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[PMID]:29441928
[Au] Autor:Wang Y; Nie W; Yao K; Wang Z; He H
[Ti] Título:Interleukin 6 induces expression of NADPH oxidase 2 in human aortic endothelial cells via long noncoding RNA MALAT1.
[So] Source:Pharmazie;71(10):592-597, 2016 Oct 01.
[Is] ISSN:0031-7144
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Human abdominal aortic aneurysm (AAA) is characterized by the induction of intracellular and extracellular inflammatory cytokines and the production of reactive oxygen species (ROS) associated with localized inflammatory responses in the vascular wall. Recent studies have shown that greater circulating levels of the proinflammatory cytokine interleukin-6 (IL-6) are closely associated with AAA presence, suggesting that IL-6 plays an important role in the development of AAA. Previous in vivo studies have indicated that excess activities of NADPH oxidase (NOX), a major oxidase system for ROS production, promote AAA development. Furthermore, long noncoding RNAs (lncRNAs) are involved in the development of AAA. LncRNA MALAT1 has been found closely involved in endothelial cell functions and dysfunctions. In the present study, we explored the effects and the underlying mechanisms of IL-6 and MALAT1 on the expression/activity of NOXs in human aortic endothelial cells (HAOECs). Primary HAOECs with or without overexpression or knockdown of MALTA1 were cultured in the presence of IL-6. We found that IL-6 concentration- and time-dependently elevated the NOX activity as well as the MALAT1 level in HAOECs. Among different NOXs, only NOX2 was induced by IL-6. Overexpression and knockdown of MALAT1 respectively augmented and abolished IL6-induced expression of NOX2, NOX activity/cellular ROS production, and activation of the human NOX2 gene promoter, whereas MALAT1 alone in the absence of IL-6 treatment showed no significant effect. Knockdown of extracellular signal-regulated kinase (ERK) abolished IL6-induced expression of MALAT1. In conclusion, this study provides the first evidence that IL-6 induces expression/activity of NOX2 in HAOECs via inducing MALAT1 by an ERK-dependent mechanism. It adds new insights into the molecular mechanisms underlying AAA development.
[Mh] Termos MeSH primário: Células Endoteliais/metabolismo
Interleucina-6/farmacologia
NADPH Oxidase 2/biossíntese
RNA Longo não Codificante/genética
[Mh] Termos MeSH secundário: Aorta Torácica/citologia
Aorta Torácica/efeitos dos fármacos
Células Endoteliais/efeitos dos fármacos
Técnicas de Silenciamento de Genes
Seres Humanos
Isoenzimas/genética
Isoenzimas/metabolismo
Sistema de Sinalização das MAP Quinases/efeitos dos fármacos
NADPH Oxidase 2/genética
Cultura Primária de Células
Processamento de Proteína Pós-Traducional
RNA Longo não Codificante/farmacologia
Espécies Reativas de Oxigênio/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (IL6 protein, human); 0 (Interleukin-6); 0 (Isoenzymes); 0 (MALAT1 long non-coding RNA, human); 0 (RNA, Long Noncoding); 0 (Reactive Oxygen Species); EC 1.6.3.- (CYBB protein, human); EC 1.6.3.- (NADPH Oxidase 2)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180227
[Lr] Data última revisão:
180227
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180215
[St] Status:MEDLINE
[do] DOI:10.1691/ph.2016.6598


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[PMID]:28458776
[Au] Autor:Stein J; Steven S; Bros M; Sudowe S; Hausding M; Oelze M; Münzel T; Grabbe S; Reske-Kunz A; Daiber A
[Ad] Endereço:Department of Dermatology, Medical Center of the Johannes Gutenberg University, Mainz, Germany.
[Ti] Título:Role of Protein Kinase C and Nox2-Derived Reactive Oxygen Species Formation in the Activation and Maturation of Dendritic Cells by Phorbol Ester and Lipopolysaccharide.
[So] Source:Oxid Med Cell Longev;2017:4157213, 2017.
