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  1 / 22721 MEDLINE  
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[PMID]:29329317
[Au] Autor:Jeong BY; Lee HY; Park CG; Kang J; Yu SL; Choi DR; Han SY; Park MH; Cho S; Lee SY; Hwang WM; Yun SR; Ryu HM; Oh EJ; Park SH; Kim YL; Yoon SH
[Ad] Endereço:Department of Pharmacology, College of Medicine, Konyang University, Daejeon, Republic of Korea.
[Ti] Título:Oxidative stress caused by activation of NADPH oxidase 4 promotes contrast-induced acute kidney injury.
[So] Source:PLoS One;13(1):e0191034, 2018.
[Is] ISSN:1932-6203
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Contrast-induced acute kidney injury (CIAKI) is a leading cause of acute kidney injury following radiographic procedures. Intrarenal oxidative stress plays a critical role in CIAKI. Nicotinamide adenine dinucleotide 3-phosphate (NADPH) oxidases (Noxs) are important sources of reactive oxygen species (ROS). Among the various types of Noxs, Nox4 is expressed predominantly in the kidney in rodents. Here, we evaluated the role of Nox4 and benefit of Nox4 inhibition on CIAKI using in vivo and in vitro models. HK-2 cells were treated with iohexol, with or without Nox4 knockdown, or the most specific Nox1/4 inhibitor (GKT137831). Effects of Nox4 inhibition on CIAKI mice were examined. Expression of Nox4 in HK-2 cells was significantly increased following iohexol exposure. Silencing of Nox4 rescued the production of ROS, downregulated pro-inflammatory markers (particularly phospho-p38) implicated in CIAKI, and reduced Bax and caspase 3/7 activity, which resulted in increased cellular survival in iohexol-treated HK-2 cells. Pretreatment with GKT137831 replicated these effects by decreasing levels of phospho-p38. In a CIAKI mouse model, even though the improvement of plasma blood urea nitrogen was unclear, pretreatment with GKT137831 resulted in preserved structure, reduced expression of 8-hydroxy-2'-deoxyguanosine (8OHdG) and kidney injury molecule-1 (KIM-1), and reduced number of TUNEL (terminal deoxynucleotidyl transferase dUTP nick end labeling)-positive cells. These results suggest Nox4 as a key source of reactive oxygen species responsible for CIAKI and provide a novel potential option for prevention of CIAKI.
[Mh] Termos MeSH primário: Lesão Renal Aguda/metabolismo
Meios de Contraste/efeitos adversos
NADPH Oxidase 4/metabolismo
Estresse Oxidativo
[Mh] Termos MeSH secundário: Lesão Renal Aguda/induzido quimicamente
Animais
Apoptose/efeitos dos fármacos
Linhagem Celular
Ativação Enzimática
Inativação Gênica
Seres Humanos
Iohexol/farmacologia
Túbulos Renais Proximais/citologia
Túbulos Renais Proximais/efeitos dos fármacos
Túbulos Renais Proximais/metabolismo
Masculino
Camundongos
Camundongos Endogâmicos C57BL
NADPH Oxidase 4/genética
Espécies Reativas de Oxigênio/metabolismo
Reação em Cadeia da Polimerase em Tempo Real
Superóxidos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Contrast Media); 0 (Reactive Oxygen Species); 11062-77-4 (Superoxides); 4419T9MX03 (Iohexol); EC 1.6.3.- (NADPH Oxidase 4)
[Em] Mês de entrada:1803
[Cu] Atualização por classe:180309
[Lr] Data última revisão:
180309
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:180113
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pone.0191034


  2 / 22721 MEDLINE  
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[PMID]:29208521
[Au] Autor:Bae D; Gautam J; Jang H; Banskota S; Lee SY; Jeong MJ; Kim AS; Kim HC; Lee IH; Nam TG; Kim JA; Jeong BS
[Ad] Endereço:College of Pharmacy and Institute for Drug Research, Yeungnam University, Gyeongsan 38541, Republic of Korea.
[Ti] Título:Protective effects of 6-ureido/thioureido-2,4,5-trimethylpyridin-3-ols against 4-hydroxynonenal-induced cell death in adult retinal pigment epithelial-19 cells.
[So] Source:Bioorg Med Chem Lett;28(2):107-112, 2018 01 15.
