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Redox thiol status plays a central role in the mobilization and metabolism of nitric oxide in human red blood cells

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dc.contributor.authorLopes de Almeida, José Pedro
dc.contributor.authorCarvalho, Filomena Almeida
dc.contributor.authorSilva-Herdade, Ana S.
dc.contributor.authorSantos-Freitas, Teresa
dc.contributor.authorSaldanha, Carlota
dc.date.accessioned2020-10-22T13:24:29Z
dc.date.available2020-10-22T13:24:29Z
dc.date.issued2009
dc.descriptionCopyright © 2008 International Federation for Cell Biology. Published by Elsevier Ltd. All rights reserved.pt_PT
dc.description.abstractWe assessed the redox thiol status influence on nitric oxide (NO) metabolism and efflux in erythrocytes stimulated with acetylcholinesterase substrate (acetylcholine, ACh) and inhibitor (velnacrine maleate, VM). Erythrocyte suspensions from healthy donors were incubated with increasing concentrations of dithiothreitol (1-50microM), in the presence and absence of acetylcholine/velnacrine (10microM). Levels of NO, nitrite/nitrate, S-nitrosohemoglobin, peroxynitrite and S-nitrosoglutathione were determined by spectrofluorimetric and spectrophotometric methods. Dithiothreitol significantly mobilized NO toward nitrite/nitrate and S-nitrosoglutathione, and decreased the amount of NO efflux. Both ACh/VM induce changes on the levels of erythrocyte nitrite/nitrate dependent on the DTT concentration. Higher levels of peroxynitrite and S-nitrosoglutathione were seen with velnacrine in presence of DTT 1 and 50microM. We concluded that dithiothreitol-induced activation of erythrocyte thiol status decreases NO efflux and allows greater intracellular NO mobilization onto different derivative molecules, both in the absence and presence of acetylcholinesterase substrate and inhibitor.pt_PT
dc.description.sponsorshipThis study was supported by grants from the GAPIC Department (Gabinete de Apoio à Investigação Científica, Tecnológica e de Inovação) of Lisbon University Faculty of Medicine.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationCell Biology International 33 (2009) 268-275pt_PT
dc.identifier.doi10.1016/j.cellbi.2008.11.012pt_PT
dc.identifier.eissn1095-8355
dc.identifier.issn1065-6995
dc.identifier.urihttp://hdl.handle.net/10451/44640
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherElsevierpt_PT
dc.relation.publisherversionhttps://onlinelibrary.wiley.com/journal/10958355pt_PT
dc.subjectAcetylcholinesterasept_PT
dc.subjectErythrocytept_PT
dc.subjectNitric oxidept_PT
dc.subjectRedox thiol statuspt_PT
dc.subjectS-nitrosothiolspt_PT
dc.titleRedox thiol status plays a central role in the mobilization and metabolism of nitric oxide in human red blood cellspt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage275pt_PT
oaire.citation.issue3pt_PT
oaire.citation.startPage268pt_PT
oaire.citation.titleCell Biology Internationalpt_PT
oaire.citation.volume33pt_PT
person.familyNameCarvalho
person.familyNameSilva-Herdade
person.familyNameSaldanha
person.givenNameFilomena
person.givenNameAna S.
person.givenNameCarlota
person.identifier749915
person.identifier53901
person.identifier.ciencia-id4615-4AEC-8D91
person.identifier.ciencia-id6517-B340-F362
person.identifier.orcid0000-0001-6088-3894
person.identifier.orcid0000-0002-3023-1315
person.identifier.orcid0000-0002-5058-2112
person.identifier.ridM-9202-2013
person.identifier.ridB-2735-2019
person.identifier.scopus-author-id7103069694
rcaap.rightsrestrictedAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication547cb993-880c-4608-b1e0-493ad469eecb
relation.isAuthorOfPublicationad32fa9b-85eb-4679-a4c9-9f6109423b88
relation.isAuthorOfPublicationad6de30c-87ca-4613-bb87-488dd5d285d0
relation.isAuthorOfPublication.latestForDiscovery547cb993-880c-4608-b1e0-493ad469eecb

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