[Is] ISSN:1942-0994
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:. Activation/maturation of dendritic cells (DCs) plays a central role in adaptive immune responses by antigen processing and (cross-) activation of T cells. There is ongoing discussion on the role of reactive oxygen species (ROS) in these processes and with the present study we investigated this enigmatic pathway. . DCs were cultured from precursors in the bone marrow of mice (BM-DCs) and analyzed for ROS formation, maturation, and T cell stimulatory capacity upon stimulation with phorbol ester (PDBu) and lipopolysaccharide (LPS). LPS stimulation of BM-DCs caused maturation with moderate intracellular ROS formation, whereas PDBu treatment resulted in maturation with significant ROS formation. The NADPH oxidase inhibitors apocynin/VAS2870 and genetic gp91phox deletion both decreased the ROS signal in PDBu-stimulated BM-DCs without affecting maturation and T cell stimulatory capacity of BM-DCs. In contrast, the protein kinase C inhibitors chelerythrine/Gö6983 decreased PDBu-stimulated ROS formation in BM-DCs as well as maturation. . Obviously Nox2-dependent ROS formation in BM-DCs is not always required for their maturation or T cell stimulatory potential. PDBu/LPS-triggered BM-DC maturation rather relies on phosphorylation cascades. Our results question the role of oxidative stress as an essential "danger signal" for BM-DC activation, although we cannot exclude contribution by other ROS sources.
[Mh] Termos MeSH primário: Células da Medula Óssea/enzimologia
Células Dendríticas/enzimologia
Lipopolissacarídeos/farmacologia
NADPH Oxidase 2/metabolismo
Proteína Quinase C/metabolismo
Espécies Reativas de Oxigênio/metabolismo
Acetato de Tetradecanoilforbol/farmacologia
[Mh] Termos MeSH secundário: Animais
Células Dendríticas/patologia
Camundongos
Camundongos Endogâmicos BALB C
Camundongos Knockout
NADPH Oxidase 2/antagonistas & inibidores
NADPH Oxidase 2/genética
Estresse Oxidativo/efeitos dos fármacos
Proteína Quinase C/antagonistas & inibidores
Proteína Quinase C/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Lipopolysaccharides); 0 (Reactive Oxygen Species); EC 1.6.3.- (Cybb protein, mouse); EC 1.6.3.- (NADPH Oxidase 2); EC 2.7.11.13 (Protein Kinase C); NI40JAQ945 (Tetradecanoylphorbol Acetate)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180220
[Lr] Data última revisão:
180220
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170502
[St] Status:MEDLINE
[do] DOI:10.1155/2017/4157213


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[PMID]:29183727
[Au] Autor:Kikuchi H; Mimuro H; Kuribayashi F
[Ad] Endereço:Laboratory of Biological Chemistry, Department of Food and Nutrition, Shokei University Junior College, 2-6-78 Kuhonji, Chuo-ku, Kumamoto 862-8678, Japan. Electronic address: masakari@shokei-gakuen.ac.jp.
[Ti] Título:Resveratrol strongly enhances the retinoic acid-induced superoxide generating activity via up-regulation of gp91-phox gene expression in U937 cells.
[So] Source:Biochem Biophys Res Commun;495(1):1195-1200, 2018 01 01.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The membrane bound cytochrome b composed of gp91-phox and p22-phox proteins, and cytosolic proteins p40-, p47-and p67-phox are important components of superoxide (O )-generating system in phagocytes. Here, we describe that resveratrol, a pleiotropic phytochemical belonging to the stilbenoids, dramatically activates the O -generating system during retinoic acid (RA)-induced differentiation of human monoblastic leukemia U937 cells to macrophage-like cells. When U937 cells were cultured in the presence of RA and resveratrol, the O -generating activity increased more than 5-fold compared with that in the absence of the latter. Semiquantitative RT-PCR showed that co-treatment with RA and resveratrol strongly enhanced transcription of the gp91-phox compared with those of the RA-treatment only. On the other hand, immunoblot analysis revealed that co-treatment with RA and resveratrol caused remarkable accumulation of protein levels of gp91-phox (to 4-fold), p22-phox (to 5-fold) and p47-phox (to 4-fold) compared with those of the RA-treatment alone. In addition, ChIP assay suggested that resveratrol participates in enhancing the gene expression of gp91-phox via promoting acetylation of Lys-9 residues and Lys-14 residues of histone H3 within chromatin around the promoter regions of the gene. These results suggested that resveratrol strongly enhances the RA-induced O -generating activity via up-regulation of gp91-phox gene expression in U937 cells.
