Base de dados : MEDLINE
Pesquisa : D08.811.682.608.575.968 [Categoria DeCS]
Referências encontradas : 87 [refinar]
Mostrando: 1 .. 10   no formato [Detalhado]

página 1 de 9 ir para página                      

  1 / 87 MEDLINE  
              next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28830888
[Au] Autor:Marzaioli V; Hurtado-Nedelec M; Pintard C; Tlili A; Marie JC; Monteiro RC; Gougerot-Pocidalo MA; Dang PM; El-Benna J
[Ad] Endereço:INSERM-U1149, CNRS-ERL8252, Centre de Recherche sur l'Inflammation, Paris, France.
[Ti] Título:NOX5 and p22phox are 2 novel regulators of human monocytic differentiation into dendritic cells.
[So] Source:Blood;130(15):1734-1745, 2017 Oct 12.
[Is] ISSN:1528-0020
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Dendritic cells (DCs) are a heterogeneous population of professional antigen-presenting cells and are key cells of the immune system, acquiring different phenotypes in accordance with their localization during the immune response. A subset of inflammatory DCs is derived from circulating monocytes (Mo) and has a key role in inflammation and infection. The pathways controlling Mo-DC differentiation are not fully understood. Our objective was to investigate the possible role of nicotinamide adenine dinucleotide phosphate reduced form oxidases (NOXs) in Mo-DC differentiation. In this study, we revealed that Mo-DC differentiation was inhibited by NOX inhibitors and reactive oxygen species scavengers. We show that the Mo-DC differentiation was dependent on p22phox, and not on gp91phox/NOX2, as shown by the reduced Mo-DC differentiation observed in chronic granulomatous disease patients lacking p22phox. Moreover, we revealed that NOX5 expression was strongly increased during Mo-DC differentiation, but not during Mo-macrophage differentiation. NOX5 was expressed in circulating myeloid DC, and at a lower level in plasmacytoid DC. Interestingly, NOX5 was localized at the outer membrane of the mitochondria and interacted with p22phox in Mo-DC. Selective inhibitors and small interfering RNAs for NOX5 indicated that NOX5 controlled Mo-DC differentiation by regulating the JAK/STAT/MAPK and NFκB pathways. These data demonstrate that the NOX5-p22phox complex drives Mo-DC differentiation, and thus could be critical for immunity and inflammation.
[Mh] Termos MeSH primário: Diferenciação Celular
Células Dendríticas/citologia
Proteínas de Membrana/metabolismo
Monócitos/citologia
NADPH Oxidases/metabolismo
[Mh] Termos MeSH secundário: Diferenciação Celular/efeitos dos fármacos
Células Dendríticas/efeitos dos fármacos
Células Dendríticas/metabolismo
Inibidores Enzimáticos/farmacologia
Depuradores de Radicais Livres/farmacologia
Seres Humanos
Glicoproteínas de Membrana/metabolismo
Proteínas de Membrana/antagonistas & inibidores
Mitocôndrias/efeitos dos fármacos
Mitocôndrias/metabolismo
Membranas Mitocondriais/efeitos dos fármacos
Membranas Mitocondriais/metabolismo
Modelos Biológicos
Monócitos/efeitos dos fármacos
Monócitos/metabolismo
NADPH Oxidase 2
NADPH Oxidase 5
NADPH Oxidases/antagonistas & inibidores
NF-kappa B/metabolismo
Ligação Proteica/efeitos dos fármacos
Espécies Reativas de Oxigênio/metabolismo
Transdução de Sinais/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Free Radical Scavengers); 0 (Membrane Glycoproteins); 0 (Membrane Proteins); 0 (NF-kappa B); 0 (Reactive Oxygen Species); EC 1.6.3.- (CYBB protein, human); EC 1.6.3.- (NADPH Oxidase 2); EC 1.6.3.- (NADPH Oxidase 5); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.- (NOX5 protein, human); EC 1.6.3.1 (CYBA protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:AIM; IM
[Da] Data de entrada para processamento:170824
[St] Status:MEDLINE
[do] DOI:10.1182/blood-2016-10-746347


  2 / 87 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28473473
[Au] Autor:Jha JC; Watson AMD; Mathew G; de Vos LC; Jandeleit-Dahm K
[Ad] Endereço:Department of Diabetes, Central Clinical School, Monash University, Australia.