[Is] ISSN:1464-3405
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Dysfunction or progressive degeneration of retinal pigment epithelium (RPE) contributes in the initial pathogenesis of age-related macular degeneration (AMD) causing irreversible vision loss, which makes RPE the prime target of the disease. The present study aimed to identify compounds to protect 4-hydroxynonenal (4-HNE)-induced RPE cell death by inhibiting NADPH oxidase 4 (NOX4) activity, not just as free radical scavengers, using ARPE-19, a human adult retinal pigment epithelial cell line, as a RPE representative. Novel thirty-two 6-ureido/thioureido-2,4,5-trimethylpyridin-3-ol derivatives 17 were synthesized and tested. We found that there was a strong correlation between level of protective effect of compounds 17 against 4-HNE-induced APRE-19 cell death and that of inhibitory activity against 4-HNE-induced superoxide production, and that most of the compounds 17 showed minimal DPPH radical scavenging activity. Compound 17-28 showed the best protective activity against 4-HNE-induced superoxide production (79.5% inhibition) and cell death (85.1% recovery) at 10 µM concentration, which was better than that of VAS2870, a NOX2/4 inhibitor. In addition, compound 17-28 blocked 4-HNE-induced apoptosis of ARPE-19 cells in a concentration-dependent manner. The results indicate that compound 17-28 may be a lead compound to develop AMD therapeutics.
[Mh] Termos MeSH primário: Aldeídos/antagonistas & inibidores
Inibidores Enzimáticos/farmacologia
Piridinas/farmacologia
[Mh] Termos MeSH secundário: Adulto
Aldeídos/farmacologia
Morte Celular/efeitos dos fármacos
Linhagem Celular
Sobrevivência Celular/efeitos dos fármacos
Relação Dose-Resposta a Droga
Inibidores Enzimáticos/síntese química
Inibidores Enzimáticos/química
Seres Humanos
Estrutura Molecular
NADPH Oxidase 4/antagonistas & inibidores
NADPH Oxidase 4/metabolismo
Piridinas/síntese química
Piridinas/química
Relação Estrutura-Atividade
Superóxidos/antagonistas & inibidores
Superóxidos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Aldehydes); 0 (Enzyme Inhibitors); 0 (Pyridines); 11062-77-4 (Superoxides); EC 1.6.3.- (NADPH Oxidase 4); EC 1.6.3.- (NOX4 protein, human); K1CVM13F96 (4-hydroxy-2-nonenal)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171207
[St] Status:MEDLINE


  3 / 22721 MEDLINE  
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[PMID]:28455970
[Au] Autor:Wong RCB; Lim SY; Hung SSC; Jackson S; Khan S; Van Bergen NJ; De Smit E; Liang HH; Kearns LS; Clarke L; Mackey DA; Hewitt AW; Trounce IA; Pébay A
[Ad] Endereço:Centre for Eye Research Australia, Royal Victorian Eye and Ear Hospital, East Melbourne, Australia.
[Ti] Título:Mitochondrial replacement in an iPSC model of Leber's hereditary optic neuropathy.
[So] Source:Aging (Albany NY);9(4):1341-1350, 2017 Apr.
[Is] ISSN:1945-4589
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:Cybrid technology was used to replace Leber hereditary optic neuropathy (LHON) causing mitochondrial DNA (mtDNA) mutations from patient-specific fibroblasts with wildtype mtDNA, and mutation-free induced pluripotent stem cells (iPSCs) were generated subsequently. Retinal ganglion cell (RGC) differentiation demonstrates increased cell death in LHON-RGCs and can be rescued in cybrid corrected RGCs.
[Mh] Termos MeSH primário: DNA Mitocondrial/genética
Terapia Genética/métodos
Células-Tronco Pluripotentes Induzidas
Mitocôndrias/genética
Atrofia Óptica Hereditária de Leber/terapia
Transplante de Células-Tronco/métodos
[Mh] Termos MeSH secundário: Apoptose
Morte Celular
Diferenciação Celular
DNA Mitocondrial/metabolismo
DNA Mitocondrial/uso terapêutico
Seres Humanos
Repetições de Microssatélites
Células Ganglionares da Retina/patologia
Superóxidos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (DNA, Mitochondrial); 11062-77-4 (Superoxides)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180216
[Lr] Data última revisão:
180216
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170430
[St] Status:MEDLINE
[do] DOI:10.18632/aging.101231


  4 / 22721 MEDLINE  
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[PMID]:29242061
[Au] Autor:Kaito Y; Kataoka R; Mihara T; Takechi K; Takahira A; Watanabe S; Han F; Tamura M
[Ad] Endereço:Department of Applied Chemistry, Graduate School of Science and Engineering, Ehime University, 3 Bunkyo-cho, Matsuyama, Ehime 790-8577, Japan.