[Mh] Termos MeSH primário: Regulação Neoplásica da Expressão Gênica/efeitos dos fármacos
NADPH Oxidase 2/metabolismo
Neoplasias Experimentais/metabolismo
Estilbenos/administração & dosagem
Superóxidos/metabolismo
Tretinoína/metabolismo
[Mh] Termos MeSH secundário: Relação Dose-Resposta a Droga
Seres Humanos
Células U937
Regulação para Cima/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Stilbenes); 11062-77-4 (Superoxides); 5688UTC01R (Tretinoin); EC 1.6.3.- (CYBB protein, human); EC 1.6.3.- (NADPH Oxidase 2); Q369O8926L (resveratrol)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:180105
[Lr] Data última revisão:
180105
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171130
[St] Status:MEDLINE


  4 / 1742 MEDLINE  
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[PMID]:28467198
[Au] Autor:Ng HH; Yildiz GS; Ku JM; Miller AA; Woodman OL; Hart JL
[Ad] Endereço:1 School of BioSciences, University of Melbourne, Parkville, VIC, Australia.
[Ti] Título:Chronic NaHS treatment decreases oxidative stress and improves endothelial function in diabetic mice.
[So] Source:Diab Vasc Dis Res;14(3):246-253, 2017 May.
[Is] ISSN:1752-8984
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Hydrogen sulphide (H S) is endogenously produced in vascular tissue and has anti-oxidant and vasoprotective properties. This study investigates whether chronic treatment using the fast H S donor NaHS could elicit a vasoprotective effect in diabetes. Diabetes was induced in male C57BL6/J mice with streptozotocin (60 mg/kg daily, ip for 2 weeks) and confirmed by elevated blood glucose and glycated haemoglobin levels. Diabetic mice were then treated with NaHS (100 µmol/kg/day) for 4 weeks, and aortae collected for functional and biochemical analyses. In the diabetic group, both endothelium-dependent vasorelaxation and basal nitric oxide (NO ) bioactivity were significantly reduced ( p < 0.05), and maximal vasorelaxation to the NO donor sodium nitroprusside was impaired ( p < 0.05) in aorta compared to control mice. Vascular superoxide generation via nicotine adenine dinucleotide phosphate (NADPH) oxidase ( p < 0.05) was elevated in aorta from diabetic mice which was associated with increased expression of NOX2 ( p < 0.05). NaHS treatment of diabetic mice restored endothelial function and exogenous NO efficacy back to control levels. NaHS treatment also reduced the diabetes-induced increase in NADPH oxidase activity, but did not affect NOX2 protein expression. These data show that chronic NaHS treatment reverses diabetes-induced vascular dysfunction by restoring NO efficacy and reducing superoxide production in the mouse aorta.
[Mh] Termos MeSH primário: Antioxidantes/administração & dosagem
Diabetes Mellitus Experimental/tratamento farmacológico
Angiopatias Diabéticas/prevenção & controle
Endotélio Vascular/efeitos dos fármacos
Estresse Oxidativo/efeitos dos fármacos
Sulfetos/administração & dosagem
[Mh] Termos MeSH secundário: Animais
Glicemia/metabolismo
Diabetes Mellitus Experimental/sangue
Diabetes Mellitus Experimental/complicações
Angiopatias Diabéticas/etiologia
Angiopatias Diabéticas/metabolismo
Angiopatias Diabéticas/fisiopatologia
Relação Dose-Resposta a Droga
Esquema de Medicação
Endotélio Vascular/metabolismo
Endotélio Vascular/fisiopatologia
Hemoglobina A Glicada/metabolismo
Masculino
Camundongos Endogâmicos C57BL
Músculo Liso Vascular/efeitos dos fármacos
Músculo Liso Vascular/metabolismo
Músculo Liso Vascular/fisiopatologia
NADPH Oxidase 2/metabolismo
Óxido Nítrico/metabolismo
Doadores de Óxido Nítrico/farmacologia
Óxido Nítrico Sintase Tipo III/metabolismo
Superóxidos/metabolismo
Fatores de Tempo
Vasodilatação/efeitos dos fármacos
Vasodilatadores/farmacologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Blood Glucose); 0 (Glycated Hemoglobin A); 0 (HbA(1c) protein, mouse); 0 (Nitric Oxide Donors); 0 (Sulfides); 0 (Vasodilator Agents); 11062-77-4 (Superoxides); 31C4KY9ESH (Nitric Oxide); EC 1.14.13.39 (Nitric Oxide Synthase Type III); EC 1.14.13.39 (Nos3 protein, mouse); EC 1.6.3.- (Cybb protein, mouse); EC 1.6.3.- (NADPH Oxidase 2); FWU2KQ177W (sodium bisulfide)
[Em] Mês de entrada:1712
[Cu] Atualização por classe:171219
[Lr] Data última revisão:
171219
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170504
[St] Status:MEDLINE
[do] DOI:10.1177/1479164117692766


  5 / 1742 MEDLINE  
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[PMID]:28880721
[Au] Autor:Cho HJ; Lee WH; Hwang OMH; Sonntag WE; Lee YW
[Ad] Endereço:a Department of Biochemistry and Molecular Biology , University of Miami Miller School of Medicine , Miami , FL , USA.
