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Peroxiredoxin 6 promotes upregulation of the prion protein (PrP) in neuronal cells of prion-infected mice

Wibke Wagner13, Andreas Reuter1, Petra Hüller14, Johannes Löwer1 and Silja Wessler2*

Author Affiliations

1 Paul Ehrlich Institute, Paul Ehrlich-Straße 51-59, Langen, D-63225, Germany

2 Division of Microbiology, University of Salzburg, Billrothstrasse 11, Salzburg, A-5020, Austria

3 Present address: Department of Biology, Division of Neurosensory systems, Technical University of Darmstadt, Schnittspahnstraße 10, Darmstadt, D-64287, Germany

4 Present address: Chiltern International GmbH, Norsk-Data-Strasse 1, Bad Homburg v.d.H, D-61352, Germany

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Cell Communication and Signaling 2012, 10:38  doi:10.1186/1478-811X-10-38

Published: 4 December 2012



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.


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.


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.

Peroxiredoxin 6; Prion protein; Scrapie