[Ti] Título:The emerging role of NADPH oxidase NOX5 in vascular disease.
[So] Source:Clin Sci (Lond);131(10):981-990, 2017 May 01.
[Is] ISSN:1470-8736
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Oxidative stress is a consequence of up-regulation of pro-oxidant enzyme-induced reactive oxygen species (ROS) production and concomitant depletion of antioxidants. Elevated levels of ROS act as an intermediate and are the common denominator for various diseases including diabetes-associated macro-/micro-vascular complications and hypertension. A range of enzymes are capable of generating ROS, but the pro-oxidant enzyme family, nicotinamide adenine dinucleotide phosphate (NADPH) oxidases (NOXs), are the only enzymes known to be solely dedicated to ROS generation in the vascular tissues, kidney, aortas and eyes. While there is convincing evidence for a role of NOX1 in vascular and eye disease and for NOX4 in renal injury, the role of NOX5 in disease is less clear. Although NOX5 is highly up-regulated in humans in disease, it is absent in rodents. Thus, so far it has not been possible to study NOX5 in traditional mouse or rat models of disease. In the present review, we summarize and critically analyse the emerging evidence for a pathophysiological role of NOX5 in disease including the expression, regulation and molecular and cellular mechanisms which have been demonstrated to be involved in NOX5 activation.
[Mh] Termos MeSH primário: Proteínas de Membrana/metabolismo
NADPH Oxidases/metabolismo
Doenças Vasculares/enzimologia
[Mh] Termos MeSH secundário: Animais
Endotélio Vascular/enzimologia
Seres Humanos
Proteínas de Membrana/genética
Camundongos
NADPH Oxidase 5
NADPH Oxidases/genética
Ratos
Espécies Reativas de Oxigênio/metabolismo
Doenças Vasculares/genética
[Pt] Tipo de publicação:EDITORIAL; REVIEW
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (Reactive Oxygen Species); EC 1.6.3.- (NADPH Oxidase 5); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.- (NOX5 protein, human)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170506
[St] Status:MEDLINE
[do] DOI:10.1042/CS20160846


  3 / 87 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:28034671
[Au] Autor:Dho SH; Kim JY; Lee KP; Kwon ES; Lim JC; Kim CJ; Jeong D; Kwon KS
[Ad] Endereço:Aging Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon 305-806, Republic of Korea; Radioisotope Research Division, Department of Research Reactor Utilization, Korea Atomic Energy Research Institute, Daejeon 305-353, Republic of Korea.
[Ti] Título:STAT5A-mediated NOX5-L expression promotes the proliferation and metastasis of breast cancer cells.
[So] Source:Exp Cell Res;351(1):51-58, 2017 Feb 01.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:NADPH oxidase (NOX) generates reactive oxygen species (ROS) and has been suggested to mediate cell proliferation in some cancers. Here, we show that an increase in the expression of NOX5 long form (NOX5-L) is critical for tumor progression in breast tumor tissues. Immunostaining of clinical samples indicated that NOX5 was overexpressed in 41.1% of breast ductal carcinoma samples. NOX5-L depletion consistently suppressed cell proliferation, invasion, and migration in vitro. Antibody-mediated neutralization of NOX5-L attenuated tumor progression in a mouse xenograft model. Promoter analysis revealed that NOX5-L expression is regulated by STAT5A in breast cancer cells. Based on our novel findings, we suggest that inhibition of NOX5-L may be a promising therapeutic strategy that exerts anti-cancer effects via the modulation of ROS-mediated cell signaling.