[Ti] Título:Role of NADPH oxidase in radiation-induced pro-oxidative and pro-inflammatory pathways in mouse brain.
[So] Source:Int J Radiat Biol;93(11):1257-1266, 2017 Nov.
[Is] ISSN:1362-3095
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:PURPOSE: The present study was designed to investigate our hypothesis that NADPH oxidase plays a role in radiation-induced pro-oxidative and pro-inflammatory environments in the brain. MATERIALS AND METHODS: C57BL/6 mice received either fractionated whole brain irradiation or sham-irradiation. The mRNA expression levels of pro-inflammatory mediators, such as TNF-α and MCP-1, were determined by quantitative real-time RT-PCR. The protein expression levels of TNF-α, MCP-1, NOX-2 and Iba1 were detected by immunofluorescence staining. The levels of ROS were visualized by in situ DHE fluorescence staining. RESULTS: A significant up-regulation of mRNA and protein expression levels of TNF-α and MCP-1 was observed in irradiated mouse brains. Additionally, immunofluorescence staining of Iba1 showed a marked increase of microglial activation in mouse brain after irradiation. Moreover, in situ DHE fluorescence staining revealed that fractionated whole brain irradiation significantly increased production of ROS. Furthermore, a significant increase in immunoreactivity of NOX-2 was detected in mouse brain after irradiation. On the contrary, an enhanced ROS generation in mouse brain after irradiation was markedly attenuated in the presence of NOX inhibitors or NOX-2 neutralizing antibody. CONCLUSIONS: These results suggest that NOX-2 may play a role in fractionated whole brain irradiation-induced pro-oxidative and pro-inflammatory pathways in mouse brain.
[Mh] Termos MeSH primário: Encéfalo/metabolismo
Encéfalo/efeitos da radiação
Glicoproteínas de Membrana/metabolismo
NADPH Oxidases/metabolismo
[Mh] Termos MeSH secundário: Animais
Encéfalo/citologia
Encéfalo/enzimologia
Quimiocina CCL2/genética
Quimiocina CCL2/metabolismo
Fracionamento de Dose
Regulação Enzimológica da Expressão Gênica/efeitos da radiação
Inflamação/enzimologia
Inflamação/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Microglia/efeitos da radiação
NADPH Oxidase 2
Oxirredução/efeitos da radiação
Estresse Oxidativo/efeitos da radiação
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
Fator de Necrose Tumoral alfa/genética
Fator de Necrose Tumoral alfa/metabolismo
Regulação para Cima/efeitos da radiação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Ccl2 protein, mouse); 0 (Chemokine CCL2); 0 (Membrane Glycoproteins); 0 (RNA, Messenger); 0 (Tumor Necrosis Factor-alpha); EC 1.6.3.- (Cybb protein, mouse); EC 1.6.3.- (NADPH Oxidase 2); EC 1.6.3.- (NADPH Oxidases)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM; S
[Da] Data de entrada para processamento:170908
[St] Status:MEDLINE
[do] DOI:10.1080/09553002.2017.1377360


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[PMID]:28844481
[Au] Autor:Bai J; Yu XJ; Liu KL; Wang FF; Li HB; Shi XL; Zhang Y; Huo CJ; Li X; Gao HL; Qi J; Liu JJ; Zhu GQ; Chen WS; Cui W; Kang YM
[Ad] Endereço:Department of Physiology and Pathophysiology, Xi'an Jiaotong University School of Basic Medical Sciences, Key Laboratory of Environment and Genes Related to Diseases (Xi'an Jiaotong University), Ministry of Education, Xi'an 710061, China.
