English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Stress-protective signalling of prion protein is corrupted by scrapie prions

Rambold, A., Müller, V., Ron, U., Ben-Tal, N., Winklhofer, K. F., & Tatzelt, J. (2008). Stress-protective signalling of prion protein is corrupted by scrapie prions. EMBO Journal, 27, 1974-1984. doi:10.1038/emboj.2008.122.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/21.11116/0000-0007-8BDE-3 Version Permalink: http://hdl.handle.net/21.11116/0000-0007-8BDF-2
Genre: Journal Article

Files

show Files
hide Files
:
Rambold et al. 2008.pdf (Publisher version), 472KB
Name:
Rambold et al. 2008.pdf
Description:
-
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show
hide
Description:
-

Creators

show
hide
 Creators:
Rambold, Angelika1, Author              
Müller, Veronika2, Author
Ron, Uri2, Author
Ben-Tal, Nir2, Author
Winklhofer, Konstanze F2, Author
Tatzelt, Jörg2, Author
Affiliations:
1Department of Developmental Immunobiology, Max Planck Institute of Immunobiology and Epigenetics, Max Planck Society, ou_2243650              
2External Organizations, ou_persistent22              

Content

show
hide
Free keywords: -
 Abstract: Studies in transgenic mice revealed that neurodegeneration induced by scrapie prion (PrPSc) propagation is dependent on neuronal expression of the cellular prion protein PrPC. On the other hand, there is evidence that PrPC itself has a stress‐protective activity. Here, we show that the toxic activity of PrPSc and the protective activity of PrPC are interconnected. With a novel co‐cultivation assay, we demonstrate that PrPSc can induce apoptotic signalling in PrPC‐expressing cells. However, cells expressing PrP mutants with an impaired stress‐protective activity were resistant to PrPSc‐induced toxicity. We also show that the internal hydrophobic domain promotes dimer formation of PrP and that dimerization of PrP is linked to its stress‐protective activity. PrP mutants defective in dimer formation did not confer enhanced stress tolerance. Moreover, in chronically scrapie‐infected neuroblastoma cells the amount of PrPC dimers inversely correlated with the amount of PrPSc and the resistance of the cells to various stress conditions. Our results provide new insight into the mechanism of PrPC‐mediated neuroprotection and indicate that pathological PrP conformers abuse PrPC‐dependent pathways for apoptotic signalling.

Details

show
hide
Language(s): eng - English
 Dates: 2008-07-23
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/emboj.2008.122
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: EMBO Journal
  Other : EMBO J.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Nature Publishing Group
Pages: - Volume / Issue: 27 Sequence Number: - Start / End Page: 1974 - 1984 Identifier: ISSN: 0261-4189
CoNE: https://pure.mpg.de/cone/journals/resource/954925497061