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[PMID]:29320567
[Au] Autor:Gil-Cayuela C; Ortega A; Tarazón E; Martínez-Dolz L; Cinca J; González-Juanatey JR; Lago F; Roselló-Lletí E; Rivera M; Portolés M
[Ad] Endereço:Cardiocirculatory Unit, Health Research Institute of La Fe University Hospital (IIS La Fe), Valencia, Spain.
[Ti] Título:Myocardium of patients with dilated cardiomyopathy presents altered expression of genes involved in thyroid hormone biosynthesis.
[So] Source:PLoS One;13(1):e0190987, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:BACKGROUND: The association between dilated cardiomyopathy (DCM) and low thyroid hormone (TH) levels has been previously described. In these patients abnormal thyroid function is significantly related to impaired left ventricular (LV) function and increased risk of death. Although TH was originally thought to be produced exclusively by the thyroid gland, we recently reported TH biosynthesis in the human ischemic heart. OBJECTIVES: Based on these findings, we evaluated whether the genes required for TH production are also altered in patients with DCM. METHODS: Twenty-three LV tissue samples were obtained from patients with DCM (n = 13) undergoing heart transplantation and control donors (n = 10), and used for RNA sequencing analysis. The number of LV DCM samples was increased to 23 to determine total T4 and T3 tissue levels by ELISA. RESULTS: We found that all components of TH biosynthesis are expressed in human dilated heart tissue. Expression of genes encoding thyroperoxidase (-2.57-fold, P < 0.05) and dual oxidase 2 (2.64-fold, P < 0.01), the main enzymatic system of TH production, was significantly altered in patients with DCM and significantly associated with LV remodeling parameters. Thyroxine (T4) cardiac tissue levels were significantly increased (P < 0.01), whilst triiodothyronine (T3) levels were significantly diminished (P < 0.05) in the patients. CONCLUSIONS: Expression of TH biosynthesis machinery in the heart and total tissue levels of T4 and T3, are altered in patients with DCM. Given the relevance of TH in cardiac pathology, our results provide a basis for new gene-based therapeutic strategies for treating DCM.
[Mh] Termos MeSH primário: Autoantígenos/genética
Cardiomiopatia Dilatada/genética
Oxidases Duais/genética
Iodeto Peroxidase/genética
Proteínas de Ligação ao Ferro/genética
Miocárdio/metabolismo
Receptores da Tireotropina/genética
Hormônios Tireóideos/biossíntese
[Mh] Termos MeSH secundário: Autoantígenos/metabolismo
Biomarcadores/metabolismo
Cardiomiopatia Dilatada/patologia
Estudos de Casos e Controles
Oxidases Duais/metabolismo
Feminino
Perfilação da Expressão Gênica
Regulação da Expressão Gênica
Sequenciamento de Nucleotídeos em Larga Escala/métodos
Seres Humanos
Iodeto Peroxidase/metabolismo
Proteínas de Ligação ao Ferro/metabolismo
Masculino
Meia-Idade
Receptores da Tireotropina/metabolismo
Remodelação Ventricular
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Autoantigens); 0 (Biomarkers); 0 (Iron-Binding Proteins); 0 (Receptors, Thyrotropin); 0 (Thyroid Hormones); EC 1.11.1.- (Dual Oxidases); EC 1.11.1.7 (TPO protein, human); EC 1.11.1.8 (Iodide Peroxidase); EC 1.6.3.1 (DUOX2 protein, human)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180212
[Lr] Data última revisão:
180212
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180111
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0190987


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[PMID]:29227594
[Au] Autor:Bazalii AV; Horak IR; Pasi chn yk GV; Komisarenko SV; Drobot LB
[Ti] Título:Transcriptional regulation of NOX genes express ion in human breast adenocarcinoma MCF-7 cells is modulated by adaptor protein Ruk/CIN 85.
