Cathepsin B and L are involved in degradation of prions in GT1-1 neuronal cells

Neuroreport
Katarina M LuhrKrister Kristensson

Abstract

In scrapie-infected cells, the abnormal isoform of the prion protein, PrP(Sc), accumulates in endosomes/lysosomes. In this study, the involvement of two lysosomal proteases, cathepsin B and L, in cellular processing of PrP(Sc) was analyzed in immortalized neuronal gonadotropin-releasing hormone cells (GT1-1) infected with scrapie. Treatment with inhibitors of either cathepsin B or L resulted in accumulation of PrP(Sc). Such an increased accumulation also occurred when the activities of both cathepsins were inhibited using RNA interference. We conclude that cathepsin B and L are involved in the degradation of PrP(Sc) in scrapie-infected GT1-1 cells and that they can compensate for each other's functions. This study shows that specific proteases, abundantly present in neurons, have the capacity to degrade PrP(Sc).

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Citations

Oct 14, 2009·Cellular and Molecular Life Sciences : CMLS·Sabine GilchHermann M Schätzl
Mar 27, 2012·The Journal of Biological Chemistry·Jingjing LiangQingzhong Kong
Jul 15, 2015·Proceedings of the National Academy of Sciences of the United States of America·Ryan P McGlinchey, Jennifer C Lee
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Apr 3, 2020·Cellular and Molecular Neurobiology·Marco ZattoniGiuseppe Legname
Sep 15, 2005·The Journal of Biological Chemistry·Mark KristiansenSarah J Tabrizi

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