[Ti] Título:Phosphorylation of Ser-525 in ßPix impairs Nox1-activating ability in Caco-2 cells.
[So] Source:Arch Biochem Biophys;638:58-65, 2018 01 15.
[Is] ISSN:1096-0384
[Cp] País de publicação:United States
[La] Idioma:eng
[Ab] Resumo:ßPix activates Nox1, an O -generating NADPH oxidase, through Rac activation. In this study, we found that S525E mutation of ßPix eliminated its Nox1-activating ability in transfected Caco-2 cells. Unexpectedly, affinity for Rac was not diminished but rather enhanced by S525E mutation, and guanine nucleotide exchange factor (GEF) activity was not altered. The N-terminal fragment (amino acids 1-400) showed similar Rac-binding and GEF activity to wild-type ßPix. In contrast, the C-terminal fragment (amino acids 408-646) had higher Rac-binding activity, particularly for Rac-GTP, than wild-type ßPix, and showed no GEF activity. These data suggest that a second Rac-binding site within the C-terminal region is opened by phosphorylation of Ser-525. The site may bind not only Rac-GDP but also Rac-GTP released from the N-terminal catalytic region, which interrupts Rac-GTP translocation to the membrane where Nox1 resides. If one considers that S340E mutation enhances Nox1 activation (Kaito et al., 2014), the present study suggests that ßPix can also play an inhibitory role in O production, depending on the sites of phosphorylation.
[Mh] Termos MeSH primário: Mutação de Sentido Incorreto
NADPH Oxidase 1/metabolismo
Fatores de Troca de Nucleotídeo Guanina Rho/metabolismo
Superóxidos/metabolismo
[Mh] Termos MeSH secundário: Substituição de Aminoácidos
Células CACO-2
Ativação Enzimática/genética
Seres Humanos
NADPH Oxidase 1/genética
Fosforilação/genética
Domínios Proteicos
Fatores de Troca de Nucleotídeo Guanina Rho/genética
Proteínas rac de Ligação ao GTP/genética
Proteínas rac de Ligação ao GTP/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Rho Guanine Nucleotide Exchange Factors); 11062-77-4 (Superoxides); EC 1.6.3.- (NADPH Oxidase 1); EC 1.6.3.- (NOX1 protein, human); EC 3.6.5.2 (rac GTP-Binding Proteins)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180214
[Lr] Data última revisão:
180214
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:171216
[St] Status:MEDLINE


  5 / 22721 MEDLINE  
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[PMID]:28599858
[Au] Autor:Shalan H; Kato M; Cheruzel L
[Ad] Endereço:San José State University, Department of Chemistry, One Washington Square, San José, CA, United States.
[Ti] Título:Keeping the spotlight on cytochrome P450.
[So] Source:Biochim Biophys Acta;1866(1):80-87, 2018 01.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:This review describes the recent advances utilizing photosensitizers and visible light to harness the synthetic potential of P450 enzymes. The structures of the photosensitizers investigated to date are first presented along with their photophysical and redox properties. Functional photosensitizers range from organic and inorganic complexes to nanomaterials as well as the biological photosystem I complex. The focus is then on the three distinct approaches that have emerged for the activation of P450 enzymes. The first approach utilizes the in situ generation of reactive oxygen species entering the P450 mechanism via the peroxide shunt pathway. The other two approaches are sustained by electron injections into catalytically competent heme domains either facilitated by redox partners or through direct heme domain reduction. Achievements as well as pitfalls of each approach are briefly summarized. This article is part of a Special Issue entitled: Cytochrome P450 biodiversity and biotechnology, edited by Erika Plettner, Gianfranco Gilardi, Luet Wong, Vlada Urlacher, Jared Goldstone.
