Methods for studying prion protein (PrP) metabolism and the formation of protease-resistant PrP in cell culture and cell-free systems |
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Authors: | Byron Caughey Gregory J Raymond Suzette A Priola David A Kocisko Richard E Race Richard A Bessen Peter T Lansbury Jr Bruce Chesebro |
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Institution: | (1) NIH Rocky Mountain Laboratories, 903 S. 4th St., 59840 Hamilton, MT |
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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. |
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Keywords: | Prion protein PrP scrapie transmissible spongiform encephalopathy |
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