[Ti] Título:Tert-butylhydroquinone attenuates oxidative stress and inflammation in hypothalamic paraventricular nucleus in high salt-induced hypertension.
[So] Source:Toxicol Lett;281:1-9, 2017 Nov 05.
[Is] ISSN:1879-3169
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:Excessive oxidative stress and inflammation in hypothalamic paraventricular nucleus (PVN) are implicated in the pathogenesis of hypertension. It is reported that tert-butylhydroquinone (tBHQ), a nuclear factor erythroid 2-related factor 2(Nrf2)-inducer, has a variety of pharmacological activities such as anti-oxidation and anti-inflammatory effect. The objective of this study was to investigate the effects of tBHQ in high salt induced hypertension and to identify whether the beneficial effects were induced by inhibiting PVN oxidative stress and inflammation. Male Sprague-Dawley rats were fed with high salt diet (HS, 8% NaCl) or normal salt diet (NS, 0.3% NaCl). These rats were administration of tBHQ (150mg/kg/d) by oral gavage for 16 weeks. Our results showed that high salt intake resulted in higher mean arterial pressure, cardiac hypertrophy as well as increased plasma level of norepinephrine and interleukin (IL)-1ß, IL-6 compared with NS rats. It increased PVN level of reactive oxygen species, gp91 , IL-1ß, IL-6, p-IKKß and nuclear factor-kappa B (NF-κB) activity, decreased PVN level of Nrf2 and Cu/Zn-SOD. Chronic administration of tBHQ significantly attenuated these changes in HS rats. These data suggest that the protective effects of tBHQ in salt induced hypertension are partly due to inhibiting oxidative stress and inflammation in PVN.
[Mh] Termos MeSH primário: Hidroquinonas/farmacologia
Hipertensão/tratamento farmacológico
Inflamação/tratamento farmacológico
Estresse Oxidativo/efeitos dos fármacos
Núcleo Hipotalâmico Paraventricular/efeitos dos fármacos
Cloreto de Sódio na Dieta/efeitos adversos
[Mh] Termos MeSH secundário: Animais
Antioxidantes/farmacologia
Pressão Arterial
Modelos Animais de Doenças
Hipertensão/induzido quimicamente
Interleucina-1beta/sangue
Interleucina-6/sangue
Masculino
Glicoproteínas de Membrana/sangue
NADPH Oxidase 2
NADPH Oxidases/sangue
Fator 2 Relacionado a NF-E2/genética
Fator 2 Relacionado a NF-E2/metabolismo
Norepinefrina/sangue
Núcleo Hipotalâmico Paraventricular/metabolismo
Ratos
Ratos Sprague-Dawley
Espécies Reativas de Oxigênio/metabolismo
Cloreto de Sódio na Dieta/administração & dosagem
Superóxido Dismutase/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Hydroquinones); 0 (Interleukin-1beta); 0 (Interleukin-6); 0 (Membrane Glycoproteins); 0 (NF-E2-Related Factor 2); 0 (Nfe2l2 protein, rat); 0 (Reactive Oxygen Species); 0 (Sodium Chloride, Dietary); C12674942B (2-tert-butylhydroquinone); EC 1.15.1.1 (Superoxide Dismutase); EC 1.6.3.- (Cybb protein, rat); EC 1.6.3.- (NADPH Oxidase 2); EC 1.6.3.- (NADPH Oxidases); X4W3ENH1CV (Norepinephrine)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170829
[St] Status:MEDLINE


  7 / 1742 MEDLINE  
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[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


  8 / 1742 MEDLINE  
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[PMID]:28801234
[Au] Autor:Xu MM; Pu Y; Han D; Shi Y; Cao X; Liang H; Chen X; Li XD; Deng L; Chen ZJ; Weichselbaum RR; Fu YX
[Ad] Endereço:Department of Pathology, University of Texas Southwestern Medical Center, Dallas, TX 75235, USA; Department of Radiation and Cellular Oncology, The Ludwig Center for Metastasis Research, University of Chicago, Chicago, IL 60637, USA.
