dc.creatorCSANYI, Gabor
dc.creatorCIFUENTES-PAGANO, Eugenia
dc.creatorGHOULEH, Imad Al
dc.creatorRANAYHOSSAINI, Daniel J.
dc.creatorEGANA, Loreto
dc.creatorLOPES, Lucia R.
dc.creatorJACKSON, Heather M.
dc.creatorKELLEY, Eric E.
dc.creatorPAGANO, Patrick J.
dc.date.accessioned2012-10-20T03:20:24Z
dc.date.accessioned2018-07-04T15:35:14Z
dc.date.available2012-10-20T03:20:24Z
dc.date.available2018-07-04T15:35:14Z
dc.date.created2012-10-20T03:20:24Z
dc.date.issued2011
dc.identifierFREE RADICAL BIOLOGY AND MEDICINE, v.51, n.6, p.1116-1125, 2011
dc.identifier0891-5849
dc.identifierhttp://producao.usp.br/handle/BDPI/28161
dc.identifier10.1016/j.freeradbiomed.2011.04.025
dc.identifierhttp://dx.doi.org/10.1016/j.freeradbiomed.2011.04.025
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1624805
dc.description.abstractIn 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.languageeng
dc.publisherELSEVIER SCIENCE INC
dc.relationFree Radical Biology and Medicine
dc.rightsCopyright ELSEVIER SCIENCE INC
dc.rightsrestrictedAccess
dc.subjectNADPH oxidase
dc.subjectReactive oxygen species
dc.subjectSuperoxide
dc.subjectNox inhibitor
dc.subjectCardiovascular disease
dc.subjectFree radicals
dc.titleNox2 B-loop peptide, Nox2ds, specifically inhibits the NADPH oxidase Nox2
dc.typeArtículos de revistas


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