[Mh] Termos MeSH primário: Proliferação Celular
Neoplasias Mamárias Experimentais/metabolismo
Proteínas de Membrana/metabolismo
NADPH Oxidases/metabolismo
Fator de Transcrição STAT5/metabolismo
Proteínas Supressoras de Tumor/metabolismo
[Mh] Termos MeSH secundário: Animais
Anticorpos Neutralizantes/imunologia
Linhagem Celular Tumoral
Feminino
Regulação Neoplásica da Expressão Gênica
Seres Humanos
Neoplasias Mamárias Experimentais/patologia
Proteínas de Membrana/genética
Proteínas de Membrana/imunologia
Camundongos
Camundongos Endogâmicos BALB C
Camundongos Nus
NADPH Oxidase 5
NADPH Oxidases/genética
NADPH Oxidases/imunologia
Metástase Neoplásica
Regiões Promotoras Genéticas
Fator de Transcrição STAT5/genética
Proteínas Supressoras de Tumor/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Neutralizing); 0 (Membrane Proteins); 0 (STAT5 Transcription Factor); 0 (STAT5A protein, human); 0 (Tumor Suppressor Proteins); EC 1.6.3.- (NADPH Oxidase 5); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.- (NOX5 protein, human)
[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:161231
[St] Status:MEDLINE


  4 / 87 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
[PMID]:27756772
[Au] Autor:Li D; Hong J; Cao W
[Ad] Endereço:Departments of Medicine (D.L., W.C.) and Pathology (W.C.), Rhode Island Hospital and Warren Alpert Medical School of Brown University, Providence, Rhode Island; and Department of Gastroenterology, Shanghai Jiao-Tong University School of Medicine, Renji Hospital, Shanghai Institute of Digestive Disease, Shanghai, China (J.H.).
[Ti] Título:Silencer-of-Death Domain Mediates Acid-Induced Decrease in Cell Apoptosis in Barrett's Associated Esophageal Adenocarcinoma Cells.
[So] Source:J Pharmacol Exp Ther;360(1):14-22, 2017 Jan.
[Is] ISSN:1521-0103
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:We have shown that NADPH oxidase (NOX)5-S may mediate the acid-induced decrease in cell apoptosis. However, mechanisms of NOX5-S-dependent decrease in cell apoptosis are not fully understood. In this study, we found that silencer-of-death domain (SODD) was significantly increased in esophageal adenocarcinoma (EA) tissues, EA cell lines FLO and OE33, and a dysplastic cell line CP-B. Strong SODD immunostaining was significantly higher in low-grade dysplasia (66.7%), high-grade dysplasia (81.2%), and EA (71.2%) than in Barrett's mucosa (10.5%). Acid treatment significantly increased SODD protein and mRNA expression and promoter activity in FLO cells, an increase that was significantly decreased by the knockdown of NOX5-S and nuclear factor κB (NF-κB)1 p50 with their small interfering RNAs. Similarly, acid-induced increase of SODD mRNA was blocked by knockdown of NOX5-S and p50 in a BE cell line CP-A. Overexpression of NOX5-S significantly increased SODD protein expression in FLO cells. Moreover, overexpression of NOX5-S or p50 significantly increased the SODD promoter activity and decreased the caspase 9 activity or apoptosis. NOX5-S overexpression-induced increase in SODD promoter activity was significantly decreased by knockdown of p50. In addition, acid treatment significantly decreased the caspase 9 activity, a decrease that was significantly inhibited by knockdown of SODD. Furthermore, chromatin immunoprecipitation assay showed that NF-κB1 p50 bound to SODD genomic DNA containing a NF-κB-binding element GGGGACACCCT. This binding element was further confirmed by a gel mobility shift assay. We conclude that acid-induced increase in SODD expression and decrease in cell apoptosis may depend on the activation of NOX5-S and NF-κB1 p50 in FLO cells.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Adenocarcinoma/complicações
Adenocarcinoma/patologia
Apoptose
Esôfago de Barrett/complicações
Neoplasias Esofágicas/complicações
Neoplasias Esofágicas/patologia
[Mh] Termos MeSH secundário: Ácidos/farmacologia
Proteínas Adaptadoras de Transdução de Sinal/genética
Apoptose/efeitos dos fármacos
Linhagem Celular Tumoral
Ativação Enzimática/efeitos dos fármacos
Esôfago/efeitos dos fármacos
Esôfago/metabolismo
Esôfago/patologia
Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
Seres Humanos
Concentração de Íons de Hidrogênio
Proteínas de Membrana/metabolismo
NADPH Oxidase 5
NADPH Oxidases/metabolismo
Subunidade p50 de NF-kappa B/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Acids); 0 (Adaptor Proteins, Signal Transducing); 0 (BAG4 protein, human); 0 (Membrane Proteins); 0 (NF-kappa B p50 Subunit); 0 (RNA, Messenger); EC 1.6.3.- (NADPH Oxidase 5); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.- (NOX5 protein, human)
[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:161021
[St] Status:MEDLINE


  5 / 87 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:27415609
[Au] Autor:Kalatskaya I
[Ad] Endereço:Ontario Institute for Cancer Research, MaRS Centre, Toronto, Ontario, Canada. irina.kalatskaya@oicr.on.ca.
