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Hormone affinity and fibril formation of piscine transthyretin: the role of the N-terminal

2008Artigo científico Acesso aberto
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dc.contributor.authorMorgado, Isabel
dc.contributor.authorMelo, Eduardo P.
dc.contributor.authorLundberg, Erik
dc.contributor.authorEstrela, Nídia L.
dc.contributor.authorSauer-Eriksson, A. Elisabeth
dc.contributor.authorPower, Deborah
dc.date.accessioned2014-10-23T09:34:13Z
dc.date.available2014-10-23T09:34:13Z
dc.date.issued2008
dc.description.abstractTransthyretin (TTR) transports thyroid hormones (THs), thyroxine (T4) and triiodothyronine (T3) in the blood of vertebrates. TH-binding sites are highly conserved in vertebrate TTR however, piscine TTR has a longer N-terminus which is thought to influence TH-binding affinity and may influence TTR stability. We produced recombinant wild-type sea bream TTR (sbTTRWT) plus two mutants in which six (sbTTRM6) and twelve (sbTTRM12) N-terminal residues were removed. Ligandbinding studies revealed similar affinities for T3 (Kd=10.6±1.7nM) and T4 (Kd=9.8±0.97nM) binding to sbTTRWT. Affinity for THs was unaltered in sbTTRM12 but sbTTRM6 had poorer affinity for T4 (Kd=252.3±15.8nM) implying that some residues in the N-terminus can influence T4 binding. sbTTRM6 inhibited acid-mediated fibril formation in vitro as shown by fluorometric measurements using thioflavine-T.In contrast, fibril formation by sbTTRM12 was significant, probably due to decreased stability of the tetramer. Such studies also suggested that sbTTRWT is more resistant to fibril formation than human TTR.por
dc.identifier.citationIsabel Morgado, Eduardo P. Melo, Erik Lundberg, N´ıdia L. Estrela, A. Elisabeth Sauer-Eriksson, Deborah M. Power, "Hormone affinity and fibril formation of piscine transthyretin The role of the N-terminal" in Molecular and Cellular Endocrinology 295, 1-2 (2008) 48.por
dc.identifier.doihttp://dx.doi.org/10.1016/j.mce.2008.06.010
dc.identifier.issn0303-7207
dc.identifier.otherAUT: ELU70091; DPO00386;
dc.identifier.urihttp://hdl.handle.net/10400.1/5419
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherElsevierpor
dc.relationDevelopment of a new methodology for assessing fish and larvae nutritional status
dc.subjectAmyloid fibrilspor
dc.subjectRecombinant proteinpor
dc.subjectLigand binding characteristicspor
dc.subjectTransthyretinpor
dc.subjectTTR tetramer stabilitypor
dc.titleHormone affinity and fibril formation of piscine transthyretin: the role of the N-terminalpor
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleDevelopment of a new methodology for assessing fish and larvae nutritional status
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/POCI/POCTI%2FCVT%2F38703%2F2001/PT
oaire.citation.endPage58por
oaire.citation.issue1-2por
oaire.citation.startPage48por
oaire.citation.titleMolecular and Cellular Endocrinologypor
oaire.citation.volume295por
oaire.fundingStreamPOCI
person.familyNameMorgado
person.familyNamePower
person.givenNameIsabel
person.givenNameDeborah Mary
person.identifier.ciencia-id3315-7715-C3B4
person.identifier.ciencia-id891A-8A44-3CAE
person.identifier.orcid0000-0002-7826-997X
person.identifier.orcid0000-0003-1366-0246
person.identifier.ridJ-4798-2013
person.identifier.scopus-author-id18134268300
person.identifier.scopus-author-id7101806760
project.funder.identifierhttp://doi.org/10.13039/501100001871
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspor
rcaap.typearticlepor
relation.isAuthorOfPublication67026aa2-ccdb-4b68-9938-b09e0fd6aca0
relation.isAuthorOfPublicationc68f5ffb-63f6-4c70-8957-29e464fb59c0
relation.isAuthorOfPublication.latestForDiscovery67026aa2-ccdb-4b68-9938-b09e0fd6aca0
relation.isProjectOfPublicationc4e7ccd9-0dc4-4cc8-827b-0c76fb61832e
relation.isProjectOfPublication.latestForDiscoveryc4e7ccd9-0dc4-4cc8-827b-0c76fb61832e

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