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Titel
Peroxiredoxin 6 promotes upregulation of the prion protein (PrP) in neuronal cells of prion-infected mice
VerfasserWagner, Wibke In der Gemeinsamen Normdatei der DNB nachschlagen ; Reuter, Andreas ; Hüller, Petra ; Löwer, Johannes ; Weßler, Silja In der Gemeinsamen Normdatei der DNB nachschlagen
Erschienen in
Cell Communication and Signaling, London, 2012, Jg. 10, H. 38, S. 1-6
ErschienenBioMed Central, 2012
SpracheEnglisch
DokumenttypAufsatz in einer Zeitschrift
Schlagwörter (EN)Peroxiredoxin 6 / Prion Protein / Scrapie
ISSN1478-811X
URNurn:nbn:at:at-ubs:3-346 Persistent Identifier (URN)
DOI10.1186/1478-811X-10-38. 
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Peroxiredoxin 6 promotes upregulation of the prion protein (PrP) in neuronal cells of prion-infected mice [0.78 mb]
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Background: It has been widely established that the conversion of the cellular prion protein (PrPC) into its abnormal isoform (PrPSc) is responsible for the development of transmissible spongiform encephalopathies (TSEs). However, the knowledge of the detailed molecular mechanisms and direct functional consequences within the cell is rare. In this study, we aimed at the identification of deregulated proteins which might be involved in prion pathogenesis. Findings: Apolipoprotein E and peroxiredoxin 6 (PRDX6) were identified as upregulated proteins in brains of scrapie-infected mice and cultured neuronal cell lines. Downregulation of PrP gene expression using specific siRNA did not result in a decrease of PRDX6 amounts. Interestingly, selective siRNA targeting PRDX6 or overexpression of PRDX6 controlled PrPC and PrPSc protein amounts in neuronal cells. Conclusions: Besides its possible function as a novel marker protein in the diagnosis of TSEs, PDRX6 represents an attractive target molecule in putative pharmacological intervention strategies in the future.