[So] Source:Ukr Biochem J;88(1):119-25, 2016 Jan-Feb.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:NADPH oxidases are key components of redox-dependent signaling networks involved in the control of cancer cell proliferation, survival and invasion. The data have been accumulated that demonstrate specific expression patterns and levels of NADPH oxidase homologues (NOXs) and accessory genes in human cancer cell lines and primary tumors as well as modulation of these parameters by extracellular cues. Our previous studies revealed that ROS production by human colorectal adenocarcinoma HT-29 cells is positively correlated with adaptor protein Ruk/CIN85 expression while increased levels of Ruk/CIN85 in weakly invasive human breast adenocarcinoma MC F-7 cells contribute to their malignant phenotype through the constitutive activation of Src/Akt pathway. In this study, to investigate whether overexpression of Ruk/CIN85 in MC F-7 cells can influence transcriptional regulation of NOXs genes, the subclones of MCF-7 cells with different levels of Ruk/CIN85 were screened for NOX1, NOX2, NOX3, NOX4, NOX5, DUOX1 and DUOX2 as well as for regulatory subunit p22Phox mRNA contents by quantitative RT-PCR (qPCR). Systemic multidirectional changes in mRNA levels for NOX1, NOX2, NOX5, DUOX2 and p22Phox were revealed in Ruk/CIN85 overexpressing cells in comparison to control WT cells. Knocking down of Ruk/CIN85 using technology of RNA-interference resulted in the reversion of these changes. Further studies are necessary to elucidate, by which molecular mechanisms Ruk/CIN85 could affect transcriptional regulation of NOXs genes.
[Mh] Termos MeSH primário: Proteínas Adaptadoras de Transdução de Sinal/genética
Regulação Neoplásica da Expressão Gênica
NADPH Oxidase 1/genética
Espécies Reativas de Oxigênio/metabolismo
Transcrição Genética
[Mh] Termos MeSH secundário: Proteínas Adaptadoras de Transdução de Sinal/antagonistas & inibidores
Proteínas Adaptadoras de Transdução de Sinal/metabolismo
Células Clonais
Oxidases Duais/genética
Oxidases Duais/metabolismo
Seres Humanos
Isoenzimas/genética
Isoenzimas/metabolismo
Células MCF-7
NADPH Oxidase 1/metabolismo
NADPH Oxidases/genética
NADPH Oxidases/metabolismo
RNA Mensageiro/genética
RNA Mensageiro/metabolismo
RNA Interferente Pequeno/genética
RNA Interferente Pequeno/metabolismo
Reação em Cadeia da Polimerase Via Transcriptase Reversa
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Adaptor Proteins, Signal Transducing); 0 (Isoenzymes); 0 (RNA, Messenger); 0 (RNA, Small Interfering); 0 (Reactive Oxygen Species); 0 (SH3KBP1 protein, human); EC 1.11.1.- (Dual Oxidases); EC 1.6.3.- (NADPH Oxidase 1); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.- (NOX1 protein, human); EC 1.6.3.1 (CYBA protein, human); EC 1.6.3.1 (DUOX1 protein, human); EC 1.6.3.1 (DUOX2 protein, human)
[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/ubj88.01.119


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[PMID]:28709950
[Au] Autor:Lu J; Risbood P; Kane CT; Hossain MT; Anderson L; Hill K; Monks A; Wu Y; Antony S; Juhasz A; Liu H; Jiang G; Harris E; Roy K; Meitzler JL; Konaté M; Doroshow JH
[Ad] Endereço:Center for Cancer Research, National Cancer Institute, Bethesda, MD 20892, USA.
[Ti] Título:Characterization of potent and selective iodonium-class inhibitors of NADPH oxidases.
[So] Source:Biochem Pharmacol;143:25-38, 2017 Nov 01.
[Is] ISSN:1873-2968
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The NADPH oxidases (NOXs) play a recognized role in the development and progression of inflammation-associated disorders, as well as cancer. To date, several NOX inhibitors have been developed, through either high throughput screening or targeted disruption of NOX interaction partners, although only a few have reached clinical trials. To improve the efficacy and bioavailability of the iodonium class NOX inhibitor diphenylene iodonium (DPI), we synthesized 36 analogs of DPI, focusing on improved solubility and functionalization. The inhibitory activity of the analogs was interrogated through cell viability and clonogenic studies with a colon cancer cell line (HT-29) that depends on NOX for its proliferative potential. Lack of altered cellular respiration at relevant iodonium analog concentrations was also demonstrated. Additionally, inhibition of ROS generation was evaluated with a luminescence assay for superoxide, or by Amplex Red® assay for H O production, in cell models expressing specific NOX isoforms. DPI and four analogs (NSCs 740104, 751140, 734428, 737392) strongly inhibited HT-29 cell growth and ROS production with nanomolar potency in a concentration-dependent manner. NSC 737392 and 734428, which both feature nitro functional groups at the meta position, had >10-fold higher activity against ROS production by cells that overexpress dual oxidase 2 (DUOX2) than the other compounds examined (IC ≈200-400nM). Based on these results, we synthesized and tested NSC 780521 with optimized potency against DUOX2. Iodonium analogs with anticancer activity, including the first generation of targeted agents with improved specificity against DUOX2, may provide a novel therapeutic approach to NOX-driven tumors.
