NR ACJM
AU Caughey,B.W.; Raymond,G.J.; Priola,S.A.; Kocisko,D.A.; Race,R.E.; Bessen,R.A.; Lansbury,P.T.Jr.; Chesebro,B.
TI Methods for studying prion protein (PrP) metabolism and the formation of protease-resistant PrP in cell culture and cell-free systems. An update.
QU Molecular Biotechnology 1999 Nov; 13(1): 45-55
PT journal article
AB 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, PrPres. 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 PrPres 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 PrPres itself can induce the conversion of PrP-sen to PrPres in a highly species- and strain-specific manner. These studies have shed light on the mechanism of PrPres formation and suggest molecular bases for TSE species barrier effects and agent strain propagation.
MH Animal; Cell Culture/methods; Cell-Free System; Endopeptidases/metabolism; Human; Methods; Prions/*analysis/metabolism
AD NIH Rocky Mountain Laboratories, Hamilton, MT 59840, USA. byron_caughey@nih.gov
SP englisch
PO USA