Base de dados : MEDLINE
Pesquisa : G02.111.595 [Categoria DeCS]
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[PMID]:29307523
[Au] Autor:Wu GJ; Lin YW; Chuang CY; Tsai HC; Chen RM
[Ad] Endereço:Department of Anesthesiology, Shin Kong Wu Ho-Su Memorial Hospital, Taipei, Taiwan; Department of Anesthesiology, School of Medicine, College of Medicine, Taipei Medical University, Taipei, Taiwan.
[Ti] Título:Liver nitrosation and inflammation in septic rats were suppressed by propofol via downregulating TLR4/NF-κB-mediated iNOS and IL-6 gene expressions.
[So] Source:Life Sci;195:25-32, 2018 Feb 15.
[Is] ISSN:1879-0631
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:AIMS: Propofol can be applied as an anesthetic or sedative agent for septic patients. Our previous studies showed that propofol ameliorated inflammation- and nitrosative stress-induced cellular insults. This study further evaluated effects of propofol on cecal ligation and puncture (CLP)-induced septic insults to rats and its possible mechanisms. MAIN METHODS: Wistar rats were administered with CLP and effects of propofol on CLP-induced liver dysfunction and rat death were evaluated. Levels of hepatic or systemic nitrogen oxides (NOx) and interleukin (IL)-6 were quantified. Sequentially, inducible nitric oxide synthase (iNOS) and IL-6 gene expressions, toll-like receptor 4 (TLR4) protein levels, and nuclear factor (NF)-κB translocation were determined. KEY FINDINGS: Subjecting rats to CLP led to body weight loss, liver weight gain, and death. Administration of propofol lessened CLP-induced augmentations of serum and hepatic nitrosative stress and IL-6 levels. Additionally, propofol suppressed CLP-induced enhancements in levels of hepatic iNOS protein. Furthermore, the CLP-induced iNOS and IL-6 mRNA expressions in the liver were inhibited following propofol administration. Sequentially, subjecting rats to CLP enhanced hepatic TLR4 protein levels and NF-κB translocation to nuclei, but propofol inhibited these augmentations. SIGNIFICANCE: Consequently, exposure to propofol protected against CLP-induced liver dysfunction and increased the survival rates of the animals. This study shows that propofol can protect rats against septic insults through suppression of systemic and hepatic nitrosative and inflammatory stress due to inhibition of TLR4/NF-κB-mediated iNOS and IL-6 mRNA and protein expressions.
[Mh] Termos MeSH primário: Hepatite/tratamento farmacológico
Hipnóticos e Sedativos/uso terapêutico
Interleucina-6/biossíntese
Fígado/metabolismo
Fígado/patologia
NF-kappa B/efeitos dos fármacos
Óxido Nítrico Sintase Tipo II/biossíntese
Nitrosação/efeitos dos fármacos
Propofol/uso terapêutico
Sepse/tratamento farmacológico
Receptor 4 Toll-Like/efeitos dos fármacos
[Mh] Termos MeSH secundário: Actinas/metabolismo
Animais
Doenças do Ceco/metabolismo
Doenças do Ceco/patologia
Regulação para Baixo
Regulação da Expressão Gênica/efeitos dos fármacos
Hepatite/metabolismo
Hepatite/patologia
Interleucina-6/genética
Masculino
Óxido Nítrico Sintase Tipo II/genética
Ratos
Ratos Wistar
Sepse/metabolismo
Sepse/patologia
Translocação Genética/efeitos dos fármacos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Actins); 0 (Hypnotics and Sedatives); 0 (Interleukin-6); 0 (NF-kappa B); 0 (Tlr4 protein, rat); 0 (Toll-Like Receptor 4); EC 1.14.13.39 (Nitric Oxide Synthase Type II); EC 1.14.13.39 (Nos2 protein, rat); YI7VU623SF (Propofol)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180208
[Lr] Data última revisão:
180208
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180109
[St] Status:MEDLINE


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[PMID]:29176872
[Au] Autor:Scrima R; Menga M; Pacelli C; Agriesti F; Cela O; Piccoli C; Cotoia A; De Gregorio A; Gefter JV; Cinnella G; Capitanio N
[Ad] Endereço:Department of Clinical and Experimental Medicine, University of Foggia, Foggia, Italy.