[Mh] Termos MeSH primário: Proliferação Celular/efeitos dos fármacos
Inibidores Enzimáticos/farmacologia
NADH NADPH Oxirredutases/antagonistas & inibidores
Oniocompostos/farmacologia
Tiofenos/farmacologia
[Mh] Termos MeSH secundário: Sobrevivência Celular/efeitos dos fármacos
Relação Dose-Resposta a Droga
Oxidases Duais
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Células HT29
Seres Humanos
Estrutura Molecular
NADH NADPH Oxirredutases/genética
NADPH Oxidases/antagonistas & inibidores
NADPH Oxidases/genética
Oniocompostos/síntese química
Oniocompostos/química
Consumo de Oxigênio/efeitos dos fármacos
Espécies Reativas de Oxigênio/antagonistas & inibidores
Tiofenos/síntese química
Tiofenos/química
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Enzyme Inhibitors); 0 (Onium Compounds); 0 (Reactive Oxygen Species); 0 (Thiophenes); 45955-43-9 (iodonium thiophene); 6HJ411TU98 (diphenyleneiodonium); EC 1.11.1.- (Dual Oxidases); EC 1.6.- (NADH, NADPH Oxidoreductases); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.1 (DUOX2 protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170716
[St] Status:MEDLINE


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[PMID]:28633507
[Au] Autor:Aycan Z; Cangul H; Muzza M; Bas VN; Fugazzola L; Chatterjee VK; Persani L; Schoenmakers N
[Ad] Endereço:Division of Paediatric Endocrinology, Dr. Sami Ulus Woman Health and Children Research Hospital, 06080 Ankara, Turkey.
[Ti] Título:Digenic DUOX1 and DUOX2 Mutations in Cases With Congenital Hypothyroidism.
[So] Source:J Clin Endocrinol Metab;102(9):3085-3090, 2017 Sep 01.
[Is] ISSN:1945-7197
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Context: The DUOX2 enzyme generates hydrogen peroxide (H2O2), a crucial electron acceptor for the thyroid peroxidase-catalyzed iodination and coupling reactions mediating thyroid hormone biosynthesis. DUOX2 mutations result in dyshormonogenetic congenital hypothyroidism (CH) that may be phenotypically heterogeneous, leading to the hypothesis that CH severity may be influenced by environmental factors (e.g., dietary iodine) and oligogenic modifiers (e.g., variants in the homologous reduced form of NAD phosphate-oxidase DUOX1). However, loss-of-function mutations in DUOX1 have not hitherto been described, and its role in thyroid biology remains undefined. Case Description: We previously described a Proband and her brother (P1, P2) with unusually severe CH associated with a DUOX2 homozygous nonsense mutation (p.R434*); P1, P2: thyrotropin >100 µU/mL [reference range (RR) 0.5 to 6.3]; and P1: free T4 (FT4) <0.09 ng/dL (RR 0.9 to 2.3). Subsequent studies have revealed a homozygous DUOX1 mutation (c.1823-1G>C) resulting in aberrant splicing and a protein truncation (p.Val607Aspfs*43), which segregates with CH in this kindred. Conclusion: This is a report of digenic mutations in DUOX1 and DUOX2 in association with CH, and we hypothesize that the inability of DUOX1 to compensate for DUOX2 deficiency in this kindred may underlie the severe CH phenotype. Our studies provide evidence for a digenic basis for CH and support the notion that oligogenicity as well as environmental modulators may underlie phenotypic variability in genetically ascertained CH.