[Mh] Termos MeSH primário: Sistema Enzimático do Citocromo P-450/química
Elétrons
Escherichia coli/enzimologia
Heme/química
Complexos de Proteínas Captadores de Luz/química
Fármacos Fotossensibilizantes/química
[Mh] Termos MeSH secundário: Biocatálise
Compostos de Cádmio/química
Sistema Enzimático do Citocromo P-450/metabolismo
Amarelo de Eosina-(YS)/química
Amarelo de Eosina-(YS)/metabolismo
Escherichia coli/química
Escherichia coli/efeitos da radiação
Heme/metabolismo
Luz
Complexos de Proteínas Captadores de Luz/metabolismo
Modelos Moleculares
Oxirredução
Peróxidos/química
Peróxidos/metabolismo
Fármacos Fotossensibilizantes/metabolismo
Estrutura Secundária de Proteína
Pontos Quânticos
Sulfetos/química
Superóxidos/química
Superóxidos/metabolismo
Tioglicolatos/química
Tioglicolatos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., EXTRAMURAL; RESEARCH SUPPORT, U.S. GOV'T, NON-P.H.S.; REVIEW
[Nm] Nome de substância:
0 (Cadmium Compounds); 0 (Light-Harvesting Protein Complexes); 0 (Peroxides); 0 (Photosensitizing Agents); 0 (Sulfides); 0 (Thioglycolates); 057EZR4Z7Q (cadmium sulfide); 11062-77-4 (Superoxides); 42VZT0U6YR (Heme); 7857H94KHM (2-mercaptoacetate); 9035-51-2 (Cytochrome P-450 Enzyme System); TDQ283MPCW (Eosine Yellowish-(YS))
[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:170611
[St] Status:MEDLINE


  6 / 22721 MEDLINE  
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[PMID]:27775125
[Au] Autor:Cásedas G; Les F; Gómez-Serranillos MP; Smith C; López V
[Ad] Endereço:Department of Pharmacy, Faculty of Health Sciences, Universidad San Jorge, 50.830 Villanueva de Gállego, Zaragoza, Spain. ilopez@usj.es.
[Ti] Título:Bioactive and functional properties of sour cherry juice (Prunus cerasus).
[So] Source:Food Funct;7(11):4675-4682, 2016 Nov 09.
[Is] ISSN:2042-650X
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:Sour cherry juice (Prunus cerasus) is consumed as a nutritional supplement claiming health effects. The aim of the study was to evaluate the different properties of sour cherry juice in terms of antioxidant activity and inhibition of target enzymes in the central nervous system and diabetes. The content of polyphenols and anthocyanins was quantified. Different experiments were carried out to determine the radical scavenging properties of the juice. The activity of sour cherry juice was also tested in physiological relevant enzymes of the central nervous system (acetylcholinesterase, monoamine oxidase A, tyrosinase) and others involved in type 2 diabetes (α-glucosidase, dipeptidyl peptidase-4). Sour cherry juice showed significant antioxidant effects but the activity of the lyophilized juice was not superior to compounds such as ascorbic, gallic or chlorogenic acid. Furthermore, sour cherry juice and one of its main polyphenols known as chlorogenic acid were also able to inhibit monoamine oxidase A and tyrosinase as well as enzymes involved in diabetes. This is the first time that sour cherry juice is reported to inhibit monoamine oxidase A, α-glucosidase and dipeptidyl peptidase-4 in a dose dependent manner, which may be of interest for human health and the prevention of certain diseases.
[Mh] Termos MeSH primário: Artemia/efeitos dos fármacos
Sucos de Frutas e Vegetais/análise
Prunus avium/química
[Mh] Termos MeSH secundário: Animais
Antioxidantes
Bioensaio
Sobrevivência Celular
Alimento Funcional
Células HeLa
Seres Humanos
Compostos Fitoquímicos/química
Compostos Fitoquímicos/metabolismo
Superóxidos/química
alfa-Glucosidases/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Antioxidants); 0 (Phytochemicals); 11062-77-4 (Superoxides); EC 3.2.1.20 (alpha-Glucosidases)
[Em] Mês de entrada:1802
[Cu] Atualização por classe:180201
[Lr] Data última revisão:
180201
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:161025
[St] Status:MEDLINE


  7 / 22721 MEDLINE  
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[PMID]:29235764
[Au] Autor:Marchenko MM; Ketsa OV; Shmarakov IO; Abutnaritsa KH
[Ti] Título:Monooxygenase system in Guerin's carcinoma of rats under conditions of ω-3 polyunsaturated fatty acids administration.