[Ti] Título:Para-hydroxyphenylpyruvate inhibits the pro-inflammatory stimulation of macrophage preventing LPS-mediated nitro-oxidative unbalance and immunometabolic shift.
[So] Source:PLoS One;12(11):e0188683, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Targeting metabolism is emerging as a promising therapeutic strategy for modulation of the immune response in human diseases. In the presented study we used the lipopolysaccharide (LPS)-mediated activation of RAW 264.7 macrophage-like cell line as a model to investigate changes in the metabolic phenotype and to test the effect of p-hydroxyphenylpyruvate (pHPP) on it. pHPP is an intermediate of the PHE/TYR catabolic pathway, selected as analogue of the ethyl pyruvate (EP), which proved to exhibit antioxidant and anti-inflammatory activities. The results obtained show that LPS-priming of RAW 264.7 cell line to the activated M1 state resulted in up-regulation of the inducible nitric oxide synthase (iNOS) expression and consequently of NO production and in release of the pro-inflammatory cytokine IL-6. All these effects were prevented dose dependently by mM concentrations of pHPP more efficiently than EP. Respirometric and metabolic flux analysis of LPS-treated RAW 264.7 cells unveiled a marked metabolic shift consisting in downregulation of the mitochondrial oxidative phosphorylation and upregulation of aerobic glycolysis respectively. The observed respiratory failure in LPS-treated cells was accompanied with inhibition of the respiratory chain complexes I and IV and enhanced production of reactive oxygen species. Inhibition of the respiratory activity was also observed following incubation of human neonatal fibroblasts (NHDF-neo) with sera from septic patients. pHPP prevented all the observed metabolic alteration caused by LPS on RAW 264.7 or by septic sera on NHDF-neo. Moreover, we provide evidence that pHPP is an efficient reductant of cytochrome c. On the basis of the presented results a working model, linking pathogen-associated molecular patterns (PAMPs)-mediated immune response to mitochondrial oxidative metabolism, is put forward along with suggestions for its therapeutic control.
[Mh] Termos MeSH primário: Inflamação/imunologia
Inflamação/metabolismo
Lipopolissacarídeos/farmacologia
Macrófagos/imunologia
Macrófagos/metabolismo
[Mh] Termos MeSH secundário: Animais
Anti-Inflamatórios/farmacologia
Respiração Celular/efeitos dos fármacos
Fibroblastos/efeitos dos fármacos
Fibroblastos/metabolismo
Seres Humanos
Subunidade alfa do Fator 1 Induzível por Hipóxia/metabolismo
Inflamação/patologia
Interleucina-6/metabolismo
Macrófagos/efeitos dos fármacos
Análise do Fluxo Metabólico
Camundongos
Mitocôndrias/efeitos dos fármacos
Mitocôndrias/metabolismo
Modelos Biológicos
Nitratos/metabolismo
Óxido Nítrico/biossíntese
Óxido Nítrico Sintase Tipo II/metabolismo
Nitritos/metabolismo
Nitrosação
Oxirredução
Peróxidos/metabolismo
Ácidos Fenilpirúvicos/química
Ácidos Fenilpirúvicos/farmacologia
Piruvatos/química
Piruvatos/farmacologia
Células RAW 264.7
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Anti-Inflammatory Agents); 0 (Hypoxia-Inducible Factor 1, alpha Subunit); 0 (Interleukin-6); 0 (Lipopolysaccharides); 0 (Nitrates); 0 (Nitrites); 0 (Peroxides); 0 (Phenylpyruvic Acids); 0 (Pyruvates); 03O98E01OB (ethyl pyruvate); 156-39-8 (4-hydroxyphenylpyruvic acid); 31C4KY9ESH (Nitric Oxide); EC 1.14.13.39 (Nitric Oxide Synthase Type II)
[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:171128
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0188683


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[PMID]:29061305
[Au] Autor:Tichá T; Lochman J; Cincalová L; Luhová L; Petrivalský M
[Ad] Endereço:Department of Biochemistry, Faculty of Science, Palacký University, Slechtitelu 27, CZ-783 71 Olomouc, Czech Republic.