[Mh] Termos MeSH primário: Hipotireoidismo Congênito/diagnóstico
Hipotireoidismo Congênito/genética
Predisposição Genética para Doença
NADPH Oxidases/genética
[Mh] Termos MeSH secundário: Códon sem Sentido
Estudos de Coortes
Oxidases Duais
Feminino
Variação Genética
Genótipo
Seres Humanos
Lactente
Recém-Nascido
Masculino
NADPH Oxidases/metabolismo
Linhagem
Fenótipo
Estudos Retrospectivos
Índice de Gravidade de Doença
Testes de Função Tireóidea
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Codon, Nonsense); EC 1.11.1.- (Dual Oxidases); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.1 (DUOX1 protein, human); EC 1.6.3.1 (DUOX2 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:170622
[St] Status:MEDLINE
[do] DOI:10.1210/jc.2017-00529


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[PMID]:28541007
[Au] Autor:Zheng X; Ma SG; Guo ML; Qiu YL; Yang LX
[Ad] Endereço:Department of Endocrinology and Metabolism, Puren Hospital Affiliated to Wuhan University of Science and Technology, Wuhan, P.R. China.
[Ti] Título:Compound Heterozygous Mutations in the DUOX2/DUOXA2 Genes Cause Congenital Hypothyroidism.
[So] Source:Yonsei Med J;58(4):888-890, 2017 Jul.
[Is] ISSN:1976-2437
[Cp] País de publicação:Korea (South)
[La] Idioma:eng
[Ab] Resumo:The mutations in the dual oxidase 2 (DUOX2) and dual oxidase maturation factor 2 (DUOXA2) genes can cause congenital hypothyroidism (CH). This study reports the pedigree with goitrous congenital hypothyroidism (GCH) due to the coexistence of heterozygous mutations in the DUOX2 and DUOXA2 genes. The two sisters with GCH were diagnosed with CH at neonatal screening and were enrolled in this study. The DUOX2, DUOXA2, and thyroid peroxidase (TPO) genes were considered for genetic defects screening. Family members of the patients and normal controls were also enrolled and evaluated. The two girls harbored compound heterozygous mutations, including a new mutation of c.2654G>T (p.R885L) in the maternal DUOX2 allele and c.738C>G (p.Y246X) in the paternal DUOXA2 allele, that has been previously reported. The germline mutations from the families were consistent with an autosomal recessive inheritance pattern. No mutations in the TPO gene and the controls were observed.
[Mh] Termos MeSH primário: Hipotireoidismo Congênito/genética
Predisposição Genética para Doença
Proteínas de Membrana/genética
Mutação/genética
NADPH Oxidases/genética
[Mh] Termos MeSH secundário: Sequência de Bases
Hipotireoidismo Congênito/sangue
Oxidases Duais
Éxons/genética
Família
Feminino
Heterozigoto
Seres Humanos
Recém-Nascido
Masculino
Linhagem
[Pt] Tipo de publicação:CASE REPORTS
[Nm] Nome de substância:
0 (DUOXA2 protein, human); 0 (Membrane Proteins); EC 1.11.1.- (Dual Oxidases); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.1 (DUOX2 protein, human)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170526
[St] Status:MEDLINE
[do] DOI:10.3349/ymj.2017.58.4.888


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[PMID]:28273705
[Au] Autor:Huang YL; Tan MY; Jiang X; Li B; Chen QY; Jia XF; Tang CF; Liu JL; Liu L
[Ad] Endereço:Department of Guangzhou Newborn Screening Center, Guangzhou Women and Children's Medical Center, Guangzhou 510180, China.
[Ti] Título:[Genetic analysis of TPO, DUOX2 and DUOXA2 genes in children with permanent congenital hypothyroidism suspected dyshormonogenesis].
[So] Source:Zhonghua Er Ke Za Zhi;55(3):210-214, 2017 Mar 02.