[Ti] Título:Overview of major molecular alterations during progression from Barrett's esophagus to esophageal adenocarcinoma.
[So] Source:Ann N Y Acad Sci;1381(1):74-91, 2016 Oct.
[Is] ISSN:1749-6632
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Esophageal adenocarcinoma (EAC) develops in the sequential transformation of normal epithelium into metaplastic epithelium, called Barrett's esophagus (BE), then to dysplasia, and finally cancer. BE is a common condition in which normal stratified squamous epithelium of the esophagus is replaced with an intestine-like columnar epithelium, and it is the most prominent risk factor for EAC. This review aims to impartially systemize the knowledge from a large number of publications that describe the molecular and biochemical alterations occurring over this progression sequence. In order to provide an unbiased extraction of the knowledge from the literature, a text-mining methodology was used to select genes that are involved in the BE progression, with the top candidate genes found to be TP53, CDKN2A, CTNNB1, CDH1, GPX3, and NOX5. In addition, sample frequencies across analyzed patient cohorts at each stage of disease progression are summarized. All six genes are altered in the majority of EAC patients, and accumulation of alterations correlates well with the sequential progression of BE to cancer, indicating that the text-mining method is a valid approach for gene prioritization. This review discusses how, besides being cancer drivers, these genes are functionally interconnected and might collectively be considered a central hub of BE progression.
[Mh] Termos MeSH primário: Adenocarcinoma/diagnóstico
Adenocarcinoma/genética
Esôfago de Barrett/diagnóstico
Esôfago de Barrett/genética
Biomarcadores Tumorais/genética
Progressão da Doença
Neoplasias Esofágicas/diagnóstico
Neoplasias Esofágicas/genética
[Mh] Termos MeSH secundário: Adenocarcinoma/metabolismo
Animais
Esôfago de Barrett/metabolismo
Biomarcadores Tumorais/metabolismo
Inibidor de Quinase Dependente de Ciclina p18/genética
Inibidor de Quinase Dependente de Ciclina p18/metabolismo
Neoplasias Esofágicas/metabolismo
Seres Humanos
Proteínas de Membrana/genética
Proteínas de Membrana/metabolismo
NADPH Oxidase 5
NADPH Oxidases/genética
NADPH Oxidases/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Proteína Supressora de Tumor p53/genética
Proteína Supressora de Tumor p53/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
0 (Biomarkers, Tumor); 0 (CDKN2A protein, human); 0 (Cyclin-Dependent Kinase Inhibitor p18); 0 (Membrane Proteins); 0 (Reactive Oxygen Species); 0 (TP53 protein, human); 0 (Tumor Suppressor Protein p53); EC 1.6.3.- (NADPH Oxidase 5); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.- (NOX5 protein, human)
[Em] Mês de entrada:1707
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160715
[St] Status:MEDLINE
[do] DOI:10.1111/nyas.13134


  6 / 87 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:27391469
[Au] Autor:Petrushanko IY; Lobachev VM; Kononikhin AS; Makarov AA; Devred F; Kovacic H; Kubatiev AA; Tsvetkov PO
[Ad] Endereço:Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Vavilov Street 32, 119991 Moscow, Russia.
