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  • Sackmann, Christopher,1988-Linköpings universitet,Avdelningen för neurobiologi,Medicinska fakulteten,Region Östergötland, Klinisk patologi (author)

Oligomeric amyloid-beta induces early and widespread changes to the proteome in human iPSC-derived neurons

  • Article/chapterEnglish2020

Publisher, publication year, extent ...

  • 2020-04-16
  • Nature Publishing Group,2020
  • electronicrdacarrier

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  • LIBRIS-ID:oai:DiVA.org:liu-169266
  • https://urn.kb.se/resolve?urn=urn:nbn:se:liu:diva-169266URI
  • https://doi.org/10.1038/s41598-020-63398-6DOI

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  • Language:English
  • Summary in:English

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  • Subject category:ref swepub-contenttype
  • Subject category:art swepub-publicationtype

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  • Funding Agencies|Swedish Research CouncilSwedish Research Council [MH: 523-2013-2735]; Swedish Alzheimer foundation; Swedish Brain Foundation; Hans-Gabriel and Alice Trolle-Wachtmeister Foundation for Medical Research; Konung Gustaf V:s och Drottning Victorias Frimurarestiftelse; Swedish Dementia Foundation; Linkoping University
  • Alzheimer’s disease (AD) is the most common form of dementia globally and is characterized by aberrant accumulations of amyloid-beta (Aβ) and tau proteins. Oligomeric forms of these proteins are believed to be most relevant to disease progression, with oligomeric amyloid-β (oAβ) particularly implicated in AD. oAβ pathology spreads among interconnected brain regions, but how oAβ induces pathology in these previously unaffected neurons requires further study. Here, we use well characterized iPSC-derived human neurons to study the early changes to the proteome and phosphoproteome after 24 h exposure to oAβ 1-42. Using nLC-MS/MS and label-free quantification, we identified several proteins that are differentially regulated in response to acute oAβ challenge. At this early timepoint, oAβ induced the decrease of TDP-43, heterogeneous nuclear ribonucleoproteins (hnRNPs), and coatomer complex I (COPI) proteins. Conversely, increases were observed in 20 S proteasome subunits and vesicle associated proteins VAMP1/2, as well as the differential phosphorylation of tau at serine 208. These changes show that there are widespread alterations to the neuronal proteome within 24 h of oAβ uptake, including proteins previously not shown to be related to neurodegeneration. This study provides new targets for the further study of early mediators of AD pathogenesis.

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  • Hallbeck, Martin,1970-Linköpings universitet,Avdelningen för neurobiologi,Medicinska fakulteten,Region Östergötland, Klinisk patologi(Swepub:liu)marha90 (author)
  • Linköpings universitetAvdelningen för neurobiologi (creator_code:org_t)

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  • In:Scientific Reports: Nature Publishing Group10:12045-2322

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