[Is] ISSN:0578-1310
[Cp] País de publicação:China
[La] Idioma:chi
[Ab] Resumo:To explore the TPO, DUOX2 and DUOXA2 genotypes and phenotypes of children with permanent congenital hypothyroidism(PCH) suspected dyshormonogenesis in Guangzhou, identified and treated at Guangzhou Newborn Screening Center. Six of them were born between 2011 and 2012. Retrospectively analyzed the clinical data of 9 children with PCH suspected dyshormonogenesis. Genetic analysis of TPO, DUOX2 and DUOXA2 genes were performed with Sanger sequencing. Of the 9 patients, four were identified variants in TPO gene including three cases with biallelic variants and one case with monoallelic variant. Novel c. 1784G>C( p. R595T) variant in TPO was predicted to be damaging by SIFT and PolyPhen-2. Four patients harbored monoallelic known variants in DUOX2 gene and the other one harbored heterozygous known mutation c. 738C>G(p.Y246X) in DUOXA2 gene.Two adolescent patients with biallelic variants in TPO gene showed classical PCH phenotypes with thyroid goiter or nodules. The six patients with monoallelic variant in TPO, DUOX2 or DUOXA2 presented variable phenotypes. Among the 433 578 newborns in the 2011-2012 cohort, there were 156 cases of CH. Six of these cases were PCH suspected dyshormonogenesis, among which 1 case was confirmed TPO biallelic variants and 5 cases were monoallelic variants of TPO, DUOX2, or DUOXA2 genes. TPO and DUOX2 variants are the common molecular pathogenesis in children with PCH suspected dyshormonogenesis. Monoallelic variants in TPO, DUOX2 or DUOXA2 are associated with PCH and showed wide variability in their phenotypes. The novel variant p. R595T in TPO is probably a pathologic variant. The prevalence of PCH caused by TPO gene defects is rare in Guangzhou.
[Mh] Termos MeSH primário: Hipotireoidismo Congênito/genética
Testes Genéticos
Glicoproteínas de Membrana
Proteínas de Membrana
NADPH Oxidases
[Mh] Termos MeSH secundário: Oxidases Duais
Genótipo
Bócio
Heterozigoto
Seres Humanos
Recém-Nascido
Mutação
Triagem Neonatal
Fenótipo
Prevalência
Estudos Retrospectivos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DUOXA2 protein, human); 0 (Membrane Glycoproteins); 0 (Membrane Proteins); 0 (TOP protein, human); EC 1.11.1.- (Dual Oxidases); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.1 (DUOX2 protein, human)
[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:170309
[St] Status:MEDLINE
[do] DOI:10.3760/cma.j.issn.0578-1310.2017.03.009


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[PMID]:28028364
[Au] Autor:Chu FF; Esworthy RS; Doroshow JH; Shen B
[Ad] Endereço:Fong-Fong Chu, Department of Gastroenterology and Hepatology, The First Affiliated Hospital and College of Clinical Medicine of Henan University of Science and Technology, Luoyang 471003, Henan Province, China.
[Ti] Título:NADPH oxidase-1 deficiency offers little protection in -induced typhlitis in mice.
[So] Source:World J Gastroenterol;22(46):10158-10165, 2016 Dec 14.
[Is] ISSN:2219-2840
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:AIM: To test whether Nox1 plays a role in typhlitis induced by Typhimurium (S. Tm) in a mouse model. METHODS: Eight-week-old male wild-type (WT) and Nox1 knockout (KO) C57BL6/J (B6) mice were administered metronidazole water for 4 d to make them susceptible to S. Tm infection by the oral route. The mice were given plain water and administered with 4 different doses of S. Tm by oral gavage. The mice were followed for another 4 d. From the time of the metronidazole application, the mice were observed twice daily and weighed daily. The ileum, cecum and colon were removed for sampling at the fourth day post-inoculation. Portions of all three tissues were fixed for histology and placed in RNAlater for mRNA/cDNA preparation and quantitative real-time PCR. The contents of the cecum were recovered for estimation of S. Tm CFU. RESULTS: We found Nox1-knockout (Nox1-KO) mice were not more sensitive to S. Tm colonization and infection than WT B6 mice. This conclusion is based on the following observations: (1) S. Tm-infection induced similar weight loss in Nox1-KO mice compared to WT mice; (2) the same S. Tm CFU was recovered from the cecal content of Nox1-KO and WT mice regardless of the inoculation dose, except the lowest inoculation dose (2 × 10 CFU) for which the Nox1-KO had one-log lower CFU than WT mice; (3) there is no difference in cecal pathology between WT and Nox1-KO groups; and (4) there are no S. Tm infection-induced changes in gene expression levels (IL-1b, TNF-α, and Duox2) between WT and Nox1-KO groups. The Alpi gene expression was more suppressed by S. Tm treatment in WT than the Nox1-KO cecum. CONCLUSION: Nox1 does not protect mice from S. Tm colonization. Nox1-KO provides a very minor protective effect against S. Tm infection. Using NOX1-specific inhibitors for colitis therapy should not increase risks in bacterial infection.
