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Actin as a potential target for decavanadate

dc.contributor.authorRamos, Susana
dc.contributor.authorMoura, José J. G.
dc.contributor.authorAureliano, M.
dc.date.accessioned2012-06-27T09:55:18Z
dc.date.available2012-06-27T09:55:18Z
dc.date.issued2010
dc.description.abstractATP prevents G-actin cysteine oxidation and vanadyl formation specifically induced by decavanadate, suggesting that the oxometalate–protein interaction is affected by the nucleotide. The ATP exchange rate is increased by 2-fold due to the presence of decavanadate when compared with control actin (3.1×10−3 s−1), and an apparent dissociation constant (kdapp) of 227.4±25.7 μM and 112.3±8.7 μM was obtained in absence or presence of 20 μM V10, respectively. Moreover, concentrations as low as 50 μM of decameric vanadate species (V10) increases the relative G-actin intrinsic fluorescence intensity by approximately 80% whereas for a 10-fold concentration of monomeric vanadate (V1) no effects were observed. Upon decavanadate titration, it was observed a linear increase in G-actin hydrophobic surface (2.6-fold), while no changes were detected for V1 (0–200 μM). Taken together, three major ideas arise: i) ATP prevents decavanadate-induced G-actin cysteine oxidation and vanadate reduction; ii) decavanadate promotes actin conformational changes resulting on its inactivation, iii) decavanadate has an effect on actin ATP binding site. Once it is demonstrated that actin is a new potential target for decavanadate, being the ATP binding site a suitable site for decavanadate binding, it is proposed that some of the biological effects of vanadate can be, at least in part, explained by decavanadate interactions with actin.por
dc.identifier.issn0162-0134
dc.identifier.urihttp://hdl.handle.net/10400.1/1325
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherElsevierpor
dc.subjectActinpor
dc.subjectDecavanadatepor
dc.titleActin as a potential target for decavanadatepor
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage1239por
oaire.citation.issue104por
oaire.citation.startPage1234por
oaire.citation.titleJournal of Inorganic Biochemistrypor
person.familyNameAureliano
person.givenNameManuel
person.identifier584146
person.identifier.ciencia-idAA14-3490-DC5E
person.identifier.orcid0000-0003-4858-3201
person.identifier.ridI-3283-2012
person.identifier.scopus-author-id6603412860
rcaap.rightsrestrictedAccesspor
rcaap.typearticlepor
relation.isAuthorOfPublicationbb413661-7edd-4b57-8338-33889cfd05db
relation.isAuthorOfPublication.latestForDiscoverybb413661-7edd-4b57-8338-33889cfd05db

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