[Ti] Título:Redox regulation of plant S-nitrosoglutathione reductase activity through post-translational modifications of cysteine residues.
[So] Source:Biochem Biophys Res Commun;494(1-2):27-33, 2017 Dec 09.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nitric oxide (NO) is considered as a signalling molecule involved in a variety of important physiological and pathological processes in plant and animal systems. The major pathway of NO reactions in vivo represents S-nitrosation of thiols to form S-nitrosothiols. S-nitrosoglutathione reductase (GSNOR) is the key enzyme in the degradation pathway of S-nitrosoglutathione (GSNO), a low-molecular weight adduct of NO and glutathione. GSNOR indirectly regulates the level of protein S-nitrosothiol in the cells. This study was focused on the dynamic regulation of the activity of plant GSNORs through reversible S-nitrosation and/or oxidative modifications of target cysteine residues. Pre-incubation with NO/NO donors or hydrogen peroxide resulted in a decreased reductase and dehydrogenase activity of all studied plant GSNORs. Incubation with thiol reducing agent completely reversed inhibitory effects of nitrosative modifications and partially also oxidative inhibition. In biotin-labelled samples, S-nitrosation of plant GSNORs was confirmed after immunodetection and using mass spectrometry S-nitrosation of conserved Cys271 was identified in tomato GSNOR. Negative regulation of constitutive GSNOR activity in vivo by nitrosative or oxidative modifications might present an important mechanism to control GSNO levels, a critical mediator of the downstream signalling effects of NO, as well as for formaldehyde detoxification in dehydrogenase reaction mode.
[Mh] Termos MeSH primário: Aldeído Oxirredutases/metabolismo
Proteínas de Plantas/metabolismo
[Mh] Termos MeSH secundário: Aldeído Oxirredutases/antagonistas & inibidores
Aldeído Oxirredutases/química
Animais
Cisteína/química
Cisteína/metabolismo
Peróxido de Hidrogênio/farmacologia
Lycopersicon esculentum/genética
Lycopersicon esculentum/crescimento & desenvolvimento
Lycopersicon esculentum/metabolismo
Óxido Nítrico/metabolismo
Doadores de Óxido Nítrico/farmacologia
Nitrosação
Oxirredução
Proteínas de Plantas/antagonistas & inibidores
Proteínas de Plantas/química
Processamento de Proteína Pós-Traducional
Proteínas Recombinantes/química
Proteínas Recombinantes/genética
Proteínas Recombinantes/metabolismo
S-Nitrosoglutationa/metabolismo
S-Nitrosotióis/metabolismo
Transdução de Sinais
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Nitric Oxide Donors); 0 (Plant Proteins); 0 (Recombinant Proteins); 0 (S-Nitrosothiols); 31C4KY9ESH (Nitric Oxide); 57564-91-7 (S-Nitrosoglutathione); BBX060AN9V (Hydrogen Peroxide); EC 1.2.- (Aldehyde Oxidoreductases); EC 1.2.1.46 (formaldehyde dehydrogenase, glutathione-independent); K848JZ4886 (Cysteine)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171025
[St] Status:MEDLINE


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[PMID]:28893506
[Au] Autor:Cheng F; Fransson LÅ; Mani K
[Ad] Endereço:Department of Experimental Medical Science, Division of Neuroscience, Glycobiology Group, Lund University, Biomedical Center A13, SE-221 84, Lund, Sweden.
[Ti] Título:Cytochrome b561, copper, ß-cleaved amyloid precursor protein and niemann-pick C1 protein are involved in ascorbate-induced release and membrane penetration of heparan sulfate from endosomal S-nitrosylated glypican-1.