[Mh] Termos MeSH primário: Ceco/metabolismo
NADH NADPH Oxirredutases/genética
RNA Mensageiro/metabolismo
Infecções por Salmonella/genética
Tiflite/genética
[Mh] Termos MeSH secundário: Fosfatase Alcalina/genética
Animais
Ceco/patologia
Modelos Animais de Doenças
Oxidases Duais
Expressão Gênica
Predisposição Genética para Doença
Interleucina-1beta/genética
Masculino
Camundongos
Camundongos Endogâmicos C57BL
Camundongos Knockout
NADPH Oxidase 1
NADPH Oxidases/genética
Reação em Cadeia da Polimerase em Tempo Real
Infecções por Salmonella/metabolismo
Infecções por Salmonella/patologia
Salmonella typhimurium
Fator de Necrose Tumoral alfa/genética
Tiflite/metabolismo
Tiflite/patologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (IL1B protein, mouse); 0 (Interleukin-1beta); 0 (RNA, Messenger); 0 (Tumor Necrosis Factor-alpha); EC 1.11.1.- (Dual Oxidases); EC 1.6.- (NADH, NADPH Oxidoreductases); EC 1.6.3.- (NADPH Oxidase 1); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.- (NOX1 protein, mouse); EC 1.6.3.1 (Duox1 protein, mouse); EC 3.1.3.1 (Alkaline Phosphatase)
[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:161229
[St] Status:MEDLINE
[do] DOI:10.3748/wjg.v22.i46.10158


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[PMID]:27650496
[Au] Autor:Heppner DE; Hristova M; Dustin CM; Danyal K; Habibovic A; van der Vliet A
[Ad] Endereço:From the Department of Pathology and Laboratory Medicine, University of Vermont, Burlington, Vermont 05405.
[Ti] Título:The NADPH Oxidases DUOX1 and NOX2 Play Distinct Roles in Redox Regulation of Epidermal Growth Factor Receptor Signaling.
[So] Source:J Biol Chem;291(44):23282-23293, 2016 10 28.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:The epidermal growth factor receptor (EGFR) plays a critical role in regulating airway epithelial homeostasis and responses to injury. Activation of EGFR is regulated by redox-dependent processes involving reversible cysteine oxidation by reactive oxygen species (ROS) and involves both ligand-dependent and -independent mechanisms, but the precise source(s) of ROS and the molecular mechanisms that control tyrosine kinase activity are incompletely understood. Here, we demonstrate that stimulation of EGFR activation by ATP in airway epithelial cells is closely associated with dynamic reversible oxidation of cysteine residues via sequential sulfenylation and S-glutathionylation within EGFR and the non-receptor-tyrosine kinase Src. Moreover, the intrinsic kinase activity of recombinant Src or EGFR was in both cases enhanced by H O but not by GSSG, indicating that the intermediate sulfenylation is the activating modification. H O -induced increase in EGFR tyrosine kinase activity was not observed with the C797S variant, confirming Cys-797 as the redox-sensitive cysteine residue that regulates kinase activity. Redox-dependent regulation of EGFR activation in airway epithelial cells was found to strongly depend on activation of either the NADPH oxidase DUOX1 or the homolog NOX2, depending on the activation mechanism. Whereas DUOX1 and Src play a primary role in EGFR transactivation by wound-derived signals such as ATP, direct ligand-dependent EGFR activation primarily involves NOX2 with a secondary role for DUOX1 and Src. Collectively, our findings establish that redox-dependent EGFR kinase activation involves a dynamic and reversible cysteine oxidation mechanism and that this activation mechanism variably involves DUOX1 and NOX2.
