NR APAW
AU Zhang,Y.; Spiess,E.; Groschup,M.H.; Bürkle,A.
TI Upregulation of Cathepsin B and Cathepsin L Activities in Scrapie-Infected Mouse Neuro2a Cells
QU International Conference - Prion diseases: from basic research to intervention concepts - TSE-Forum, 08.10.-10.10.2003, Gasteig, München - Poster session - BR-51
PT Konferenz-Poster
AB Prion diseases are characterised by the accumulation of an abnormal, proteinase K-resistant isoform of the prion protein, PrPsc, which is generated by posttranslational conversion of the protease-sensitive normal cell-surface glycoprotein PrPc involving major conformational changes. The conversion is thought to occur at the plasma membrane or along the endocytic pathway towards the lysosome. PrPsc aggregates have been found to accumulate in secondary lysosomes. In our study, activities of two major lysosomal cysteine proteases, cathepsins B and L, were found significantly increased in scrapie-infected Neuro2a cells compared with uninfected cells using biochemical and cytochemical methods. We hypothesise that lysosomal proteases may be involved in a 'second autocatalytic loop' of PrPsc formation, acting in concert with the well-known autocatalytic enhancement of PrP conversion by the presence of PrPsc.
AD Yonghua Zhang, Alexander Bürkle, University of Newcastle, Newcastle upon Tyne, UK; Yonghua Zhang,Eberhard Spiess, Alexander Bürkle, Deutsches Krebsforschungszentrum, Heidelberg, Germany; Martin H. Groschup, Federal Research Centre for Virus Diseases, Insel Riems, Germany; Alexander Bürkle, Universität Konstanz, Konstanz, Germany
SP englisch
PO Deutschland