[So] Source:Exp Cell Res;360(2):171-179, 2017 Nov 15.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Ascorbate-induced release of heparan sulfate from S-nitrosylated heparan sulfate proteoglycan glypican-1 takes place in endosomes. Heparan sulfate penetrates the membrane and is transported to the nucleus. This process is dependent on copper and on expression and processing of the amyloid precursor protein. It remains unclear how exogenously supplied ascorbate can generate HS-anMan in endosomes and how passage through the membrane is facilitated. Here we have examined wild-type, Alzheimer Tg2576 and amyloid precursor protein (-/-) mouse fibroblasts and human fetal and Niemann-Pick C1 fibroblasts by using deconvolution immunofluorescence microscopy, siRNA technology and [S ]sulfate-labeling, vesicle isolation and gel chromatography. We found that ascorbate-induced release of heparan sulfate was dependent on expression of endosomal cytochrome b561. Formation and nuclear transport of heparan sulfate was suppressed by inhibition of ß-processing of the amyloid precursor protein and formation was restored by copper (I) ions. Membrane penetration was not dependent on amyloid beta channel formation. Inhibition of endosomal exit resulted in accumulation of heparan sulfate in vesicles that exposed the C-terminal of the amyloid precursor protein externally. Endosome-to-nucleus transport was also dependent on expression of the Niemann-Pick C1 protein. We propose that ascorbate is taken up from the medium and is oxidized by cytochrome b561 which, in turn, reduces copper (II) to copper (I) present in the N-terminal, ß-cleaved domain of the amyloid precursor protein. Re-oxidation of copper (I) is coupled to reductive, deaminative release of heparan sulfate from glypican-1. Passage through the membrane may be facilitated by the C-terminal, ß-cleaved fragment of the amyloid precursor protein and the Niemann-Pick C1 protein.
[Mh] Termos MeSH primário: Precursor de Proteína beta-Amiloide/fisiologia
Ácido Ascórbico/farmacologia
Proteínas de Transporte/fisiologia
Cobre/fisiologia
Grupo dos Citocromos b/fisiologia
Endossomos/metabolismo
Glipicanas/metabolismo
Glicoproteínas de Membrana/fisiologia
[Mh] Termos MeSH secundário: Precursor de Proteína beta-Amiloide/metabolismo
Animais
Células Cultivadas
Endossomos/efeitos dos fármacos
Heparitina Sulfato
Seres Humanos
Membranas/efeitos dos fármacos
Membranas/metabolismo
Camundongos
Camundongos Transgênicos
Nitrosação
Processamento de Proteína Pós-Traducional
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Amyloid beta-Protein Precursor); 0 (Carrier Proteins); 0 (Cytochrome b Group); 0 (Glypicans); 0 (Membrane Glycoproteins); 0 (NPC1 protein, human); 11130-51-1 (cytochrome b561); 789U1901C5 (Copper); 9050-30-0 (Heparitin Sulfate); PQ6CK8PD0R (Ascorbic Acid)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171103
[Lr] Data última revisão:
171103
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170913
[St] Status:MEDLINE


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[PMID]:28883020
[Au] Autor:Zhang Y; Wu K; Su W; Zhang DF; Wang P; Qiao X; Yao Q; Yuan Z; Yao YG; Liu G; Zhang C; Liu L; Chen C
[Ad] Endereço:National Laboratory of Biomacromolecules, Chinese Academy of Sciences Center for Excellence in Biomacromolecules, Institute of Biophysics, Beijing 100101, China.
[Ti] Título:Increased GSNOR Expression during Aging Impairs Cognitive Function and Decreases S-Nitrosation of CaMKIIα.
[So] Source:J Neurosci;37(40):9741-9758, 2017 Oct 04.
