Document Detail


Observing fibrillar assemblies on scrapie-infected cells.
MedLine Citation:
PMID:  18175144     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The infectious agent in prion diseases is an aberrant-folded isoform of the cellular prion protein (PrPC). This scrapie-related prion protein (PrPSc) has an increased beta-sheet content, is detergent insoluble and proteinase K resistant, and accumulates in prion-infected organisms and cells. In vitro, PrPSc self-aggregates into amyloid fibrils. However, there is no direct experimental proof for the occurrence of PrPSc-containing fibrils in vivo or in cell cultures. Applying atomic force microscopy (AFM) to scrapie-infected mouse neuroblastoma (ScN2a) cells, we discovered growing patch-like assemblies of amyloid-like fibrillar structures on the cell surfaces. Immunofluorescence and AFM images showed heterogeneous accumulation and aggregation of PrPSc in ScN2a cell cultures. The percentage of cells having characteristic fibrils on their surface increased with time after scrapie infection. These endogeneous fibrils had lengths from 0.5 to 3 microm and protruded from the cell surface by 108 +/- 30 nm, and thus resembled the heterogeneous shapes and networks of in vitro prepared amyloid fibrils.
Authors:
Susanne Wegmann; Margit Miesbauer; Konstanze F Winklhofer; Jörg Tatzelt; Daniel J Muller
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-01-03
Journal Detail:
Title:  Pflügers Archiv : European journal of physiology     Volume:  456     ISSN:  0031-6768     ISO Abbreviation:  Pflugers Arch.     Publication Date:  2008 Apr 
Date Detail:
Created Date:  2008-03-21     Completed Date:  2008-07-22     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0154720     Medline TA:  Pflugers Arch     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  83-93     Citation Subset:  IM    
Affiliation:
Center of Biotechnology, University of Technology, Dresden, Germany.
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MeSH Terms
Descriptor/Qualifier:
Amyloid / ultrastructure*
Animals
Brain Neoplasms / metabolism,  pathology
Cell Line
Cell Line, Tumor
Mice
Microscopy, Atomic Force
Neuroblastoma / metabolism,  pathology
PrP 27-30 Protein / chemistry,  metabolism
Prions / chemistry,  metabolism,  ultrastructure*
Protein Folding
Scrapie / pathology*
Chemical
Reg. No./Substance:
0/Amyloid; 0/Prions; 105268-27-7/PrP 27-30 Protein

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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