[Mh] Termos MeSH primário: Glicoproteínas de Membrana/metabolismo
NADPH Oxidases/metabolismo
Receptor do Fator de Crescimento Epidérmico/metabolismo
Transdução de Sinais
[Mh] Termos MeSH secundário: Animais
Oxidases Duais
Células Epiteliais/enzimologia
Células Epiteliais/metabolismo
Feminino
Masculino
Glicoproteínas de Membrana/genética
Camundongos
Camundongos Endogâmicos C57BL
NADPH Oxidase 2
NADPH Oxidases/genética
Oxirredução
Espécies Reativas de Oxigênio/metabolismo
Receptor do Fator de Crescimento Epidérmico/genética
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Membrane Glycoproteins); 0 (Reactive Oxygen Species); EC 1.11.1.- (Dual Oxidases); EC 1.6.3.- (Cybb protein, mouse); EC 1.6.3.- (NADPH Oxidase 2); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.1 (Duox1 protein, mouse); EC 2.7.10.1 (Receptor, Epidermal Growth Factor)
[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:160922
[St] Status:MEDLINE


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[PMID]:27612966
[Au] Autor:Danyal K; de Jong W; O'Brien E; Bauer RA; Heppner DE; Little AC; Hristova M; Habibovic A; van der Vliet A
[Ad] Endereço:Department of Pathology and Laboratory Medicine, College of Medicine, University of Vermont, Burlington, Vermont.
[Ti] Título:Acrolein and thiol-reactive electrophiles suppress allergen-induced innate airway epithelial responses by inhibition of DUOX1 and EGFR.
[So] Source:Am J Physiol Lung Cell Mol Physiol;311(5):L913-L923, 2016 Nov 01.
[Is] ISSN:1522-1504
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Acrolein is a major thiol-reactive component of cigarette smoke (CS) that is thought to contribute to increased asthma incidence associated with smoking. Here, we explored the effects of acute acrolein exposure on innate airway responses to two common airborne allergens, house dust mite and Alternaria alternata, and observed that acrolein exposure of C57BL/6 mice (5 ppm, 4 h) dramatically inhibited innate airway responses to subsequent allergen challenge, demonstrated by attenuated release of the epithelial-derived cytokines IL-33, IL-25, and IL-1α. Acrolein and other anti-inflammatory thiol-reactive electrophiles, cinnamaldehyde, curcumin, and sulforaphane, similarly inhibited allergen-induced production of these cytokines from human or murine airway epithelial cells in vitro. Based on our previous observations indicating the importance of Ca -dependent signaling, activation of the NADPH oxidase DUOX1, and Src/EGFR-dependent signaling in allergen-induced epithelial secretion of these cytokines, we explored the impact of acrolein on these pathways. Acrolein and other thiol-reactive electrophiles were found to dramatically prevent allergen-induced activation of DUOX1 as well as EGFR, and acrolein was capable of inhibiting EGFR tyrosine kinase activity via modification of C797. Biotin-labeling strategies indicated increased cysteine modification and carbonylation of Src, EGFR, as well as DUOX1, in response to acrolein exposure in vitro and in vivo, suggesting that direct alkylation of these proteins on accessible cysteine residues may be responsible for their inhibition. Collectively, our findings indicate a novel anti-inflammatory mechanism of CS-derived acrolein and other thiol-reactive electrophiles, by directly inhibiting DUOX1- and EGFR-mediated airway epithelial responses to airborne allergens.
