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Cu2+-induced isoproterenol oxidation into isoprenochrome in adult rat calcium-tolerant cardiomyocytes

2002Journal article Restricted access
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dc.contributor.authorRemião, Fernando
dc.contributor.authorCarvalho, Márcia
dc.contributor.authorCarmo, Helena
dc.contributor.authorCarvalho, Félix
dc.contributor.authorBastos, Maria L.
dc.date.accessioned2021-07-01T15:34:07Z
dc.date.available2021-07-01T15:34:07Z
dc.date.issued2002
dc.description.abstractSustained high levels of circulating catecholamines may induce cardiotoxicity. There is increasing evidence that this could result from catecholamine oxidation into aminochromes, which is catalyzed by transition metals. In fact, it has already been shown that copper-induced oxidation of the beta-agonist isoproterenol decreases the viability of isolated cardiomyocytes. Thus, the aim of this work was to contribute for the clarification of the mechanisms underlying the toxic effects of isoproterenol, Cu2+ and their concomitant effect in isolated rat cardiomyocytes. Freshly isolated calcium-tolerant cardiomyocytes from adult rat were incubated with 1 mM isoproterenol, 20 microM Cu2+ or with both during 4 h. Isoproterenol and its aminochrome (isoprenochrome), and reduced and oxidized glutathione were measured at each hour in the incubation medium and in the cells. The intracellular activities of the selenium-dependent glutathione peroxidase, glutathione reductase, and glutathione-S-transferase were determined after 4 h of incubation. Isoprenochrome was found in both cells and incubation medium in samples incubated with isoproterenol alone. However, in the isoproterenol plus Cu2+ samples, a greater depletion of isoproterenol accompanied by a proportional increase of isoprenochrome was observed. This higher ISO oxidation resulted in the depletion of intracellular glutathione and in the release of oxidized glutathione to the incubation medium. The content of total glutathione (intra- and extracellular) and the intracellular activity of the selenium-dependent glutathione peroxidase, glutathione reductase, and glutathione-S-transferase were also decreased in the isoproterenol plus Cu2+ samples. These results seem to indicate that the oxidative stress resulting from catecholamine/transition metal association may contribute to catecholamine cardiotoxicity.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.doi10.1021/tx025518qpt_PT
dc.identifier.issn0893-228X
dc.identifier.urihttp://hdl.handle.net/10284/10001
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherAmerican Chemical Societypt_PT
dc.relationThis work was supported by a project from FCT and POCTI, Portugal, and by FEDER European Community funding (project POCTI/36099/ FCB/2000).pt_PT
dc.subjectCopperpt_PT
dc.subjectGlutathione peroxidasept_PT
dc.subjectGlutathione reductasept_PT
dc.subjectIsoproterenolpt_PT
dc.subjectCardiomyocytespt_PT
dc.titleCu2+-induced isoproterenol oxidation into isoprenochrome in adult rat calcium-tolerant cardiomyocytespt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage869pt_PT
oaire.citation.issue6pt_PT
oaire.citation.startPage861pt_PT
oaire.citation.titleChemical Research in Toxicologypt_PT
oaire.citation.volume15pt_PT
person.familyNameCarvalho
person.givenNameMarcia
person.identifier2017111
person.identifier.ciencia-id8B10-171E-E63E
person.identifier.orcid0000-0001-9884-4751
person.identifier.ridD-5999-2013
person.identifier.scopus-author-id7201413997
rcaap.rightsclosedAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication3837b828-ba57-47f7-a811-cce65e4922c6
relation.isAuthorOfPublication.latestForDiscovery3837b828-ba57-47f7-a811-cce65e4922c6

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