[Is] ISSN:1529-2401
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:As the population ages, an increasing number of people suffer from age-related cognitive impairment. However, the mechanisms underlying this process remain unclear. Here, we found that S-nitrosoglutathione reductase (GSNOR), the key enzyme that metabolizes intracellular nitric oxide (NO) and regulates S-nitrosation, was significantly increased in the hippocampus of both aging humans and mice. Transgenic mice overexpressing GSNOR exclusively in neurons showed cognitive impairment in behavioral tests, including the Morris water maze, fear conditioning, and the Y-maze test. We also found that transgenic mice have LTP defects and lower dendrite spine density, whereas knock-out mice rescued the age-related cognitive impairment. Analysis of S-nitrosation showed significantly decreased hippocampal CaMKIIα S-nitrosation in naturally aged mice and transgenic mice. Consistent with the change in CaMKIIα S-nitrosation, the accumulation of CaMKIIα in the hippocampal synaptosomal fraction, as well as its downstream signaling targets p(S831)-GLUR1, was also significantly decreased. All these effects could be rescued in the knock-out mice. We further verified that the S-nitrosation of CaMKIIα was responsible for the CaMKIIα synaptosomal accumulation by mutating CaMKIIα S-nitrosated sites (C280/C289). Upregulation of the NO signaling pathway rescued the cognitive impairment in transgenic mice. In summary, our research demonstrates that GSNOR impairs cognitive function in aging and it could serve as a new potential target for the treatment of age-related cognitive impairment. In contrast to the free radical theory of aging, NO signaling deficiency may be the main mediator of age-related cognitive impairment. This study indicated that S-nitrosoglutathione reductase (GSNOR), a key protein S-nitrosation metabolic enzyme, is a new potential target in age-related cognitive impairment; and in contrast to the free radical theory of aging, NO signaling deficiency may be the main cause of this process. In addition, increased GSNOR expression during aging decreases S-nitrosation of CaMKIIα and reduces CaMKIIα synaptosomal accumulation. To our knowledge, it is for the first time to show the cellular function regulation of CaMKIIα by GSNOR-dependent S-nitrosation as a new post-translational modification after its phosphorylation was explored. These findings elucidate a novel mechanism of age-related cognitive impairment and may provide a new potential target and strategy for slowing down this process.
[Mh] Termos MeSH primário: Envelhecimento/metabolismo
Álcool Desidrogenase/biossíntese
Proteína Quinase Tipo 2 Dependente de Cálcio-Calmodulina/metabolismo
Transtornos Cognitivos/metabolismo
Cognição/fisiologia
Regulação Enzimológica da Expressão Gênica
[Mh] Termos MeSH secundário: Envelhecimento/genética
Álcool Desidrogenase/genética
Animais
Proteína Quinase Tipo 2 Dependente de Cálcio-Calmodulina/genética
Transtornos Cognitivos/genética
Potenciais Pós-Sinápticos Excitadores/fisiologia
Feminino
Células HEK293
Hipocampo/metabolismo
Seres Humanos
Masculino
Camundongos
Camundongos Knockout
Nitrosação/fisiologia
Técnicas de Cultura de Órgãos
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
EC 1.1.1.1 (Adh5 protein, mouse); EC 1.1.1.1 (Alcohol Dehydrogenase); EC 2.7.11.17 (Calcium-Calmodulin-Dependent Protein Kinase Type 2)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171012
[Lr] Data última revisão:
171012
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170909
[St] Status:MEDLINE
[do] DOI:10.1523/JNEUROSCI.0681-17.2017


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[PMID]:28822219
[Au] Autor:Belcastro E; Gaucher C; Corti A; Leroy P; Lartaud I; Pompella A
[Ad] Endereço:.
[Ti] Título:Regulation of protein function by S-nitrosation and S-glutathionylation: processes and targets in cardiovascular pathophysiology.
[So] Source:Biol Chem;398(12):1267-1293, 2017 Nov 27.
[Is] ISSN:1437-4315
[Cp] País de publicação:Germany
[La] Idioma:eng
[Ab] Resumo:Decades of chemical, biochemical and pathophysiological research have established the relevance of post-translational protein modifications induced by processes related to oxidative stress, with critical reflections on cellular signal transduction pathways. A great deal of the so-called 'redox regulation' of cell function is in fact mediated through reactions promoted by reactive oxygen and nitrogen species on more or less specific aminoacid residues in proteins, at various levels within the cell machinery. Modifications involving cysteine residues have received most attention, due to the critical roles they play in determining the structure/function correlates in proteins. The peculiar reactivity of these residues results in two major classes of modifications, with incorporation of NO moieties (S-nitrosation, leading to formation of protein S-nitrosothiols) or binding of low molecular weight thiols (S-thionylation, i.e. in particular S-glutathionylation, S-cysteinylglycinylation and S-cysteinylation). A wide array of proteins have been thus analyzed in detail as far as their susceptibility to either modification or both, and the resulting functional changes have been described in a number of experimental settings. The present review aims to provide an update of available knowledge in the field, with a special focus on the respective (sometimes competing and antagonistic) roles played by protein S-nitrosations and S-thionylations in biochemical and cellular processes specifically pertaining to pathogenesis of cardiovascular diseases.
