Please use this identifier to cite or link to this item: https://hdl.handle.net/20.500.12104/67801
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dc.contributor.authorRivas-Estilla, A.M.
dc.contributor.authorBryan-Marrugo, O.L.
dc.contributor.authorTrujillo-Murillo, K.
dc.contributor.authorPerez-Ibave, D.
dc.contributor.authorCharles-Nino, C.
dc.contributor.authorPedroza-Roldan, C.
dc.contributor.authorRios-Ibarra, C.
dc.contributor.authorRamirez-Valles, E.
dc.contributor.authorOrtiz-Lopez, R.
dc.contributor.authorIslas-Carbajal, M.C.
dc.contributor.authorNieto, N.
dc.contributor.authorRincon-Sanchez, A.R.
dc.date.accessioned2015-11-19T18:52:30Z-
dc.date.available2015-11-19T18:52:30Z-
dc.date.issued2012
dc.identifier.urihttp://hdl.handle.net/20.500.12104/67801-
dc.description.abstractWe evaluated the participation of oxidative stress in the negative regulation of hepatitis C virus (HCV)- RNA induced by acetylsalicylic acid (ASA). We used the HCV subgenomic replicon cell system that stably expresses HCV-nonstructural proteins (Huh7 HCV replicon cells) and the parental cell line. Cells were exposed to 4 mM ASA at different times (12-72 h), and pyrrolidine dithiocarbamate (PDTC) was used as an antioxidant control. Reactive oxygen species (ROS) production, oxidized protein levels, cytosolic superoxide dismutase (Cu/Zn-SOD), and glutathione peroxidase (GPx) activity were measured to evaluate oxidative stress. In addition, viral RNA and prostaglandin (PGE 2) levels were determined. We observed that ASA treatment decreased ROS production and oxidized protein levels in a time-dependent fashion in both parental and HCV replicon cells with a greater extent in the latter. Similar results were found with PDTC exposure. Average GPx activity was decreased, whereas a striking increase was observed in average cytosolic SOD activity at 48 and 72 h in both cells exposed to ASA, compared with untreated cells. HCV replicon cells showed higher levels of Cu/Zn-SOD expression (mRNA and protein) with ASA treatment (48 and 72 h), whereas NS5A protein levels showed decreased expression. In addition, we found that inhibition of SOD1 expression reversed the effect of ASA. Interestingly, PDTC downregulated HCV-RNA expression (55%) and PGE 2 (60%) levels, imitating ASA exposure. These results suggest that ASA treatment could reduce cellular oxidative stress markers and modify Cu/Zn- SOD expression, a phenomenon that may contribute to the mechanisms involved in HCV downregulation. © 2012 by the American Physiological Society.
dc.titleCu/Zn superoxide dismutase (SOD1) induction is implicated in the antioxidative and antiviral activity of acetylsalicylic acid in HCV-expressing cells
dc.typeArticle
dc.identifier.doi10.1152/ajpgi.00237.2011
dc.relation.ispartofjournalAmerican Journal of Physiology - Gastrointestinal and Liver Physiology
dc.relation.ispartofvolume302
dc.relation.ispartofissue11
dc.relation.ispartofpageG1264
dc.relation.ispartofpageG1273
dc.subject.keywordAntioxidants; Glutathione peroxidase; Hepatitis C virus; Oxidative stress; Pyrrolidine dithiocarbamate; Gastroenterology & Hepatology; Physiology
dc.contributor.affiliationRivas-Estilla, A.M., Department of Biochemistry and Molecular Medicine, School of Medicine, Autonomous Univ. of Nuevo León, Ave. Francisco I. Madero y Ave. Gonzalitos s/n, Col. Mitras Centro Monterrey, Nuevo León, 64460, Mexico; Bryan-Marrugo, O.L., Department of Biochemistry and Molecular Medicine, School of Medicine, Autonomous Univ. of Nuevo León, Ave. Francisco I. Madero y Ave. Gonzalitos s/n, Col. Mitras Centro Monterrey, Nuevo León, 64460, Mexico; Trujillo-Murillo, K., Department of Biochemistry and Molecular Medicine, School of Medicine, Autonomous Univ. of Nuevo León, Ave. Francisco I. Madero y Ave. Gonzalitos s/n, Col. Mitras Centro Monterrey, Nuevo León, 64460, Mexico; Pérez-Ibave, D., Department of Biochemistry and Molecular Medicine, School of Medicine, Autonomous Univ. of Nuevo León, Ave. Francisco I. Madero y Ave. Gonzalitos s/n, Col. Mitras Centro Monterrey, Nuevo León, 64460, Mexico; Charles-Niño, C., Biomedical Research Institute, National Autonomous University of Mexico, Distrito Federal, Mexico; Pedroza-Roldan, C., Biomedical Research Institute, National Autonomous University of Mexico, Distrito Federal, Mexico; Ríos-Ibarra, C., Department of Biochemistry and Molecular Medicine, School of Medicine, Autonomous Univ. of Nuevo León, Ave. Francisco I. Madero y Ave. Gonzalitos s/n, Col. Mitras Centro Monterrey, Nuevo León, 64460, Mexico; Ramírez-Valles, E., Department of Biochemistry and Molecular Medicine, School of Medicine, Autonomous Univ. of Nuevo León, Ave. Francisco I. Madero y Ave. Gonzalitos s/n, Col. Mitras Centro Monterrey, Nuevo León, 64460, Mexico; Ortiz-López, R., Department of Biochemistry and Molecular Medicine, School of Medicine, Autonomous Univ. of Nuevo León, Ave. Francisco I. Madero y Ave. Gonzalitos s/n, Col. Mitras Centro Monterrey, Nuevo León, 64460, Mexico, CIDCS, Autonomous University of Nuevo León, Nuevo León, Mexico; Islas-Carbajal, M.C., Cardiovascular Unit, Department of Physiology, United States; Nieto, N., Division of Liver Diseases, Mount Sinai School of Medicine, New York City, NY, United States; Rincón-Sánchez, A.R., CUCS, University of Guadalajara, JAL, Mexico
dc.relation.isReferencedByScopus
dc.relation.isReferencedByWOS
dc.identifier.urlhttp://www.scopus.com/inward/record.url?eid=2-s2.0-84861855852&partnerID=40&md5=0ac4bd7fc35c2b2f3466c7000ba129c4
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