Differential redox proteomics allows identification of proteins reversibly oxidized at cysteine residues in endothelial cells in response to acute hypoxia

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dc.contributor.authorIzquierdo-Álvarez, Alicia
dc.contributor.authorRamos, Elena
dc.contributor.authorVillanueva, Joan
dc.contributor.authorHernansanz-Agustín, Pablo
dc.contributor.authorFernández-Rodríguez, Rubén
dc.contributor.authorTello, Daniel
dc.contributor.authorCarrascal, Montserrat
dc.contributor.authorMartínez Ruiz, Antonio
dc.date.accessioned2024-05-21T14:40:25Z
dc.date.available2024-05-21T14:40:25Z
dc.date.issued2012-09
dc.description.abstractAdaptation to decreased oxygen availability (hypoxia) is crucial for proper cell function and survival. In metazoans, this is partly achieved through gene transcriptional responses mediated by hypoxia-inducible factors (HIFs). There is abundant evidence that production of reactive oxygen species (ROS) increases during hypoxia, which contributes to the activation of the HIF pathway. In addition to altering the cellular redox balance, leading to oxidative stress, ROS can transduce signals by reversibly modifying the redox state of cysteine residues in certain proteins. Using the “redox fluorescence switch” (RFS), a thiol redox proteomic technique that fluorescently labels reversibly oxidized cysteines, we analyzed endothelial cells subjected to acute hypoxia and subsequent reoxygenation. We observed a general increase in cysteine oxidation during hypoxia, which was reversed by reoxygenation, and two-dimensional electrophoresis revealed the differential oxidation of specific proteins. Using complementary derivatization techniques, we confirmed the modification of individual target proteins and identified specific cysteine residues that were oxidized in hypoxic conditions, thereby overcoming several limitations associated with fluorescence derivatization. These findings provide an important basis for future studies of the role of these modifications in HIF activation and in other acute adaptive responses to hypoxia.
dc.description.departmentDepto. de Bioquímica y Biología Molecular
dc.description.facultyFac. de Farmacia
dc.description.refereedTRUE
dc.description.sponsorshipGobierno de España
dc.description.sponsorshipMinisterio de Ciencia e Innovación
dc.description.statuspub
dc.identifier.doi10.1016/j.jprot.2012.06.035
dc.identifier.issn1874-3919
dc.identifier.urihttps://hdl.handle.net/20.500.14352/104285
dc.journal.titleJournal of Proteomics
dc.language.isoeng
dc.page.final5462
dc.page.initial5449
dc.relation.projectIDinfo:eu-repo/grantAgreement/MSC//CP07%2F00143/ES/CP07%2F00143/
dc.relation.projectIDCSD2007-00020
dc.relation.projectIDinfo:eu-repo/grantAgreement/MICINN//PS09%2F00101/ES/PAPEL DE LAS ESPECIES REACTIVAS DE OXIGENO Y NITROGENO Y DE LAS MODIFICACIONES OXIDATIVAS DE PROTEINAS EN LA RESPUESTA A HIPOXIA EN FISIOPATOLOGIA CARDIOVASCULAR/
dc.rights.accessRightsopen access
dc.subject.cdu577.1
dc.subject.cdu577.2
dc.subject.keywordPost-translational modifications
dc.subject.keywordCysteine oxidation
dc.subject.keywordThiol redox proteomics
dc.subject.keywordRedox fluorescence switch (RFS)
dc.subject.keywordTwo-dimensional electrophoresis (2-DE)
dc.subject.keywordCell signaling
dc.subject.ucmBioquímica (Farmacia)
dc.subject.unesco2302 Bioquímica
dc.titleDifferential redox proteomics allows identification of proteins reversibly oxidized at cysteine residues in endothelial cells in response to acute hypoxia
dc.typejournal article
dc.type.hasVersionAM
dc.volume.number75
dspace.entity.typePublication
relation.isAuthorOfPublicationeec0b303-34c9-47dd-9ec6-704b6c6c7acd
relation.isAuthorOfPublication.latestForDiscoveryeec0b303-34c9-47dd-9ec6-704b6c6c7acd
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