[Mh] Termos MeSH primário: Doenças Cardiovasculares/metabolismo
Doenças Cardiovasculares/fisiopatologia
Glutationa/metabolismo
Óxido Nítrico/metabolismo
Nitrosação
[Mh] Termos MeSH secundário: Animais
Seres Humanos
[Pt] Tipo de publicação:JOURNAL ARTICLE; REVIEW
[Nm] Nome de substância:
31C4KY9ESH (Nitric Oxide); GAN16C9B8O (Glutathione)
[Em] Mês de entrada:1711
[Cu] Atualização por classe:171113
[Lr] Data última revisão:
171113
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170820
[St] Status:MEDLINE


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[PMID]:28780307
[Au] Autor:Wang K; Zhu X; Zhang K; Zhou F; Zhu L
[Ad] Endereço:Key Laboratory of Nuclear Medicine, Ministry of Health, Jiangsu Key Laboratory of Molecular Nuclear Medicine, Jiangsu Institute of Nuclear Medicine, Wuxi 214063, Jiangsu Province, China. Electronic address: wangke@jsinm.org.
[Ti] Título:Neuroprotective effect of tetramethylpyrazine against all-trans-retinal toxicity in the differentiated Y-79 cells via upregulation of IRBP expression.
[So] Source:Exp Cell Res;359(1):120-128, 2017 Oct 01.
[Is] ISSN:1090-2422
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:It is estimated that abnormal accumulation of all-trans-retinal (atRAL) is a leading cause of photoreceptor degeneration in retinal degenerative diseases. Deficiency of interphotoreceptor retinoid-binding protein (IRBP), a retinoid transporter in the visual cycle, is responsible for the impaired clearance of atRAL and results in atRAL toxicity in retina. Therefore, IRBP has been proposed to be a potent target in preventing atRAL-induced photoreceptor degeneration. In this study, the neuroprotective effect of tetramethylpyrazine (TMP) against atRAL toxicity in the differentiated Y-79 cells, a in vitro model of photoreceptor, was first investigated. Our findings showed that atRAL could induce cytotoxicity, oxidative/nitrosative stresses, apoptosis and leukostasis in the differentiated Y-79 cells; however, the pre-treatment of TMP significantly attenuated such effects in a dose-dependent manner. Furthermore, our results indicated that TMP exerted its neuroprotective effect mainly through upregulating IRBP expression. The present study significantly contributes to better understanding the important role of IRBP in retinal degenerative diseases and forms the basis of the therapeutic development of TMP in such diseases in the future.
[Mh] Termos MeSH primário: Diferenciação Celular/efeitos dos fármacos
Proteínas do Olho/metabolismo
Fármacos Neuroprotetores/farmacologia
Pirazinas/farmacologia
Retinaldeído/toxicidade
Proteínas de Ligação ao Retinol/metabolismo
Regulação para Cima/efeitos dos fármacos
[Mh] Termos MeSH secundário: Apoptose/efeitos dos fármacos
Morte Celular/efeitos dos fármacos
Linhagem Celular Tumoral
Seres Humanos
Molécula 1 de Adesão Intercelular/metabolismo
Leucostasia/patologia
Mitocôndrias/efeitos dos fármacos
Mitocôndrias/metabolismo
Neurônios/efeitos dos fármacos
Neurônios/metabolismo
Neurônios/patologia
Neuroproteção/efeitos dos fármacos
Nitrosação
Estresse Oxidativo/efeitos dos fármacos
Molécula 1 de Adesão de Célula Vascular/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Eye Proteins); 0 (Neuroprotective Agents); 0 (Pyrazines); 0 (Retinol-Binding Proteins); 0 (Vascular Cell Adhesion Molecule-1); 0 (interstitial retinol-binding protein); 126547-89-5 (Intercellular Adhesion Molecule-1); RR725D715M (Retinaldehyde); V80F4IA5XG (tetramethylpyrazine)
[Em] Mês de entrada:1710
[Cu] Atualização por classe:171016
[Lr] Data última revisão:
171016
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170807
[St] Status:MEDLINE


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[PMID]:28710281
[Au] Autor:Chouchani ET; James AM; Methner C; Pell VR; Prime TA; Erickson BK; Forkink M; Lau GY; Bright TP; Menger KE; Fearnley IM; Krieg T; Murphy MP
[Ad] Endereço:From the Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, Massachusetts 02284-9168, EdwardT_Chouchani@dfci.harvard.edu.
