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Metallothionein role in the kinetic model of copper accumulation and elimination in the clam Ruditapes decussatus

2009Journal article Restricted access
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dc.contributor.authorSerafim, A.
dc.contributor.authorBebianno, Maria João
dc.date.accessioned2020-04-30T15:36:36Z
dc.date.available2020-04-30T15:36:36Z
dc.date.issued2009
dc.description.abstractIn order to clarify the role of metallothioneins (MT) in copper (Cu) toxicity, this work aimed to assess the involvement of this protein in the accumulation and elimination strategies of Cu in the clam Ruditapes decussatus exposed to two sublethal concentrations (25 and 50 microgCul(-1)). The behaviour of MT in three different tissues of clams during the accumulation and depuration processes was also followed by gel-filtration chromatography to assess if Cu was bound to MT or to other cytosolic components. The 96 h LC50 for water-borne copper was 715 microgL(-1) in R. decussatus. The Cu accumulation pattern was dependent on Cu exposure concentrations. In clams exposed to 25 microgl(-1), total Cu accumulation in the three tissues increased linearly during the exposure period, while in those exposed to 50 microgl(-1) it followed the first order kinetic model. The greatest amount of Cu accumulated in all tissues is associated to the low molecular weight cytosolic fraction (>50%). The chromatographic assay indicated that Cu in the cytosolic fraction is bound to MT and MT levels increase with the increase of Cu exposure confirming the binding affinity of Cu to MT in all tissues. However, a smaller percentage of Cu seems to be bond to other ligands, such as GSH. Copper was exponentially eliminated (only studied in clams exposed to 25 microgl(-1)) and the estimated half-life was tissue dependent (9, 5 and 14 days for the gills, digestive gland and remaining tissues, respectively). Copper bound to the thermostable compounds was eliminated more quickly (t(1/2)=4-7 days) in all tissues than those bound to the thermolabile compounds (t(1/2)=7-18 days). Interestingly, MT is rapidly degraded (t(1/2)=7 and 18 days), suggesting that this protein is actively involved in the elimination of this metal, through the Cu-MT complex since MT and Cu are turning over simultaneously. Therefore, when Cu exposure is low, the clam can cope efficiently with the excess of Cu levels by increasing MT induction as well as rapidly eliminating this metal via the MT-Cu complex. Copper toxicity in the clam R. decussatus is associated to the limited capacity of MT induction at higher and environmental unrealistic Cu exposures especially in the gills and remaining tissues.pt_PT
dc.description.sponsorshipPortuguese Foundation for Science and Technology CIENCIA/BD/2541/93pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.doi10.1016/j.envres.2009.03.001pt_PT
dc.identifier.issn0013-9351
dc.identifier.urihttp://hdl.handle.net/10400.1/13821
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherElsevierpt_PT
dc.subjectAnimalspt_PT
dc.subjectBivalviapt_PT
dc.subjectCopperpt_PT
dc.subjectCytosolpt_PT
dc.subjectDose-response relationshippt_PT
dc.subjectEnvironmental monitoringpt_PT
dc.subjectGillspt_PT
dc.subjectHalf-Lifept_PT
dc.subjectKineticspt_PT
dc.subjectLethal dose 50pt_PT
dc.subjectMetallothioneinpt_PT
dc.subjectMolecular weightpt_PT
dc.subjectProtein bindingpt_PT
dc.subjectTissue distributionpt_PT
dc.subjectWater pollutantspt_PT
dc.subjectDrugpt_PT
dc.titleMetallothionein role in the kinetic model of copper accumulation and elimination in the clam Ruditapes decussatuspt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage399pt_PT
oaire.citation.issue4pt_PT
oaire.citation.startPage390pt_PT
oaire.citation.titleEnvironmental Researchpt_PT
oaire.citation.volume109pt_PT
person.familyNamePereira Serafim
person.familyNameBebianno
person.givenNameMaria Angela
person.givenNameMaria
person.identifier.ciencia-id9C18-090A-5E3D
person.identifier.ciencia-id2B11-46AC-B94B
person.identifier.orcid0000-0002-1165-0645
person.identifier.orcid0000-0003-1492-8566
person.identifier.scopus-author-id7004152715
rcaap.rightsrestrictedAccesspt_PT
rcaap.typearticlept_PT
relation.isAuthorOfPublication0e42fc03-7052-438d-952b-b3caa5bdc36a
relation.isAuthorOfPublication2e00a26d-1dd3-4c22-a6bf-ac7943ae0d32
relation.isAuthorOfPublication.latestForDiscovery0e42fc03-7052-438d-952b-b3caa5bdc36a

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