The effects of lysosomal and proteasomal inhibitors on abnormal forms of prion protein degradation in murine macrophages
Article first published online: 23 NOV 2010
© 2010 The Societies and Blackwell Publishing Asia Pty Ltd
Microbiology and Immunology
Volume 54, Issue 12, pages 763–768, December 2010
How to Cite
Sassa, Y., Yamasaki, T., Horiuchi, M., Inoshima, Y. and Ishiguro, N. (2010), The effects of lysosomal and proteasomal inhibitors on abnormal forms of prion protein degradation in murine macrophages. Microbiology and Immunology, 54: 763–768. doi: 10.1111/j.1348-0421.2010.00272.x
- Issue published online: 23 NOV 2010
- Article first published online: 23 NOV 2010
- Accepted manuscript online: 27 SEP 2010 04:57PM EST
- Received 13 May 2010; revised 23 August 2010; accepted 5 September 2010.
It has been reported that macrophages degrade infectious forms of prion protein (PrPSc). In order to investigate the mechanisms underlying PrPSc degradation in macrophages, the effects of lysosomal and proteasomal inhibitors on macrophage cell lines which were incubated with scrapie-affected brain homogenate were studied. PrPSc degradation was inhibited in the presence of both proteasomal and lysosomal inhibitors. Indirect fluorescence assays to determine the cellular localization of PrPSc were undertaken. PrPSc colocalized with the lysosomal membrane protein Lamp-1 and ubiquitin, a protein that is related to the proteasome. The present data indicate that macrophages might degrade PrPSc via the lysosomal and proteasomal pathways.