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Baccharis trimera inhibits reactive oxygen species production through PKC and down-regulation p47 phox phosphorylation of NADPH oxidase in SK Hep-1 cells.
de Araújo, Glaucy Rodrigues; Rabelo, Ana Carolina Silveira; Meira, Janaína Serenato; Rossoni-Júnior, Joamyr Victor; Castro-Borges, William de; Guerra-Sá, Renata; Batista, Maurício Azevedo; Silveira-Lemos, Denise da; Souza, Gustavo Henrique Bianco de; Brandão, Geraldo Célio; Chaves, Míriam Martins; Costa, Daniela Caldeira.
Afiliação
  • de Araújo GR; 1 Center for Research in Biological Sciences - NUPEB, Federal University of Ouro Preto, 35400-000 Ouro Preto, Brazil.
  • Rabelo AC; 2 Department of Biological Sciences, Federal University of Ouro Preto, 35400-000 Ouro Preto, Brazil.
  • Meira JS; 2 Department of Biological Sciences, Federal University of Ouro Preto, 35400-000 Ouro Preto, Brazil.
  • Rossoni-Júnior JV; 1 Center for Research in Biological Sciences - NUPEB, Federal University of Ouro Preto, 35400-000 Ouro Preto, Brazil.
  • Castro-Borges W; 1 Center for Research in Biological Sciences - NUPEB, Federal University of Ouro Preto, 35400-000 Ouro Preto, Brazil.
  • Guerra-Sá R; 2 Department of Biological Sciences, Federal University of Ouro Preto, 35400-000 Ouro Preto, Brazil.
  • Batista MA; 1 Center for Research in Biological Sciences - NUPEB, Federal University of Ouro Preto, 35400-000 Ouro Preto, Brazil.
  • Silveira-Lemos DD; 2 Department of Biological Sciences, Federal University of Ouro Preto, 35400-000 Ouro Preto, Brazil.
  • Souza GH; 3 Postgraduate Program in Parasitology, Immunology Laboratory and Genomic Parasites, Federal University of Minas Gerais, 31270-901 Belo Horizonte, MG, Brazil.
  • Brandão GC; 3 Postgraduate Program in Parasitology, Immunology Laboratory and Genomic Parasites, Federal University of Minas Gerais, 31270-901 Belo Horizonte, MG, Brazil.
  • Chaves MM; 1 Center for Research in Biological Sciences - NUPEB, Federal University of Ouro Preto, 35400-000 Ouro Preto, Brazil.
  • Costa DC; 4 Department of Pharmaceutical Sciences - DEFAR, Program Postgraduate Pharmaceutical Sciences (CIPHARMA), School of Pharmacy, Federal University of Ouro Preto, 35400-000 Ouro Preto, Brazil.
Exp Biol Med (Maywood) ; 242(3): 333-343, 2017 02.
Article em En | MEDLINE | ID: mdl-28103717
Baccharis trimera, popularly known as "carqueja", is a native South-American plant possessing a high concentration of polyphenolic compounds and therefore high antioxidant potential. Despite the antioxidant potential described for B. trimera, there are no reports concerning the signaling pathways involved in this process. So, the aim of the present study was to assess the influence of B. trimera on the modulation of PKC signaling pathway and to characterize the effect of the nicotinamide adenine dinucleotide phosphate oxidase enzyme (NOX) on the generation of reactive oxygen species in SK Hep-1 cells. SK-Hep 1 cells were treated with B. trimera, quercetin, or rutin and then stimulated or not with PMA/ionomycin and labeled with carboxy H2DCFDA for detection of reactive oxygen species by flow cytometer. The PKC expression by Western blot and enzyme activity was performed to evaluate the influence of B. trimera and quercetin on PKC signaling pathway. p47 phox and p47 phox phosphorylated expression was performed by Western blot to evaluate the influence of B. trimera on p47 phox phosphorylation. The results showed that cells stimulated with PMA/ionomycin (activators of PKC) showed significantly increased reactive oxygen species production, and this production returned to baseline levels after treatment with DPI (NOX inhibitor). Both B. trimera and quercetin modulated reactive oxygen species production through the inhibition of PKC protein expression and enzymatic activity, also with inhibition of p47 phox phosphorylation. Taken together, these results suggest that B. trimera has a potential mechanism for inhibiting reactive oxygen species production through the PKC signaling pathway and inhibition subunit p47 phox phosphorylation of nicotinamide adenine dinucleotide phosphate oxidase.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteína Quinase C / Espécies Reativas de Oxigênio / NADPH Oxidases / Baccharis / Antioxidantes Idioma: En Ano de publicação: 2017 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Proteína Quinase C / Espécies Reativas de Oxigênio / NADPH Oxidases / Baccharis / Antioxidantes Idioma: En Ano de publicação: 2017 Tipo de documento: Article