[Ti] Título:Oxidation of Са2+-Binding Domain of NADPH Oxidase 5 (NOX5): Toward Understanding the Mechanism of Inactivation of NOX5 by ROS.
[So] Source:PLoS One;11(7):e0158726, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:NOX5 protein, one of the most active generators of reactive oxygen species (ROS), plays an important role in many processes, including regulation of cell growth, death and differentiation. Because of its central role in ROS generation, it needs to be tightly regulated to guarantee cellular homeostasis. Contrary to other members of NADPH-oxidases family, NOX5 has its own regulatory calcium-binding domain and thus could be activated directly by calcium ions. While several mechanisms of activation have been described, very little is known about the mechanisms that could prevent the overproduction of ROS by NOX5. In the present study using calorimetric methods and circular dichroism we found that oxidation of cysteine and methionine residues of NOX5 decreases binding of Ca2+ ions and perturbs both secondary and tertiary structure of protein. Our data strongly suggest that oxidation of calcium-binding domain of NOX5 could be implicated in its inactivation, serving as a possible defense mechanism against oxidative stress.
[Mh] Termos MeSH primário: Proteínas de Membrana/química
Proteínas de Membrana/metabolismo
NADPH Oxidases/química
NADPH Oxidases/metabolismo
Espécies Reativas de Oxigênio/metabolismo
[Mh] Termos MeSH secundário: Sequência de Aminoácidos
Calorimetria
Varredura Diferencial de Calorimetria
Cromatografia Líquida
Dicroísmo Circular
Cisteína/metabolismo
Homeostase
Seres Humanos
Proteínas de Membrana/genética
Metionina/metabolismo
Dados de Sequência Molecular
NADPH Oxidase 5
NADPH Oxidases/genética
Oxirredução
Domínios Proteicos
Análise de Sequência de Proteína
Espectrometria de Massas em Tandem
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (Reactive Oxygen Species); AE28F7PNPL (Methionine); EC 1.6.3.- (NADPH Oxidase 5); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.- (NOX5 protein, human); K848JZ4886 (Cysteine)
[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:160709
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0158726


  7 / 87 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
Texto completo
[PMID]:26968548
[Au] Autor:Yeung KR; Chiu CL; Pidsley R; Makris A; Hennessy A; Lind JM
[Ad] Endereço:School of Medicine, Western Sydney University, Sydney, Australia;
[Ti] Título:DNA methylation profiles in preeclampsia and healthy control placentas.
[So] Source:Am J Physiol Heart Circ Physiol;310(10):H1295-303, 2016 May 15.
[Is] ISSN:1522-1539
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Preeclampsia is a hypertensive disorder of pregnancy that affects 3-5% of all pregnancies. There is evidence to suggest that epigenetic mechanisms, such as DNA methylation, play a role in placental development and function. This study compared DNA methylation profiles of placentas from preeclampsia-affected pregnancies with placentas from healthy pregnancies to identify gene-specific changes in DNA methylation that may contribute to the development of preeclampsia. The methylation status of eight placental biopsies taken from preeclampsia-affected and 16 healthy pregnancies was analyzed using the Illumina Infinium Methylation 450 BeadChip array. Bisulfite pyrosequencing was used to confirm regions found to be differentially methylated between preeclampsia and healthy placentas. A total of 303 differentially methylated regions, 214 hypermethylated and 89 hypomethylated, between preeclampsia cases and controls were identified, after adjusting for gestational age (adjusted P < 0.05). Functional annotation found cell adhesion, wingless type MMTV Integration Site family member 2 (Wnt) signaling pathway, and regulation of transcription were significantly enriched in these gene regions. Hypermethylation of WNT2, sperm equatorial segment protein (SPESP1), NADPH oxidase 5 (NOX5), and activated leukocyte cell adhesion molecule (ALCAM) in preeclampsia placentas was confirmed with pyrosequencing. This study found differences in methylation in gene regions involved in cell signaling (WNT2), fertilization and implantation (SPESP1), reactive oxygen species signaling (NOX5), and cell adhesion (ALCAM). These results build on recently published studies that have reported significant differences in DNA methylation in preeclampsia placentas.