[Ti] Título:Identification and quantification of protein -nitrosation by nitrite in the mouse heart during ischemia.
[So] Source:J Biol Chem;292(35):14486-14495, 2017 Sep 01.
[Is] ISSN:1083-351X
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Nitrate (NO ) and nitrite (NO ) are known to be cardioprotective and to alter energy metabolism NO action results from its conversion to NO by salivary bacteria, but the mechanism(s) by which NO affects metabolism remains obscure. NO may act by -nitrosating protein thiols, thereby altering protein activity. But how this occurs, and the functional importance of -nitrosation sites across the mammalian proteome, remain largely uncharacterized. Here we analyzed protein thiols within mouse hearts using quantitative proteomics to determine -nitrosation site occupancy. We extended the thiol-redox proteomic technique, isotope-coded affinity tag labeling, to quantify the extent of NO -dependent -nitrosation of proteins thiols Using this approach, called SNOxICAT ( -nitrosothiol redox isotope-coded affinity tag), we found that exposure to NO under normoxic conditions or exposure to ischemia alone results in minimal -nitrosation of protein thiols. However, exposure to NO in conjunction with ischemia led to extensive -nitrosation of protein thiols across all cellular compartments. Several mitochondrial protein thiols exposed to the mitochondrial matrix were selectively -nitrosated under these conditions, potentially contributing to the beneficial effects of NO on mitochondrial metabolism. The permeability of the mitochondrial inner membrane to HNO , but not to NO , combined with the lack of -nitrosation during anoxia alone or by NO during normoxia places constraints on how -nitrosation occurs and on its mechanisms of cardioprotection and modulation of energy metabolism. Quantifying -nitrosated protein thiols now allows determination of modified cysteines across the proteome and identification of those most likely responsible for the functional consequences of NO exposure.
[Mh] Termos MeSH primário: Modelos Animais de Doenças
Mitocôndrias Cardíacas/metabolismo
Isquemia Miocárdica/metabolismo
Miocárdio/metabolismo
Nitritos/metabolismo
Processamento de Proteína Pós-Traducional
Regulação para Cima
[Mh] Termos MeSH secundário: Marcadores de Afinidade/metabolismo
Animais
Cardiotônicos/farmacologia
Permeabilidade da Membrana Celular/efeitos dos fármacos
Cisteína/metabolismo
Feminino
Coração/efeitos dos fármacos
Camundongos
Camundongos Endogâmicos C57BL
Mitocôndrias Cardíacas/efeitos dos fármacos
Mitocôndrias Hepáticas/efeitos dos fármacos
Mitocôndrias Hepáticas/metabolismo
Dilatação Mitocondrial/efeitos dos fármacos
Isquemia Miocárdica/tratamento farmacológico
Nitratos/farmacologia
Nitritos/farmacologia
Nitrosação/efeitos dos fármacos
Compostos de Potássio/farmacologia
Proteômica/métodos
Ratos Wistar
Regulação para Cima/efeitos dos fármacos
[Pt] Tipo de publicação:COMPARATIVE STUDY; JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Affinity Labels); 0 (Cardiotonic Agents); 0 (Nitrates); 0 (Nitrites); 0 (Potassium Compounds); 794654G42L (potassium nitrite); K848JZ4886 (Cysteine); RU45X2JN0Z (potassium nitrate)
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170926
[Lr] Data última revisão:
170926
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170716
[St] Status:MEDLINE
[do] DOI:10.1074/jbc.M117.798744


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[PMID]:28528978
[Au] Autor:Kar P; Biswas P; Ghosh S
[Ad] Endereço:Department of Biochemistry, University of Calcutta, 35, Ballygunge Circular Road, Kolkata 700019, West Bengal, India.