[So] Source:Ukr Biochem J;88(4):48-56, 2016 Jul-Aug.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:The aim of the study was to determine the variations of function in components of monooxygenase system (MOS) of rat Guerin's carcinoma under ω-3 polyunsaturated fatty acids (PUFAs) administration. The activity of Guerin's carcinoma microsomal NADH-cytochrome b5 reductase, the content and the rate of cytochrome b5 oxidation-reduction, the content and the rate of cytochrome Р450 oxidation-reduction have been investigated in rats with tumor under conditions of ω-3 PUFAs administration. ω-3 PUFAs supplementation before and after transplantation of Guerin's carcinoma resulted in the increase of NADH-cytochrome b5 reductase activity and decrease of cytochrome b5 level in the Guerin's carcinoma microsomal fraction in the logarithmic phases of carcinogenesis as compared to the tumor-bearing rats. Increased activity of NADH-cytochrome b5 reductase facilitates higher electron flow in redox-chain of MOS. Under decreased cytochrome b5 levels the electrons are transferred to oxygen, which leads to heightened generation of superoxide (O2•-) in comparison to control. It was shown, that the decrease of cytochrome P450 level in the Guerin's carcinoma microsomal fraction in the logarithmic phases of oncogenesis under ω-3 PUFAs administration may be associated with its transition into an inactive form ­ cytochrome P420. This decrease in cytochrome P450 coincides with increased generation of superoxide by MOS oxygenase chain.
[Mh] Termos MeSH primário: Carcinoma/tratamento farmacológico
Elétrons
Ácidos Graxos Ômega-3/farmacologia
Expressão Gênica/efeitos dos fármacos
Microssomos/efeitos dos fármacos
Substâncias Protetoras/farmacologia
[Mh] Termos MeSH secundário: Animais
Carcinoma/enzimologia
Carcinoma/patologia
Sistema Enzimático do Citocromo P-450/genética
Sistema Enzimático do Citocromo P-450/metabolismo
Citocromo-B(5) Redutase/genética
Citocromo-B(5) Redutase/metabolismo
Citocromos/genética
Citocromos/metabolismo
Citocromos b5/genética
Citocromos b5/metabolismo
Transporte de Elétrons/efeitos dos fármacos
Feminino
Membro Posterior
Injeções Subcutâneas
Microssomos/enzimologia
Transplante de Neoplasias
Oxirredução/efeitos dos fármacos
Estresse Oxidativo/efeitos dos fármacos
Ratos
Superóxidos/metabolismo
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Cytochromes); 0 (Fatty Acids, Omega-3); 0 (Protective Agents); 11062-77-4 (Superoxides); 9035-39-6 (Cytochromes b5); 9035-49-8 (cytochrome P420); 9035-51-2 (Cytochrome P-450 Enzyme System); EC 1.6.2.2 (Cytochrome-B(5) Reductase)
[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:171214
[St] Status:MEDLINE
[do] DOI:10.15407/ubj88.04.048


  8 / 22721 MEDLINE  
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[PMID]:29227606
[Au] Autor:Kopylchuk GP; Voloshchuk OM
[Ti] Título:Peculiarities of the free radical processes in rat liver mitochondria under toxic hepatitis on the background of alimentary protein deficiency.
[So] Source:Ukr Biochem J;88(2):66-72, 2016 Mar-Apr.
[Is] ISSN:2409-4943
[Cp] País de publicação:Ukraine
[La] Idioma:eng
[Ab] Resumo:The rate of superoxide anion radical, hydroxyl radical and hydrogen peroxide generation, the level of oxidative modification of mitochondrial proteins in the liver of rats with toxic hepatitis was investigated on the background of alimentary protein deficiency. We did not find significant increases of the intensity of free radical processes in liver mitochondria of rats maintained on the protein-deficient ration. The most significant intensification of free radical processes in liver mitochondria is observed under the conditions of toxic hepatitis, induced on the background of alimentary protein deprivation. Under these conditions the aggravation of all studied forms of reactive oxygen species generation was observed in liver mitochondria. The generation rates were increased as follows: O2 ­ by 1.7 times, Н2О2 ­ by 1.5 times, •ОН ­ practically double on the background of accumulation of oxidized mitochondria-derived proteins. The established changes in thiol groups' redox status of respiratory chain proteins insoluble in 0.05 M sodium-phosphate buffer (pH 11.5), and changes of their carbonyl derivatives content may be considered as one of the regulatory factors of mitochondrial energy-generating function.