[Mh] Termos MeSH primário: Metilação de DNA
Epigênese Genética
Placenta/química
Pré-Eclâmpsia/genética
[Mh] Termos MeSH secundário: Adulto
Antígenos CD/genética
Proteínas de Transporte/genética
Estudos de Casos e Controles
Moléculas de Adesão Celular Neuronais/genética
Epigenômica/métodos
Feminino
Proteínas Fetais/genética
Perfilação da Expressão Gênica
Predisposição Genética para Doença
Estudo de Associação Genômica Ampla
Seres Humanos
Proteínas de Membrana/genética
NADPH Oxidase 5
NADPH Oxidases/genética
Pré-Eclâmpsia/diagnóstico
Gravidez
Proteínas de Plasma Seminal/genética
Transcrição Genética
Proteína Wnt2/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (ALCAM protein, human); 0 (Antigens, CD); 0 (Carrier Proteins); 0 (Cell Adhesion Molecules, Neuronal); 0 (Fetal Proteins); 0 (Membrane Proteins); 0 (SPESP1 protein, human); 0 (Seminal Plasma Proteins); 0 (WNT2 protein, human); 0 (Wnt2 Protein); EC 1.6.3.- (NADPH Oxidase 5); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.- (NOX5 protein, human)
[Em] Mês de entrada:1706
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160313
[St] Status:MEDLINE
[do] DOI:10.1152/ajpheart.00958.2015


  8 / 87 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:26901778
[Au] Autor:Hong J; Li D; Cao W
[Ad] Endereço:Department of Medicine, Rhode Island Hospital and the Warren Alpert Medical School of Brown University, Providence, RI, United States of America.
[Ti] Título:Rho Kinase ROCK2 Mediates Acid-Induced NADPH Oxidase NOX5-S Expression in Human Esophageal Adenocarcinoma Cells.
[So] Source:PLoS One;11(2):e0149735, 2016.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Mechanisms of the progression from Barrett's esophagus (BE) to esophageal adenocarcinoma (EA) are not fully understood. We have shown that NOX5-S may be involved in this progression. However, how acid upregulates NOX5-S is not well known. We found that acid-induced increase in NOX5-S expression was significantly decreased by the Rho kinase (ROCK) inhibitor Y27632 in BE mucosal biopsies and FLO-1 EA cells. In addition, acid treatment significantly increased the Rho kinase activity in FLO-1 cells. The acid-induced increase in NOX5-S expression and H2O2 production was significantly decreased by knockdown of Rho kinase ROCK2, but not by knockdown of ROCK1. Conversely, the overexpression of the constitutively active ROCK2, but not the constitutively active ROCK1, significantly enhanced the NOX5-S expression and H2O2 production. Moreover, the acid-induced increase in Rho kinase activity and in NOX5-S mRNA expression was blocked by the removal of calcium in both FLO-1 and OE33 cells. The calcium ionophore A23187 significantly increased the Rho kinase activity and NOX5-S mRNA expression. We conclude that acid-induced increase in NOX5-S expression and H2O2 production may depend on the activation of ROCK2, but not ROCK1, in EA cells. The acid-induced activation of Rho kinase may be mediated by the intracellular calcium increase. It is possible that persistent acid reflux present in BE patients may increase the intracellular calcium, activate ROCK2 and thereby upregulate NOX5-S. High levels of reactive oxygen species derived from NOX5-S may cause DNA damage and thereby contribute to the progression from BE to EA.
