Document Detail


Normal and scrapie-associated forms of prion protein differ in their sensitivities to phospholipase and proteases in intact neuroblastoma cells.
MedLine Citation:
PMID:  1968104     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Previous studies have indicated that scrapie infection results in the accumulation of a proteinase K-resistant form of an endogenous brain protein generally referred to as prion protein (PrP). The molecular nature of the scrapie-associated modification of PrP accounting for proteinase K resistance is not known. As an approach to understanding the cellular events associated with the PrP modification in brain tissue, we sought to identify proteinase K-resistant PrP (PrP-res) in scrapie-infected neuroblastoma cells in vitro and to compare properties of PrP-res with those of its normal proteinase K-sensitive homolog, PrP-sen. PrP-res was detected by immunoblot in scrapie-infected but not uninfected neuroblastoma clones. Densitometry of immunoblots indicated that there was two- to threefold more PrP-res than PrP-sen in one infected clone. Metabolic labeling and membrane immunofluorescence experiments indicated that PrP-sen was located on the cell surface and could be removed from intact cells by phosphatidylinositol-specific phospholipase C and proteases. In contrast, PrP-res was not removed after reaction with these enzymes. Thus, either the scrapie-associated PrP-res was not on the cell surface or it was there in a form that is resistant to these hydrolytic enzymes. Attempts to detect intracellular PrP-res by immunofluorescent staining of fixed and permeabilized cells revealed that PrP was present in discrete perinuclear Golgi-like structures. However, the staining pattern was similar in both scrapie-infected and uninfected clones, and thus the intracellular staining may have represented only PrP-sen. Analysis of scrapie infectivity in cells treated with extracellular phospholipase, proteinase K, and trypsin indicated that, like PrP-res, the scrapie agent was not removed from the infected cells by any of these enzymes.
Authors:
B Caughey; K Neary; R Buller; D Ernst; L L Perry; B Chesebro; R E Race
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Journal of virology     Volume:  64     ISSN:  0022-538X     ISO Abbreviation:  J. Virol.     Publication Date:  1990 Mar 
Date Detail:
Created Date:  1990-03-26     Completed Date:  1990-03-26     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  0113724     Medline TA:  J Virol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1093-101     Citation Subset:  IM    
Affiliation:
Laboratory of Persistent Viral Diseases, National Institute of Allergy and Infectious Diseases, Hamilton, Montana 59840.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cell Line
Endopeptidase K
Flow Cytometry
Fluorescent Antibody Technique
Immunoblotting
Neuroblastoma
PrPSc Proteins
Prions / metabolism*
Serine Endopeptidases / metabolism*
Trypsin / metabolism*
Type C Phospholipases / metabolism*
Viral Proteins / analysis,  metabolism*
Chemical
Reg. No./Substance:
0/PrPSc Proteins; 0/Prions; 0/Viral Proteins; EC 3.1.4.-/Type C Phospholipases; EC 3.4.21.-/Serine Endopeptidases; EC 3.4.21.4/Trypsin; EC 3.4.21.64/Endopeptidase K
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