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Membrane-enriched proteome changes and prion protein expression during neural differentiation and in neuroblastoma cells

2017-04-22Journal article Open access
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dc.contributor.authorMacedo, J.A.
dc.contributor.authorSchrama, Denise
dc.contributor.authorDuarte, I.
dc.contributor.authorTavares, E.
dc.contributor.authorRenaut, J.
dc.contributor.authorFutschik, Matthias
dc.contributor.authorRodrigues, Pedro
dc.contributor.authorMelo, E. P.
dc.date.accessioned2017-05-19T11:13:05Z
dc.date.available2017-05-19T11:13:05Z
dc.date.issued2017-04-22
dc.date.updated2017-04-22T06:05:07Z
dc.description.abstractBackground The function of the prion protein, involved in the so-called prion diseases, remains a subject of intense debate and the possibility that it works as a pleiotropic protein through the interaction with multiple membrane proteins is somehow supported by recent reports. Therefore, the use of proteomic and bioinformatics combined to uncover cellular processes occurring together with changes in the expression of the prion protein may provide further insight into the putative pleiotropic role of the prion protein. Results This study assessed the membrane-enriched proteome changes accompanying alterations in the expression of the prion protein. A 2D-DIGE approach was applied to two cell lines after prefractionation towards the membrane protein subset: an embryonic stem cell line and the PK1 subline of neuroblastoma cells which efficiently propagates prion infection. Several proteins were differentially abundant with the increased expression of the prion protein during neural differentiation of embryonic stem cells and with the knockdown of the prion protein in PK1 cells. The identity of around 20% of the differentially abundant proteins was obtained by tandem MS. The catalytic subunit A of succinate dehydrogenase, a key enzyme for the aerobic energy metabolism and redox homeostasis, showed a similar abundance trend as the prion protein in both proteomic experiments. A gene ontology analysis revealed “myelin sheath”, “organelle membrane” and “focal adhesion” associated proteins as the main cellular components, and “protein folding” and “ATPase activity” as the biological processes enriched in the first set of differentially abundant proteins. The known interactome of these differentially abundant proteins was customized to reveal four interactors with the prion protein, including two heat shock proteins and a protein disulfide isomerase. Conclusions Overall, our study shows that expression of the prion protein occurs concomitantly with changes in chaperone activity and cell-redox homeostasis, emphasizing the functional link between these cellular processes and the prion protein.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationBMC Genomics. 2017 Apr 22;18(1):319pt_PT
dc.identifier.doihttp://dx.doi.org/10.1186/s12864-017-3694-6pt_PT
dc.identifier.otherMFU02241; EME01032
dc.identifier.urihttp://hdl.handle.net/10400.1/9812
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherBMJ Publishing Grouppt_PT
dc.relationFunctionalized Metal Nano-Gaps for Plasmon-Enhanced Single Protein Biosensing
dc.relationAN ANIMAL CELL-BASED APPROACH TO STUDY PRION DISEASES: CELLULAR TRAFFICKING, CONFORMATIONAL CHANGES AND PRION INFECTIVITY
dc.rights.holderThe Author(s).
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectPrion proteinpt_PT
dc.subjectNeural differentiationpt_PT
dc.subjectChaperone activitypt_PT
dc.subjectRedox homeostasispt_PT
dc.subject2D-DIGEpt_PT
dc.titleMembrane-enriched proteome changes and prion protein expression during neural differentiation and in neuroblastoma cellspt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleFunctionalized Metal Nano-Gaps for Plasmon-Enhanced Single Protein Biosensing
oaire.awardTitleAN ANIMAL CELL-BASED APPROACH TO STUDY PRION DISEASES: CELLULAR TRAFFICKING, CONFORMATIONAL CHANGES AND PRION INFECTIVITY
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FQUI-BIQ%2F119677%2F2010/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FCTM-NAN%2F2700%2F2012/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/5876/UID%2FBIM%2F04773%2F2013/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/5876/UID%2FMulti%2F04326%2F2013/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT//SFRH%2FBD%2F48664%2F2008/PT
oaire.citation.issue1pt_PT
oaire.citation.startPage319pt_PT
oaire.citation.titleBMC Genomicspt_PT
oaire.citation.volume18pt_PT
oaire.fundingStream3599-PPCDT
oaire.fundingStream3599-PPCDT
oaire.fundingStream5876
oaire.fundingStream5876
person.familyNameMacedo
person.familyNameSchrama
person.familyNameFutschik
person.familyNameRodrigues
person.givenNameJoana
person.givenNameDenise
person.givenNameMatthias
person.givenNamePedro
person.identifier159154
person.identifier.ciencia-idE812-421F-FF29
person.identifier.ciencia-id501C-AC69-68C0
person.identifier.ciencia-idA71B-AD01-3501
person.identifier.orcid0000-0001-9564-4770
person.identifier.orcid0000-0003-0274-5957
person.identifier.orcid0000-0002-6245-8071
person.identifier.orcid0000-0002-9668-1204
person.identifier.ridH-6511-2016
person.identifier.ridM-3406-2013
person.identifier.scopus-author-id56094485100
person.identifier.scopus-author-id55755583400
person.identifier.scopus-author-id14017989400
person.identifier.scopus-author-id55107531000
project.funder.identifierhttp://doi.org/10.13039/501100001871
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project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
project.funder.nameFundação para a Ciência e a Tecnologia
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT
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