[Ti] Título:Dendritic Cells but Not Macrophages Sense Tumor Mitochondrial DNA for Cross-priming through Signal Regulatory Protein α Signaling.
[So] Source:Immunity;47(2):363-373.e5, 2017 Aug 15.
[Is] ISSN:1097-4180
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Inhibition of cytosolic DNA sensing represents a strategy that tumor cells use for immune evasion, but the underlying mechanisms are unclear. Here we have shown that CD47-signal regulatory protein α (SIRPα) axis dictates the fate of ingested DNA in DCs for immune evasion. Although macrophages were more potent in uptaking tumor DNA, increase of DNA sensing by blocking the interaction of SIRPα with CD47 preferentially occurred in dendritic cells (DCs) but not in macrophages. Mechanistically, CD47 blockade enabled the activation of NADPH oxidase NOX2 in DCs, which in turn inhibited phagosomal acidification and reduced the degradation of tumor mitochondrial DNA (mtDNA) in DCs. mtDNA was recognized by cyclic-GMP-AMP synthase (cGAS) in the DC cytosol, contributing to type I interferon (IFN) production and antitumor adaptive immunity. Thus, our findings have demonstrated how tumor cells inhibit innate sensing in DCs and suggested that the CD47-SIRPα axis is critical for DC-driven antitumor immunity.
[Mh] Termos MeSH primário: Antígenos de Diferenciação/metabolismo
Neoplasias do Colo/imunologia
DNA Mitocondrial/imunologia
Células Dendríticas/imunologia
Proteínas de Membrana/metabolismo
Receptores Imunológicos/metabolismo
[Mh] Termos MeSH secundário: Animais
Anticorpos Bloqueadores/uso terapêutico
Antígeno CD47/imunologia
Antígeno CD47/metabolismo
Células Cultivadas
Neoplasias do Colo/genética
Neoplasias do Colo/terapia
Apresentação Cruzada
Modelos Animais de Doenças
Seres Humanos
Interferon Tipo I/metabolismo
Macrófagos/imunologia
Glicoproteínas de Membrana/metabolismo
Proteínas de Membrana/genética
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
NADPH Oxidase 2
NADPH Oxidases/metabolismo
Nucleotidiltransferases/metabolismo
Transdução de Sinais
Evasão Tumoral
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antibodies, Blocking); 0 (Antigens, Differentiation); 0 (CD47 Antigen); 0 (DNA, Mitochondrial); 0 (Interferon Type I); 0 (MPYS protein, mouse); 0 (Membrane Glycoproteins); 0 (Membrane Proteins); 0 (Ptpns1 protein, mouse); 0 (Receptors, Immunologic); 0 (SIRPA protein, human); EC 1.6.3.- (CYBB protein, human); EC 1.6.3.- (NADPH Oxidase 2); EC 1.6.3.- (NADPH Oxidases); EC 2.7.7.- (MB21D1 protein, mouse); EC 2.7.7.- (Nucleotidyltransferases)
[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:170813
[St] Status:MEDLINE


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[PMID]:28771483
[Au] Autor:Pepping JK; Vandanmagsar B; Fernandez-Kim SO; Zhang J; Mynatt RL; Bruce-Keller AJ
[Ad] Endereço:Pennington Biomedical Research Center, Louisiana State University System, Baton Rouge, LA, United States of America.
[Ti] Título:Myeloid-specific deletion of NOX2 prevents the metabolic and neurologic consequences of high fat diet.
[So] Source:PLoS One;12(8):e0181500, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:High fat diet-induced obesity is associated with inflammatory and oxidative signaling in macrophages that likely participates in metabolic and physiologic impairment. One key factor that could drive pathologic changes in macrophages is the pro-inflammatory, pro-oxidant enzyme NADPH oxidase. However, NADPH oxidase is a pleiotropic enzyme with both pathologic and physiologic functions, ruling out indiscriminant NADPH oxidase inhibition as a viable therapy. To determine if targeted inhibition of monocyte/macrophage NADPH oxidase could mitigate obesity pathology, we generated mice that lack the NADPH oxidase catalytic subunit NOX2 in myeloid lineage cells. C57Bl/6 control (NOX2-FL) and myeloid-deficient NOX2 (mNOX2-KO) mice were given high fat diet for 16 weeks, and subject to comprehensive metabolic, behavioral, and biochemical analyses. Data show that mNOX2-KO mice had lower body weight, delayed adiposity, attenuated visceral inflammation, and decreased macrophage infiltration and cell injury in visceral adipose relative to control NOX2-FL mice. Moreover, the effects of high fat diet on glucose regulation and circulating lipids were attenuated in mNOX2-KO mice. Finally, memory was impaired and markers of brain injury increased in NOX2-FL, but not mNOX2-KO mice. Collectively, these data indicate that NOX2 signaling in macrophages participates in the pathogenesis of obesity, and reinforce a key role for macrophage inflammation in diet-induced metabolic and neurologic decline. Development of macrophage/immune-specific NOX-based therapies could thus potentially be used to preserve metabolic and neurologic function in the context of obesity.
