Methods for studying prion protein (PrP) metabolism and the formation of protease-resistant PrP in cell culture and cell-free systems. An update.

Abstract

Transmissible spongiform encephalopathies (TSE) or prion diseases result in aberrant metabolism of prion protein (PrP) and the accumulation of a protease-resistant, insoluble, and possibly infectious form of PrP, PrP-res. Studies of PrP biosynthesis, intracellular trafficking, and degradation has been studied in a variety of tissue culture cells. Pulse-chase metabolic labeling studies in scrapie-infected cells indicated that PrP-res is made posttranslationally from an apparently normal protease-sensitive precursor, PrP-sen, after the latter reaches the cell surface. Cell-free reactions have provided evidence that PrP-res itself can induce the conversion of PrP-sen to PrP-res in a highly species- and strain-specific manner. These studies have shed light on the mechanism of PrP-res formation and suggest molecular bases for TSE species barrier effects and agent strain propagation.

• Authors: B Caughey, G J Raymond, S A Priola, D A Kocisko, R E Race, R A Bessen, P T Lansbury Jr, B Chesebro
• Journal: Molecular biotechnology (Mol Biotechnol) Vol. 13 Issue 1 Pg. 45-55 (Nov 1999) ISSN: 1073-6085 [Print] United States
• PMID: 10934521 (Publication Type: Journal Article)

Chemical References

• Prions
• Endopeptidases

Topics

• Animals
• Cell Culture Techniques (methods)
• Cell-Free System
• Endopeptidases (metabolism)
• Humans
• Methods
• Prions (analysis, metabolism)