[Mh] Termos MeSH primário: Adenocarcinoma/genética
Adenocarcinoma/metabolismo
Neoplasias Esofágicas/genética
Neoplasias Esofágicas/metabolismo
Regulação Neoplásica da Expressão Gênica
Proteínas de Membrana/genética
NADPH Oxidases/genética
Quinases Associadas a rho/metabolismo
[Mh] Termos MeSH secundário: Adenocarcinoma/patologia
Esôfago de Barrett/genética
Esôfago de Barrett/metabolismo
Esôfago de Barrett/patologia
Cálcio/metabolismo
Linhagem Celular Tumoral
Ativação Enzimática
Neoplasias Esofágicas/patologia
Seres Humanos
Peróxido de Hidrogênio/metabolismo
NADPH Oxidase 5
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
RNA Interferente Pequeno/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL
[Nm] Nome de substância:
0 (Membrane Proteins); 0 (RNA, Messenger); 0 (RNA, Small Interfering); BBX060AN9V (Hydrogen Peroxide); EC 1.6.3.- (NADPH Oxidase 5); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.- (NOX5 protein, human); EC 2.7.11.1 (ROCK2 protein, human); EC 2.7.11.1 (rho-Associated Kinases); SY7Q814VUP (Calcium)
[Em] Mês de entrada:1607
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160223
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0149735


  9 / 87 MEDLINE  
              first record previous record next record last record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:26878911
[Au] Autor:Lin C; Zhao X; Sun D; Zhang L; Fang W; Zhu T; Wang Q; Liu B; Wei S; Chen G; Xu Z; Gao X
[Ad] Endereço:Institute of Environmental Medicine, Zhejiang University School of Medicine, Hangzhou, China.
[Ti] Título:Transcriptional activation of follistatin by Nrf2 protects pulmonary epithelial cells against silica nanoparticle-induced oxidative stress.
[So] Source:Sci Rep;6:21133, 2016 Feb 16.
[Is] ISSN:2045-2322
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Silica nanoparticles (SiO2 NPs) cause oxidative stress in respiratory system. Meanwhile, human cells launch adaptive responses to overcome SiO2 NP toxicity. However, besides a few examples, the regulation of SiO2 NP-responsive proteins and their functions in SiO2 NP response remain largely unknown. In this study, we demonstrated that SiO2 NP induced the expression of follistatin (FST), a stress responsive gene, in mouse lung tissue as well as in human lung epithelial cells (A549). The levels of Ac-H3(K9/18) and H3K4me2, two active gene markers, at FST promoter region were significantly increased during SiO2 NP treatment. The induction of FST transcription was mediated by the nuclear factor erythroid 2-related factor 2 (Nrf2), as evidenced by the decreased FST expression in Nrf2-deficient cells and the direct binding of Nrf2 to FST promoter region. Down-regulation of FST promoted SiO2 NP-induced apoptosis both in cultured cells and in mouse lung tissue. Furthermore, knockdown of FST increased while overexpression of FST decreased the expression level of NADPH oxidase 1 (NOX1) and NOX5 as well as the production of cellular reactive oxygen species (ROS). Taken together, these findings demonstrated a protective role of FST in SiO2 NP-induced oxidative stress and shed light on the interaction between SiO2 NPs and biological systems.
[Mh] Termos MeSH primário: Células Epiteliais Alveolares/metabolismo
Folistatina/genética
Fator 2 Relacionado a NF-E2/metabolismo
Nanopartículas
Estresse Oxidativo
Dióxido de Silício
Ativação Transcricional
[Mh] Termos MeSH secundário: Animais
Apoptose/genética
Linhagem Celular
Expressão Gênica
Seres Humanos
Masculino
Proteínas de Membrana/genética
Camundongos
NADPH Oxidase 1
NADPH Oxidase 5
NADPH Oxidases/genética
Nanopartículas/efeitos adversos
Espécies Reativas de Oxigênio/metabolismo
Dióxido de Silício/efeitos adversos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Follistatin); 0 (Membrane Proteins); 0 (NF-E2-Related Factor 2); 0 (Reactive Oxygen Species); 7631-86-9 (Silicon Dioxide); EC 1.6.3.- (NADPH Oxidase 1); EC 1.6.3.- (NADPH Oxidase 5); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.- (NOX1 protein, human); EC 1.6.3.- (NOX5 protein, human)
[Em] Mês de entrada:1612
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160217
[St] Status:MEDLINE
[do] DOI:10.1038/srep21133


  10 / 87 MEDLINE  
              first record previous record
seleciona
para imprimir
Fotocópia
PubMed Central Texto completo
Texto completo
[PMID]:25559363
[Au] Autor:Höll M; Koziel R; Schäfer G; Pircher H; Pauck A; Hermann M; Klocker H; Jansen-Dürr P; Sampson N
[Ad] Endereço:Institute for Biomedical Aging Research, University of Innsbruck, Innsbruck, Austria.
