Please use this identifier to cite or link to this item: https://hdl.handle.net/10316/112594
DC FieldValueLanguage
dc.contributor.authorFerreira, Maria J.-
dc.contributor.authorRodrigues, Tony A.-
dc.contributor.authorPedrosa, Ana G.-
dc.contributor.authorGales, Luís-
dc.contributor.authorSalvador, Armindo-
dc.contributor.authorFrancisco, Tânia-
dc.contributor.authorAzevedo, Jorge E.-
dc.date.accessioned2024-02-01T12:22:19Z-
dc.date.available2024-02-01T12:22:19Z-
dc.date.issued2023-07-
dc.identifier.issn22132317pt
dc.identifier.urihttps://hdl.handle.net/10316/112594-
dc.description.abstractDespite the large amounts of H2O2 generated in mammalian peroxisomes, cysteine residues of intraperoxisomal proteins are maintained in a reduced state. The biochemistry behind this phenomenon remains unexplored, and simple questions such as "is the peroxisomal membrane permeable to glutathione?" or "is there a thiol-disulfide oxidoreductase in the organelle matrix?" still have no answer. We used a cell-free in vitro system to equip rat liver peroxisomes with a glutathione redox sensor. The organelles were then incubated with glutathione solutions of different redox potentials and the oxidation/reduction kinetics of the redox sensor was monitored. The data suggest that the mammalian peroxisomal membrane is promptly permeable to both reduced and oxidized glutathione. No evidence for the presence of a robust thiol-disulfide oxidoreductase in the peroxisomal matrix could be found. Also, prolonged incubation of organelle suspensions with glutaredoxin 1 did not result in the internalization of the enzyme. To explore a potential role of glutathione in intraperoxisomal redox homeostasis we performed kinetic simulations. The results suggest that even in the absence of a glutaredoxin, glutathione is more important in protecting cysteine residues of matrix proteins from oxidation by H2O2 than peroxisomal catalase itself.pt
dc.language.isoengpt
dc.publisherElsevierpt
dc.relationUIDB/04293/2020pt
dc.relationPOCI-01-0145-FEDER-007274pt
dc.relationUIDB/04539/2020pt
dc.relationLA/P/0058/2020pt
dc.relationUIDB/00313/2020pt
dc.relationinfo:eu-repo/grantAgreement/UIDP/04539/2020pt
dc.relationUIDP/00313/2020pt
dc.relationNORTE-01-0145-FEDER-000008pt
dc.rightsopenAccesspt
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt
dc.subjectPeroxisomept
dc.subjectGlutathionept
dc.subjectMembrane permeabilitypt
dc.subjectGlutaredoxinpt
dc.subjectProtein importpt
dc.subjectKinetic simulationpt
dc.subject.meshRatspt
dc.subject.meshAnimalspt
dc.subject.meshGlutathione Disulfidept
dc.subject.meshCysteinept
dc.subject.meshHydrogen Peroxidept
dc.subject.meshGlutathionept
dc.subject.meshOxidation-Reductionpt
dc.subject.meshProteinspt
dc.subject.meshMammalspt
dc.subject.meshHomeostasispt
dc.subject.meshPeroxisomespt
dc.subject.meshProtein Disulfide Reductase (Glutathione)pt
dc.titleThe mammalian peroxisomal membrane is permeable to both GSH and GSSG - Implications for intraperoxisomal redox homeostasispt
dc.typearticle-
degois.publication.firstPage102764pt
degois.publication.titleRedox Biologypt
dc.peerreviewedyespt
dc.identifier.doi10.1016/j.redox.2023.102764pt
degois.publication.volume63pt
dc.date.embargo2023-07-01*
uc.date.periodoEmbargo0pt
item.openairetypearticle-
item.fulltextCom Texto completo-
item.languageiso639-1en-
item.grantfulltextopen-
item.cerifentitytypePublications-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
crisitem.project.grantnoInstitute for Research and Innovation in Health-
crisitem.project.grantnoCenter for Innovative Biomedicine and Biotechnology - CIBB-
crisitem.project.grantnoCenter for Innovative Biomedicine and Biotechnology - Associate Laboratory-
crisitem.project.grantnoCoimbra Chemistry Center-
crisitem.project.grantnoCenter for Innovative Biomedicine and Biotechnology-
Appears in Collections:I&D CQC - Artigos em Revistas Internacionais
I&D CNC - Artigos em Revistas Internacionais
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