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dc.contributor.author
Jongsma, Elisabeth
dc.contributor.author
Goyala, Anita
dc.contributor.author
Mateos, José María
dc.contributor.author
Ewald, Collin
dc.date.accessioned
2023-10-23T12:01:56Z
dc.date.available
2023-10-18T01:34:28Z
dc.date.available
2023-10-23T12:01:56Z
dc.date.issued
2023-09-29
dc.identifier.issn
2050-084X
dc.identifier.other
10.7554/eLife.83465
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/637192
dc.identifier.doi
10.3929/ethz-b-000637192
dc.description.abstract
The amyloid beta (Aβ) plaques found in Alzheimer's disease (AD) patients' brains contain collagens and are embedded extracellularly. Several collagens have been proposed to influence Aβ aggregate formation, yet their role in clearance is unknown. To investigate the potential role of collagens in forming and clearance of extracellular aggregates in vivo, we created a transgenic Caenorhabditis elegans strain that expresses and secretes human Aβ1-42. This secreted Aβ forms aggregates in two distinct places within the extracellular matrix. In a screen for extracellular human Aβ aggregation regulators, we identified different collagens to ameliorate or potentiate Aβ aggregation. We show that a disintegrin and metalloprotease a disintegrin and metalloprotease 2 (ADM-2), an ortholog of ADAM9, reduces the load of extracellular Aβ aggregates. ADM-2 is required and sufficient to remove the extracellular Aβ aggregates. Thus, we provide in vivo evidence of collagens essential for aggregate formation and metalloprotease participating in extracellular Aβ aggregate removal.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
eLife Sciences Publications
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/4.0/
dc.title
Removal of extracellular human amyloid beta aggregates by extracellular proteases in C. elegans
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 4.0 International
ethz.journal.title
eLife
ethz.journal.volume
12
en_US
ethz.pages.start
e83465
en_US
ethz.size
21 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.grant
The role of extracellular matrix enhancement in promoting healthy aging
en_US
ethz.grant
Protein homeostasis of extracellular proteins during aging
en_US
ethz.identifier.wos
ethz.identifier.scopus
ethz.publication.place
Cambridge
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02070 - Dep. Gesundheitswiss. und Technologie / Dep. of Health Sciences and Technology::02540 - Institut für Translationale Medizin / Institute of Translational Medicine::09598 - Ewald, Collin Y. (ehemalig) / Ewald, Collin Y. (former)
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02070 - Dep. Gesundheitswiss. und Technologie / Dep. of Health Sciences and Technology::02540 - Institut für Translationale Medizin / Institute of Translational Medicine::09598 - Ewald, Collin Y. (ehemalig) / Ewald, Collin Y. (former)
ethz.grant.agreementno
163898
ethz.grant.agreementno
190072
ethz.grant.fundername
SNF
ethz.grant.fundername
SNF
ethz.grant.funderDoi
10.13039/501100001711
ethz.grant.funderDoi
10.13039/501100001711
ethz.grant.program
SNF-Förderungsprofessuren Stufe 2
ethz.grant.program
SNF-Förderungsprofessuren: Fortsetzungsgesuche
ethz.date.deposited
2023-10-18T01:34:29Z
ethz.source
SCOPUS
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2024-02-03T05:29:38Z
ethz.rosetta.lastUpdated
2024-02-03T05:29:38Z
ethz.rosetta.exportRequired
true
ethz.rosetta.versionExported
true
ethz.COinS
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