[Mh] Termos MeSH primário: Cognição
Dieta Hiperlipídica/efeitos adversos
Deleção de Genes
Glicoproteínas de Membrana/deficiência
Glicoproteínas de Membrana/genética
Células Mieloides/metabolismo
NADPH Oxidases/deficiência
NADPH Oxidases/genética
[Mh] Termos MeSH secundário: Animais
Composição Corporal/genética
Peso Corporal/genética
Encéfalo/fisiologia
Linhagem da Célula
Técnicas de Inativação de Genes
Gordura Intra-Abdominal/metabolismo
Camundongos
NADPH Oxidase 2
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Glycoproteins); EC 1.6.3.- (Cybb protein, mouse); 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:170804
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0181500


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[PMID]:28733324
[Au] Autor:Marlein CR; Zaitseva L; Piddock RE; Robinson SD; Edwards DR; Shafat MS; Zhou Z; Lawes M; Bowles KM; Rushworth SA
[Ad] Endereço:Norwich Medical School and.
[Ti] Título:NADPH oxidase-2 derived superoxide drives mitochondrial transfer from bone marrow stromal cells to leukemic blasts.
[So] Source:Blood;130(14):1649-1660, 2017 Oct 05.
[Is] ISSN:1528-0020
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Improvements in the understanding of the metabolic cross-talk between cancer and its microenvironment are expected to lead to novel therapeutic approaches. Acute myeloid leukemia (AML) cells have increased mitochondria compared with nonmalignant CD34 hematopoietic progenitor cells. Furthermore, contrary to the Warburg hypothesis, AML relies on oxidative phosphorylation to generate adenosine triphosphate. Here we report that in human AML, NOX2 generates superoxide, which stimulates bone marrow stromal cells (BMSC) to AML blast transfer of mitochondria through AML-derived tunneling nanotubes. Moreover, inhibition of NOX2 was able to prevent mitochondrial transfer, increase AML apoptosis, and improve NSG AML mouse survival. Although mitochondrial transfer from BMSC to nonmalignant CD34 cells occurs in response to oxidative stress, NOX2 inhibition had no detectable effect on nonmalignant CD34 cell survival. Taken together, we identify tumor-specific dependence on NOX2-driven mitochondrial transfer as a novel therapeutic strategy in AML.
[Mh] Termos MeSH primário: Leucemia Mieloide Aguda/patologia
Glicoproteínas de Membrana/metabolismo
Células Mesenquimais Estromais/patologia
Mitocôndrias/patologia
NADPH Oxidases/metabolismo
Superóxidos/metabolismo
[Mh] Termos MeSH secundário: Animais
Antígenos CD34/metabolismo
Células-Tronco Hematopoéticas/metabolismo
Células-Tronco Hematopoéticas/patologia
Seres Humanos
Leucemia Mieloide Aguda/metabolismo
Células Mesenquimais Estromais/metabolismo
Camundongos
Mitocôndrias/metabolismo
NADPH Oxidase 2
Estresse Oxidativo
Espécies Reativas de Oxigênio/metabolismo
Células Tumorais Cultivadas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antigens, CD34); 0 (Membrane Glycoproteins); 0 (Reactive Oxygen Species); 11062-77-4 (Superoxides); EC 1.6.3.- (CYBB protein, human); EC 1.6.3.- (Cybb protein, mouse); EC 1.6.3.- (NADPH Oxidase 2); EC 1.6.3.- (NADPH Oxidases)
[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:170723
[St] Status:MEDLINE
[do] DOI:10.1182/blood-2017-03-772939



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