[Ti] Título:ROS signaling by NADPH oxidase 5 modulates the proliferation and survival of prostate carcinoma cells.
[So] Source:Mol Carcinog;55(1):27-39, 2016 Jan.
[Is] ISSN:1098-2744
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Prostate cancer (PCa) is the most commonly diagnosed cancer and second leading cause of male cancer death in Western nations. Thus, new treatment modalities are urgently needed. Elevated production of reactive oxygen species (ROS) by NADPH oxidase (Nox) enzymes is implicated in tumorigenesis of the prostate and other tissues. However, the identity of the Nox enzyme(s) involved in prostate carcinogenesis remains largely unknown. Analysis of radical prostatectomy tissue samples and benign and malignant prostate epithelial cell lines identified Nox5 as an abundantly expressed Nox isoform. Consistently, immunohistochemical staining of a human PCa tissue microarray revealed distinct Nox5 expression in epithelial cells of benign and malignant prostatic glands. shRNA-mediated knockdown of Nox5 impaired proliferation of Nox5-expressing (PC-3, LNCaP) but not Nox5-negative (DU145) PCa cell lines. Similar effects were observed upon ROS ablation via the antioxidant N-acetylcysteine confirming ROS as the mediators. In addition, Nox5 silencing increased apoptosis of PC-3 cells. Concomitantly, protein kinase C zeta (PKCζ) protein levels and c-Jun N-terminal kinase (JNK) phosphorylation were reduced. Moreover, the effect of Nox5 knockdown on PC-3 cell proliferation could be mimicked by pharmacological inhibition of JNK. Collectively, these data indicate that Nox5 is expressed at functionally relevant levels in the human prostate and clinical PCa. Moreover, findings herein suggest that Nox5-derived ROS and subsequent depletion of PKCζ and JNK inactivation play a critical role in modulating intracellular signaling cascades involved in the proliferation and survival of PCa cells. © 2014 The Authors. Molecular Carcinogenesis published by Wiley Periodicals, Inc.
[Mh] Termos MeSH primário: Carcinoma/metabolismo
Proteínas de Membrana/metabolismo
NADPH Oxidases/metabolismo
Neoplasias da Próstata/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Carcinoma/genética
Linhagem Celular Tumoral
Proliferação Celular
Sobrevivência Celular/genética
Células Epiteliais/metabolismo
Expressão Gênica
Perfilação da Expressão Gênica
Seres Humanos
Isoenzimas
Proteínas Quinases JNK Ativadas por Mitógeno/metabolismo
Masculino
Proteínas de Membrana/genética
NADPH Oxidase 5
NADPH Oxidases/genética
Fosforilação
Neoplasias da Próstata/genética
Proteína Quinase C/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Isoenzymes); 0 (Membrane Proteins); 0 (Reactive Oxygen Species); EC 1.6.3.- (NADPH Oxidase 5); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.- (NOX5 protein, human); EC 2.7.11.1 (protein kinase C zeta); EC 2.7.11.13 (Protein Kinase C); EC 2.7.11.24 (JNK Mitogen-Activated Protein Kinases)
[Em] Mês de entrada:1605
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:150107
[St] Status:MEDLINE
[do] DOI:10.1002/mc.22255



página 1 de 9 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