dc.creator | CSANYI, Gabor | |
dc.creator | CIFUENTES-PAGANO, Eugenia | |
dc.creator | GHOULEH, Imad Al | |
dc.creator | RANAYHOSSAINI, Daniel J. | |
dc.creator | EGANA, Loreto | |
dc.creator | LOPES, Lucia R. | |
dc.creator | JACKSON, Heather M. | |
dc.creator | KELLEY, Eric E. | |
dc.creator | PAGANO, Patrick J. | |
dc.date.accessioned | 2012-10-20T03:20:24Z | |
dc.date.accessioned | 2018-07-04T15:35:14Z | |
dc.date.available | 2012-10-20T03:20:24Z | |
dc.date.available | 2018-07-04T15:35:14Z | |
dc.date.created | 2012-10-20T03:20:24Z | |
dc.date.issued | 2011 | |
dc.identifier | FREE RADICAL BIOLOGY AND MEDICINE, v.51, n.6, p.1116-1125, 2011 | |
dc.identifier | 0891-5849 | |
dc.identifier | http://producao.usp.br/handle/BDPI/28161 | |
dc.identifier | 10.1016/j.freeradbiomed.2011.04.025 | |
dc.identifier | http://dx.doi.org/10.1016/j.freeradbiomed.2011.04.025 | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1624805 | |
dc.description.abstract | In recent years, reactive oxygen species (ROS) derived from the vascular isoforms of NADPH oxidase, Nox1, Nox2, and Nox4, have been implicated in many cardiovascular pathologies. As a result, the selective inhibition of these isoforms is an area of intense current investigation. In this study, we postulated that Nox2ds, a peptidic inhibitor that mimics a sequence in the cytosolic B-loop of Nox2, would inhibit ROS production by the Nox2-. but not the Noxl- and Nox4-oxidase systems. To test our hypothesis, the inhibitory activity of Nox2ds was assessed in cell-free assays using reconstituted systems expressing the Nox2-, canonical or hybrid Nox1- or Nox4-oxidase. Our findings demonstrate that Nox2ds, but not its scrambled control, potently inhibited superoxide (O(2)(center dot-)) production in the Nox2 cell-free system, as assessed by the cytochrome c assay. Electron paramagnetic resonance confirmed that Nox2ds inhibits O(2)(center dot-) production by Nox2 oxidase. In contrast, Nox2ds did not inhibit ROS production by either Nox1- or Nox4-oxidase. These findings demonstrate that Nox2ds is a selective inhibitor of Nox2-oxidase and support its utility to elucidate the role of Nox2 in organ pathophysiology and its potential as a therapeutic agent. (C) 2011 Elsevier Inc. All rights reserved. | |
dc.language | eng | |
dc.publisher | ELSEVIER SCIENCE INC | |
dc.relation | Free Radical Biology and Medicine | |
dc.rights | Copyright ELSEVIER SCIENCE INC | |
dc.rights | restrictedAccess | |
dc.subject | NADPH oxidase | |
dc.subject | Reactive oxygen species | |
dc.subject | Superoxide | |
dc.subject | Nox inhibitor | |
dc.subject | Cardiovascular disease | |
dc.subject | Free radicals | |
dc.title | Nox2 B-loop peptide, Nox2ds, specifically inhibits the NADPH oxidase Nox2 | |
dc.type | Artículos de revistas | |