NR AATJ
AU Arnold,J.E.; Tipler,C.; Laszlo,L.; Hope,J.; Landon,M.; Mayer,R.J.
TI The abnormal isoform of the prion protein accumulates in late-endosome-like organelles in scrapie-infected mouse brain
QU Journal of Pathology 1995 Aug; 176(4): 403-11
PT journal article
AB The prion encephalopathies are characterized by accumulation in the brain of the abnormal form PrPsc of a normal host gene product PrPc. The mechanism and site of formation of PrPsc from PrPc are currently unknown. In this study, ME7 scrapie-infected mouse brain was used to show, both biochemically and by double-labelled immunogold electron microscopy, that proteinase K-resistant PrPsc is enriched in subcellular structures which contain the cation-independent mannose 6-phosphate receptor, ubiquitin-protein conjugates, beta-glucuronidase, and cathepsin B, termed late endosome-like organelles. The glycosylinositol phospholipid membrane-anchored PrPc will enter such compartment for normal degradation and the organelles may therefore act as chambers for the conversion of PrPc into infectious PrPsc in this murine model of scrapie.
ZR 43 Zitate
IN In den Gehirnzellen Scrapie-infizierter ME7-Mäuse wurde eine Anreicherung der proteaseresistenten Form des Prionproteins in späten endosomenähnlichen Organellen festgestellt, in denen die normalen zellulären Prionproteine abgebaut werden.
MH Animal; Blotting, Western; Brain/*metabolism/ultrastructure; Endosomes/*metabolism; Mice; Mice, Inbred C57BL; Microscopy, Electron; Prions/chemistry/*metabolism; Scrapie/*metabolism/pathology; Support, Non-U.S. Gov't
AD Jane E. Arnold, Carron Tipler, Michael Landon, Professor R. John Mayer, Department of Biochemistry, University of Nottingham Medical School, Queen's Medical Centre, Nottingham NG7 2UH, U.K.; Lajos Laszlo, Department of General Zoology, Eotvos University, H-1088, Budapest, Hungary; James Hope, AFRC/MRC Neuropathogenesis Unit, Ogston Building, West Mains Road, Edinburgh EH9 3JF, U.K.
SP englisch
PO England