in response to lysosomal damage, the prototypical cytosolic secretory autophagy cargo IL-1ß is recognized by specialized secretory autophagy cargo receptor TRIM16 and that this receptor interacts with the R-SNARE Sec22b to recruit cargo to the LC3-II sequestration membranes. Cargo secretion is unaffected by downregulation of syntaxin 17, a SNARE promoting autophagosome-lysosome fusion and cargo degradation. Instead, Sec22b in combination with plasma membrane syntaxin 3 and syntaxin 4 as well as SNAP-23 and SNAP-29 completes cargo secretion. Thus, secretory autophagy utilizes a specialized cytosolic cargo receptor and a dedicated SNARE system. Other unconventionally secreted cargo, such as ferritin, is secreted via the same pathway.
[Mh] Termos MeSH primário: Autofagia
Proteínas de Ligação a DNA/metabolismo
Interleucina-1beta/secreção
Proteínas Associadas aos Microtúbulos/metabolismo
Proteínas R-SNARE/metabolismo
Fatores de Transcrição/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular
Ferritinas/secreção
Seres Humanos
Monócitos/metabolismo
Proteínas Qa-SNARE/metabolismo
Proteínas Qb-SNARE/metabolismo
Proteínas Qc-SNARE/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA-Binding Proteins); 0 (Interleukin-1beta); 0 (MAP1LC3A protein, human); 0 (Microtubule-Associated Proteins); 0 (Qa-SNARE Proteins); 0 (Qb-SNARE Proteins); 0 (Qc-SNARE Proteins); 0 (R-SNARE Proteins); 0 (SNAP23 protein, human); 0 (SNAP29 protein, human); 0 (Sec22B protein, human); 0 (TRIM16 protein, human); 0 (Transcription Factors); 9007-73-2 (Ferritins)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:170830
[Lr] Data última revisão:
170830
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161210
[St] Status:MEDLINE
[do] DOI:10.15252/embj.201695081


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[PMID]:27836773
[Au] Autor:Kobayashi K; Oyama S; Kuki C; Tsugami Y; Matsunaga K; Suzuki T; Nishimura T
[Ad] Endereço:Laboratory of Cell and Tissue Biology, Research Faculty of Agriculture, Hokkaido University, North 9, West 9, 060-8589, Sapporo, Japan. Electronic address: kkobaya@anim.agr.hokudai.ac.jp.
[Ti] Título:Distinct roles of prolactin, epidermal growth factor, and glucocorticoids in ß-casein secretion pathway in lactating mammary epithelial cells.
[So] Source:Mol Cell Endocrinol;440:16-24, 2017 Jan 15.
[Is] ISSN:1872-8057
[Cp] País de publicação:Ireland
[La] Idioma:eng
[Ab] Resumo:Beta-casein is a secretory protein contained in milk. Mammary epithelial cells (MECs) synthesize and secrete ß-casein during lactation. However, it remains unclear how the ß-casein secretion pathway is developed after parturition. In this study, we focused on prolactin (PRL), epidermal growth factor (EGF), and glucocorticoids, which increase in blood plasma and milk around parturition. MECs cultured with PRL, EGF and dexamethasone (DEX: glucocorticoid analog) developed the ß-casein secretion pathway. In the absence of PRL, MECs hardly expressed ß-casein. EGF enhanced the expression and secretion of ß-casein in the presence of PRL and DEX. DEX treatment rapidly increased secreted ß-casein concurrent with enhancing ß-casein expression. DEX also up-regulated the expression of SNARE proteins, such as SNAP-23, VAMP-8 and Syntaxin-12. Furthermore, PRL and DEX regulated the expression ratio of α -, ß- and κ-casein. These results indicate that PRL, EGF and glucocorticoids have distinct roles in the establishment of ß-casein secretion pathway.
[Mh] Termos MeSH primário: Caseínas/secreção
Fator de Crescimento Epidérmico/farmacologia
Células Epiteliais/metabolismo
Glucocorticoides/farmacologia
Lactação/efeitos dos fármacos
Glândulas Mamárias Animais/citologia
Prolactina/farmacologia
Via Secretória/efeitos dos fármacos
[Mh] Termos MeSH secundário: Animais
Diferenciação Celular/efeitos dos fármacos
Células Cultivadas
Dexametasona/farmacologia
Regulação para Baixo/efeitos dos fármacos
Células Epiteliais/citologia
Células Epiteliais/efeitos dos fármacos
Feminino
Camundongos Endogâmicos ICR
Proteínas Qb-SNARE/metabolismo
Proteínas Qc-SNARE/metabolismo
Via Secretória/genética
Ovinos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Caseins); 0 (Glucocorticoids); 0 (Qb-SNARE Proteins); 0 (Qc-SNARE Proteins); 0 (Snap23 protein, mouse); 62229-50-9 (Epidermal Growth Factor); 7S5I7G3JQL (Dexamethasone); 9002-62-4 (Prolactin)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161113
[St] Status:MEDLINE


