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Up-regulation of cathepsin B and cathepsin L activities in scrapie-infected mouse Neuro2a cells

Alexander Bürkle^1,2,

¹ Department of Gerontology, Institute for Ageing and Health, University of Newcastle upon Tyne, Newcastle upon Tyne, UK
² Abteilung Tumorvirologie, Deutsches Krebsforschungszentrum, Heidelberg, Germany
³ Arbeitsgruppe Biomedizinische Strukturforschung, Deutsches Krebsforschungszentrum, Heidelberg, Germany
⁴ Institute for Novel and Emerging Infectious Diseases, Federal Research Centre for Virus Diseases, Insel Riems, Germany

Correspondence
Alexander Bürkle
Alexander.Buerkle{at}uni-konstanz.de

Prion diseases are characterized by the accumulation of an abnormal, proteinase K-resistant isoform of the prion protein, PrP^Sc, which is generated by a post-translational conversion of the protease-sensitive normal cell-surface glycoprotein PrP^c involving major conformational changes. The conversion is thought to occur at the plasma membrane or along the endocytic pathway towards the lysosome. PrP^Sc aggregates have been found to accumulate in secondary lysosomes. In our study, the activities of two major lysosomal cysteine proteases, cathepsins B and L, were found to be significantly increased in scrapie-infected Neuro2a cells compared with uninfected cells using biochemical and cytochemical methods. We hypothesize that lysosomal proteases may be involved in a ‘second autocatalytic loop’ of PrP^Sc formation, acting in concert with the well-known autocatalytic enhancement of PrP conversion in the presence of PrP^Sc.

Present address: Lehrstuhl Molekulare Toxikologie, Universität Konstanz, Fach X911, D-78457 Konstanz, Germany.

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