[Mh] Termos MeSH primário: Acroleína/farmacologia
Alérgenos/efeitos adversos
Brônquios/patologia
Células Epiteliais/metabolismo
NADPH Oxidases/antagonistas & inibidores
Receptor do Fator de Crescimento Epidérmico/metabolismo
Compostos de Sulfidrila/farmacologia
[Mh] Termos MeSH secundário: Acroleína/química
Administração por Inalação
Animais
Cálcio/metabolismo
Cisteína/metabolismo
Oxidases Duais
Ativação Enzimática/efeitos dos fármacos
Células Epiteliais/efeitos dos fármacos
Seres Humanos
Peróxido de Hidrogênio/metabolismo
Imunidade Inata/efeitos dos fármacos
Interleucina-33/secreção
Camundongos Endogâmicos C57BL
NADPH Oxidases/metabolismo
Carbonilação Proteica/efeitos dos fármacos
Pyroglyphidae/efeitos dos fármacos
Pyroglyphidae/fisiologia
Compostos de Sulfidrila/química
Quinases da Família src/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Allergens); 0 (Interleukin-33); 0 (Sulfhydryl Compounds); 7864XYD3JJ (Acrolein); BBX060AN9V (Hydrogen Peroxide); EC 1.11.1.- (Dual Oxidases); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.1 (Duox1 protein, mouse); EC 2.7.10.1 (Receptor, Epidermal Growth Factor); EC 2.7.10.2 (src-Family Kinases); K848JZ4886 (Cysteine); SY7Q814VUP (Calcium)
[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:160911
[St] Status:MEDLINE
[do] DOI:10.1152/ajplung.00276.2016


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[PMID]:27557340
[Au] Autor:Tan M; Huang Y; Jiang X; Li P; Tang C; Jia X; Chen Q; Chen W; Sheng H; Feng Y; Wu D; Liu L
[Ad] Endereço:Department of Guangzhou Neonatal Screening Center, Guangzhou Women and Children's Medical Center, Guangzhou Medical University, Renminzhong Road, Guangzhou, China.
[Ti] Título:The Prevalence, Clinical, and Molecular Characteristics of Congenital Hypothyroidism Caused by DUOX2 Mutations: A Population-Based Cohort Study in Guangzhou.
[So] Source:Horm Metab Res;48(9):581-8, 2016 Sep.
[Is] ISSN:1439-4286
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Thyroid dyshormonogenesis (DH) has recently been reported to be more frequently associated with mutations in the dual oxidase 2 (DUOX2) gene. The present study was aimed to investigate the prevalence, clinical, and molecular characteristics of congenital hypothyroidism (CH) caused by DUOX2 mutations in Guangzhou. A population-based cohort of 156 patients with CH was recruited based on neonatal screening among 433 578 newborns born in Guangzhou from 2011 to 2012. Genetic analysis of DUOX2 was performed in 96 patients with suspected thyroid dyshormonogenesis (SDH) by PCR-amplified direct sequencing. Apart from 2 cases without ultrasonographic data, 118 (76.6%) of the 156 patients were classified as SDH and 36 (23.4%) as thyroid dysgenesis (TD) according to thyroid ultrasound at diagnosis. Genetic analysis revealed 23 different variants in 60 unrelated individuals (60/96, 62.5%), including 13 novel variants that were absent from HGMD, dbSNP databases, and the 50 normal controls. The novel missense variants were predicted to be pathogenic by SIFT and PolyPhen-2. The p.K530X was the most common mutation. Ninety-three percent of mutant alleles occurred in exons 5, 6, 9, 14, 17, 20, 25, 27, and 28. There were no significant differences in phenotypes between biallelic and monoallelic variants cases or between with-DUOX2 and non-DUOX2 variants cases. Most patients with DUOX2 defects (78.2%) were transient CH. In conclusion, the prevalence of DUOX2 pathogenic variants was high (62.5%) in this cohort. Thirteen novel probably pathologic variants were reported. The p.K530X was the most common mutation in the Chinese population. There was no correlation between DUOX2 genotypes and clinical phenotypes.
[Mh] Termos MeSH primário: Hipotireoidismo Congênito/epidemiologia
Hipotireoidismo Congênito/genética
Mutação/genética
NADPH Oxidases/genética
[Mh] Termos MeSH secundário: Estudos de Casos e Controles
China/epidemiologia
Estudos de Coortes
Hipotireoidismo Congênito/patologia
Oxidases Duais
Feminino
Seguimentos
Testes Genéticos
Genótipo
Seres Humanos
Lactente
Recém-Nascido
Masculino
Fenótipo
Prevalência
Prognóstico
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.11.1.- (Dual Oxidases); EC 1.6.3.- (NADPH Oxidases); EC 1.6.3.1 (DUOX2 protein, human)
[Em] Mês de entrada:1703
[Cu] Atualização por classe:171116
[Lr] Data última revisão:
171116
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:160825
[St] Status:MEDLINE
[do] DOI:10.1055/s-0042-112224



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