  8 / 352 MEDLINE  
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[PMID]:27795355
[Au] Autor:Min A; Lee YA; Kim KA; El-Benna J; Shin MH
[Ad] Endereço:Department of Environmental Medical Biology, Institute of Tropical Medicine, Yonsei University College of Medicine, Seoul, South Korea.
[Ti] Título:SNAP23-Dependent Surface Translocation of Leukotriene B4 (LTB4) Receptor 1 Is Essential for NOX2-Mediated Exocytotic Degranulation in Human Mast Cells Induced by Trichomonas vaginalis-Secreted LTB4.
[So] Source:Infect Immun;85(1), 2017 Jan.
[Is] ISSN:1098-5522
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Trichomonas vaginalis is a sexually transmitted parasite that causes vaginitis in women and itself secretes lipid mediator leukotriene B (LTB ). Mast cells are important effector cells of tissue inflammation during infection with parasites. Membrane-bridging SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) complexes are critical for fusion during exocytosis. Although T. vaginalis-derived secretory products (TvSP) have been shown to induce exocytosis in mast cells, information regarding the signaling mechanisms between mast cell activation and TvSP is limited. In this study, we found that SNAP23-dependent surface trafficking of LTB receptor 1 (BLT1) is required for nicotinamide adenine dinucleotide phosphate oxidase 2 (NOX2)-mediated exocytotic degranulation of mast cells induced by TvSP. First, stimulation with TvSP induced exocytotic degranulation and reactive oxygen species (ROS) generation in HMC-1 cells. Next, TvSP-induced ROS generation and exocytosis were strongly inhibited by transfection of BLT1 small interfering RNA (siRNA). TvSP induced trafficking of BLT1 from the cytosol to the plasma membrane. We also found that knockdown of SNAP23 abrogated TvSP-induced ROS generation, exocytosis, and surface trafficking of BLT1 in HMC-1 cells. By coimmunoprecipitation, there was a physical interaction between BLT1 and SNAP23 in TvSP-stimulated HMC-1 cells. Taken together, our results suggest that SNAP23-dependent surface trafficking of BLT1 is essential for exocytosis in human mast cells induced by T. vaginalis-secreted LTB Our data collectively demonstrate a novel regulatory mechanism for SNAP23-dependent mast cell activation of T. vaginalis-secreted LTB involving surface trafficking of BLT1. These results can help to explain how the cross talk mechanism between parasite and host can govern deliberately tissue inflammatory responses.
[Mh] Termos MeSH primário: Exocitose/fisiologia
Leucotrieno B4/metabolismo
Glicoproteínas de Membrana/metabolismo
NADPH Oxidases/metabolismo
Transporte Proteico/fisiologia
Proteínas Qb-SNARE/metabolismo
Proteínas Qc-SNARE/metabolismo
Receptores do Leucotrieno B4/metabolismo
Trichomonas vaginalis/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular
Membrana Celular/metabolismo
Feminino
Seres Humanos
Inflamação/metabolismo
Inflamação/microbiologia
Mastócitos
NADPH Oxidase 2
RNA Interferente Pequeno/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Transdução de Sinais
Vaginite por Trichomonas/parasitologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (LTB4R1 protein, human); 0 (Membrane Glycoproteins); 0 (Qb-SNARE Proteins); 0 (Qc-SNARE Proteins); 0 (RNA, Small Interfering); 0 (Reactive Oxygen Species); 0 (Receptors, Leukotriene B4); 0 (SNAP23 protein, human); 1HGW4DR56D (Leukotriene B4); EC 1.6.3.- (CYBB protein, human); EC 1.6.3.- (NADPH Oxidase 2); EC 1.6.3.- (NADPH Oxidases)
[Em] Mês de entrada:1705
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161101
[St] Status:MEDLINE


