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dc.contributor.authorTorres-Garcia, Laura
dc.contributor.authorP Domingues, Joana M
dc.contributor.authorBrandi, Edoardo
dc.contributor.authorHaikal, Caroline
dc.contributor.authorMudannayake, Janitha M
dc.contributor.authorBrás, Inês C
dc.contributor.authorGerhardt, Ellen
dc.contributor.authorLi, Wen
dc.contributor.authorSvanbergsson, Alexander
dc.contributor.authorOuteiro, Tiago F
dc.contributor.authorGouras, Gunnar K
dc.contributor.authorLi, Jia-Yi
dc.date.accessioned2022-03-28T19:06:27Z
dc.date.available2022-03-28T19:06:27Z
dc.date.issued2022-02-22
dc.identifier.issn2045-2322
dc.identifier.other35194057
dc.identifier.otherPMC8863885
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/335414
dc.description.abstractParkinson's disease (PD) and Alzheimer's disease (AD) are characterized by pathological accumulation and aggregation of different amyloidogenic proteins, α-synuclein (aSyn) in PD, and amyloid-β (Aβ) and Tau in AD. Strikingly, few PD and AD patients' brains exhibit pure pathology with most cases presenting mixed types of protein deposits in the brain. Bimolecular fluorescence complementation (BiFC) is a technique based on the complementation of two halves of a fluorescent protein, which allows direct visualization of protein-protein interactions. In the present study, we assessed the ability of aSyn and Tau to interact with each other. For in vitro evaluation, HEK293 and human neuroblastoma cells were used, while in vivo studies were performed by AAV6 injection in the substantia nigra pars compacta (SNpc) of mice and rats. We observed that the co-expression of aSyn and Tau led to the emergence of fluorescence, reflecting the interaction of the proteins in cell lines, as well as in mouse and rat SNpc. Thus, our data indicates that aSyn and Tau are able to interact with each other in a biologically relevant context, and that the BiFC assay is an effective tool for studying aSyn-Tau interactions in vitro and in different rodent models in vivo.
dc.languageeng
dc.publisherSpringer Science and Business Media LLC
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourceessn: 2045-2322
dc.sourcenlmid: 101563288
dc.subjectCell Line, Tumor
dc.subjectAnimals
dc.subjectHumans
dc.subjectMice
dc.subjectRats
dc.subjecttau Proteins
dc.subjectFluorescent Antibody Technique
dc.subjectFluorescence
dc.subjectalpha-Synuclein
dc.subjectHEK293 Cells
dc.subjectProtein Interaction Maps
dc.subjectIn Vitro Techniques
dc.subjectProtein Aggregates
dc.titleMonitoring the interactions between alpha-synuclein and Tau in vitro and in vivo using bimolecular fluorescence complementation.
dc.typeArticle
dc.date.updated2022-03-28T19:06:27Z
prism.issueIdentifier1
prism.publicationNameSci Rep
prism.volume12
dc.identifier.doi10.17863/CAM.82843
dcterms.dateAccepted2022-01-31
rioxxterms.versionofrecord10.1038/s41598-022-06846-9
rioxxterms.versionVoR
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0/
dc.contributor.orcidGouras, Gunnar K [0000-0002-5500-6325]
dc.identifier.eissn2045-2322
cam.issuedOnline2022-02-22


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Attribution 4.0 International
Except where otherwise noted, this item's licence is described as Attribution 4.0 International