[Mh] Termos MeSH primário: Doença Hepática Induzida por Substâncias e Drogas/metabolismo
Peróxido de Hidrogênio/metabolismo
Radical Hidroxila/metabolismo
Mitocôndrias Hepáticas/metabolismo
Deficiência de Proteína/metabolismo
Superóxidos/metabolismo
[Mh] Termos MeSH secundário: Acetaminofen/toxicidade
Animais
Animais não Endogâmicos
Doença Hepática Induzida por Substâncias e Drogas/complicações
Doença Hepática Induzida por Substâncias e Drogas/patologia
Dieta com Restrição de Proteínas/efeitos adversos
Peróxido de Hidrogênio/agonistas
Radical Hidroxila/agonistas
Fígado/efeitos dos fármacos
Fígado/metabolismo
Fígado/patologia
Mitocôndrias Hepáticas/efeitos dos fármacos
Oxirredução
Estresse Oxidativo
Carbonilação Proteica
Deficiência de Proteína/complicações
Deficiência de Proteína/etiologia
Deficiência de Proteína/patologia
Ratos
Superóxidos/agonistas
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
11062-77-4 (Superoxides); 3352-57-6 (Hydroxyl Radical); 362O9ITL9D (Acetaminophen); BBX060AN9V (Hydrogen Peroxide)
[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/ubj88.02.066


  9 / 22721 MEDLINE  
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[PMID]:28745761
[Au] Autor:Wang Y; Deng W; Wang F; Su Y; Feng Y; Chen P; Ma J; Su H; Yao K; Liu Y; Lv W; Liu G
[Ad] Endereço:School of Environmental Science and Engineering, Guangdong University of Technology, No. 100 Waihuan Xi Road, Guangzhou Higher Education Mega Center, Panyu District, Guangzhou 510006, China. liugg615@163.com.
[Ti] Título:Study of the simulated sunlight photolysis mechanism of ketoprofen: the role of superoxide anion radicals, transformation byproducts, and ecotoxicity assessment.
[So] Source:Environ Sci Process Impacts;19(9):1176-1184, 2017 Sep 20.
[Is] ISSN:2050-7895
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The aim of this study was to investigate the photolysis mechanism of ketoprofen (KET) under simulated sunlight. The results demonstrated that the photolysis of KET aligned well with pseudo first-order kinetics. Radical scavenging experiments and dissolved oxygen experiments revealed that the superoxide anion radical (O ˙ ) played a primary role in the photolytic process in pure water. Bicarbonate slightly increased the photodegradation of KET through generating carbonate radicals, while DOM inhibited the photolysis via both attenuating light and competing radicals. Moreover, Zhujiang river water inhibited KET phototransformation. Potential KET degradation pathways were proposed based on the identification of products using LC/MS/MS and GC/MS techniques. The theoretical prediction of reaction sites was derived from Frontier Electron Densities (FEDs), which primarily involved the KET decarboxylation reaction. The ecotoxicity of the treated solutions was evaluated by employing Daphnia magna and V. fischeri as biological indicators. Ecotoxicity was also hypothetically predicted through the "ecological structure-activity relationship" (ECOSAR) program, which revealed that toxic products might be generated during the photolysis process.
[Mh] Termos MeSH primário: Cetoprofeno/toxicidade
Modelos Teóricos
Fotólise
Luz Solar
Superóxidos/toxicidade
Poluentes Químicos da Água/toxicidade
[Mh] Termos MeSH secundário: Aliivibrio fischeri/efeitos dos fármacos
Animais
Clorófitas/efeitos dos fármacos
Daphnia/efeitos dos fármacos
Peixes/crescimento & desenvolvimento
Cetoprofeno/análise
Cetoprofeno/efeitos da radiação
Cinética
Valor Preditivo dos Testes
Superóxidos/análise
Espectrometria de Massas em Tandem
Testes de Toxicidade Aguda
Testes de Toxicidade Crônica
Poluentes Químicos da Água/análise
Poluentes Químicos da Água/efeitos da radiação
[Pt] Tipo de publicação:JOURNAL ARTICLE
[Nm] Nome de substância:
0 (Water Pollutants, Chemical); 11062-77-4 (Superoxides); 90Y4QC304K (Ketoprofen)
[Em] Mês de entrada:1801
[Cu] Atualização por classe:180108
[Lr] Data última revisão:
180108
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:170727
[St] Status:MEDLINE
[do] DOI:10.1039/c7em00111h


  10 / 22721 MEDLINE  
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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



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