  9 / 352 MEDLINE  
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[PMID]:27855700
[Au] Autor:Sun Q; Huang X; Zhang Q; Qu J; Shen Y; Wang X; Sun H; Wang J; Xu L; Chen X; Ren B
[Ad] Endereço:Department of Jiangsu Key Laboratory of Molecular and Translational Cancer Research, Cancer Institute of Jiangsu Province, Nanjing, Jiangsu, China, 210009.
[Ti] Título:SNAP23 promotes the malignant process of ovarian cancer.
[So] Source:J Ovarian Res;9(1):80, 2016 Nov 17.
[Is] ISSN:1757-2215
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: Ovarian cancer (OC) was the primary malignant gynecological cancer and SNARE protein is closely related with tumor progression. Here, we identified SNAP23, a member of SNARE complex, as a potential oncogene in OC. METHODS: We determined the expression of SNAP23 in OC tissues and explored the clinical significance through bioinformatics analysis. The effects of SNAP23 on OC cell proliferation, migration, invasion, cell cycle and apoptosis were then evaluated in vitro. RESULTS: SNAP23 is hyper-expressed in OC tumor tissues compared to normal tissues, and increased expression of SNAP23 is associated with a poor progression free survival (HR = 1.24, 95% CI = 1.07-1.44, p = 0.0042). SNAP23 knock down increases cell apoptosis and inhibits cell proliferation, migration and invasion of OC cells. GO analysis reveals that most genes correlated highly with SNAP23 were enriched in metabolic process. CONCLUSIONS: Our data suggest that SNAP23 may serve as an oncogene promoting tumorigenicity of OC cells by decreasing apoptotic process.
[Mh] Termos MeSH primário: Regulação Neoplásica da Expressão Gênica
Neoplasias Ovarianas/patologia
Proteínas Qb-SNARE/genética
Proteínas Qb-SNARE/metabolismo
Proteínas Qc-SNARE/genética
Proteínas Qc-SNARE/metabolismo
[Mh] Termos MeSH secundário: Linhagem Celular Tumoral
Movimento Celular
Proliferação Celular
Progressão da Doença
Feminino
Seres Humanos
Invasividade Neoplásica
Neoplasias Ovarianas/genética
Neoplasias Ovarianas/metabolismo
Prognóstico
Regulação para Cima
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Qb-SNARE Proteins); 0 (Qc-SNARE Proteins); 0 (SNAP23 protein, human)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:170315
[Lr] Data última revisão:
170315
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161119
[St] Status:MEDLINE


  10 / 352 MEDLINE  
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[PMID]:27697926
[Au] Autor:Kunii M; Ohara-Imaizumi M; Takahashi N; Kobayashi M; Kawakami R; Kondoh Y; Shimizu T; Simizu S; Lin B; Nunomura K; Aoyagi K; Ohno M; Ohmuraya M; Sato T; Yoshimura SI; Sato K; Harada R; Kim YJ; Osada H; Nemoto T; Kasai H; Kitamura T; Nagamatsu S; Harada A
[Ad] Endereço:Laboratory of Molecular Traffic, Department of Molecular and Cellular Biology, Institute for Molecular and Cellular Regulation, Gunma University, Gunma 371-8512, Japan Department of Cell Biology, Graduate School of Medicine, Osaka University, Osaka 565-0871, Japan.
[Ti] Título:Opposing roles for SNAP23 in secretion in exocrine and endocrine pancreatic cells.
[So] Source:J Cell Biol;215(1):121-138, 2016 Oct 10.
[Is] ISSN:1540-8140
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The membrane fusion of secretory granules with plasma membranes is crucial for the exocytosis of hormones and enzymes. Secretion disorders can cause various diseases such as diabetes or pancreatitis. Synaptosomal-associated protein 23 (SNAP23), a soluble N-ethyl-maleimide sensitive fusion protein attachment protein receptor (SNARE) molecule, is essential for secretory granule fusion in several cell lines. However, the in vivo functions of SNAP23 in endocrine and exocrine tissues remain unclear. In this study, we show opposing roles for SNAP23 in secretion in pancreatic exocrine and endocrine cells. The loss of SNAP23 in the exocrine and endocrine pancreas resulted in decreased and increased fusion of granules to the plasma membrane after stimulation, respectively. Furthermore, we identified a low molecular weight compound, MF286, that binds specifically to SNAP23 and promotes insulin secretion in mice. Our results demonstrate opposing roles for SNAP23 in the secretion mechanisms of the endocrine and exocrine pancreas and reveal that the SNAP23-binding compound MF286 may be a promising drug for diabetes treatment.
[Mh] Termos MeSH primário: Ilhotas Pancreáticas/citologia
Pâncreas Exócrino/citologia
Proteínas Qb-SNARE/metabolismo
Proteínas Qc-SNARE/metabolismo
[Mh] Termos MeSH secundário: Células Acinares/metabolismo
Células Acinares/ultraestrutura
Amilases/metabolismo
Animais
Fusão Celular
Exocitose
Transportador de Glucose Tipo 4/metabolismo
Insulina/secreção
Camundongos Knockout
Microscopia de Fluorescência por Excitação Multifotônica
Modelos Biológicos
Glândula Parótida/citologia
Transporte Proteico
Proteínas Qb-SNARE/deficiência
Proteínas Qc-SNARE/deficiência
Proteínas SNARE/metabolismo
Vesículas Secretórias/metabolismo
Proteína 25 Associada a Sinaptossoma/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Glucose Transporter Type 4); 0 (Insulin); 0 (Qb-SNARE Proteins); 0 (Qc-SNARE Proteins); 0 (SNARE Proteins); 0 (Slc2a4 protein, mouse); 0 (Snap23 protein, mouse); 0 (Snap25 protein, mouse); 0 (Synaptosomal-Associated Protein 25); EC 3.2.1.- (Amylases)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:170601
[Lr] Data última revisão:
170601
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161005
[St] Status:MEDLINE



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