[Ti] Título:Multimodal control of transcription factor Pap1 in Schizosaccharomyces pombe under nitrosative stress.
[So] Source:Biochem Biophys Res Commun;489(1):42-47, 2017 Jul 15.
[Is] ISSN:1090-2104
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Schizosaccharomyces pombe Pap1, a bZIP transcription factor, is highly homologous to the mammalian c-Jun protein that belongs to the AP1 family of transcriptional regulators. The role of transcription factor Pap1 has been extensively studied under oxidative stress. Two cysteine residues in Pap1p namely, C278 and C501 form disulfide linkage under oxidative stress resulting in nuclear accumulation. We first time showed the involvement of Pap1 in the protection against nitrosative stress. In the present study we show that pap1 deletion makes growth of S. pombe sensitive to nitrosative stress. pap1 deletion also causes delayed recovery in terms of mitotic index under nitrosative stress. Our flow cytometry data shows that pap1 deletion causes slower recovery from the slowdown of DNA replication under nitrosative stress. This is the first report where we show that Pap1 transcription factor is localized in the nucleus under nitrosative stress. From our study it is evident that nuclear localization of Pap1 under nitrosative stress was not due to reactive oxygen species formation.
[Mh] Termos MeSH primário: Fatores de Transcrição de Zíper de Leucina Básica/metabolismo
Estresse Oxidativo
Proteínas de Schizosaccharomyces pombe/metabolismo
Schizosaccharomyces/metabolismo
[Mh] Termos MeSH secundário: Sobrevivência Celular
Microscopia de Fluorescência
Nitrosação
Proteínas Associadas a Pancreatite
Espécies Reativas de Oxigênio/metabolismo
Schizosaccharomyces/citologia
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Basic-Leucine Zipper Transcription Factors); 0 (Pancreatitis-Associated Proteins); 0 (Pap1 protein, S pombe); 0 (REG3A protein, human); 0 (Reactive Oxygen Species); 0 (Schizosaccharomyces pombe Proteins)
[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:170523
[St] Status:MEDLINE


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[PMID]:28472095
[Au] Autor:Wang X; Shults NV; Suzuki YJ
[Ad] Endereço:Department of Pharmacology and Physiology, Georgetown University Medical Center, Washington, DC, United States of America.
[Ti] Título:Oxidative profiling of the failing right heart in rats with pulmonary hypertension.
[So] Source:PLoS One;12(5):e0176887, 2017.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Right heart failure is the major cause of death among patients with pulmonary arterial hypertension (PAH). Understanding the biology of the right ventricle (RV) should help developing new therapeutic strategies. Rats subjected to the injection of Sugen5416 (an inhibitors of vascular endothelial growth factor receptor) plus the ovalbumin immunization had increased pulmonary arterial pressure and severe vascular remodeling. RVs of these rats were hypertrophied and had severe cardiac fibrosis. No apoptosis was, however, detected. Metabolomics analysis revealed that oxidized glutathione, xanthine and uric acid had increased in PAH RVs, suggesting the production of reactive oxygen species by xanthine oxidase. PAH RVs were also found to have a 30-fold lower level of α-tocopherol nicotinate, consistent with oxidative stress decreasing antioxidants and also demonstrating for the first time that the nicotinate ester of vitamin E is endogenously expressed. Oxidative/nitrosative protein modifications including S-glutathionylation, S-nitrosylation and nitrotyrosine formation, but not protein carbonylation, were found to be increased in RVs of rats with PAH. Mass spectrometry identified that S-nitrosylated proteins include heat shock protein 90 and sarcoplasmic reticulum Ca2+-ATPase. These results demonstrate that RV failure is associated with the promotion of specific oxidative and nitrosative stress.
[Mh] Termos MeSH primário: Ventrículos do Coração/patologia
Hipertensão Pulmonar/metabolismo
[Mh] Termos MeSH secundário: Animais
Hipertensão Pulmonar/patologia
Masculino
Espectrometria de Massas
Metabolômica
Nitrosação
Oxirredução
Ratos
Ratos Sprague-Dawley
Remodelação Vascular
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Em] Mês de entrada:1709
[Cu] Atualização por classe:170915
[Lr] Data última revisão:
170915
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170505
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0176887



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