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The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive.

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Caughey, B., Raymond, G.J.·1991·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(18)55257-1
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Abstract

A common feature of scrapie and related transmissible spongiform encephalopathies is the accumulation of an abnormal protease-resistant form of PrP which may be the major component of the infectious agent. While it is known that both the normal (protease-sensitive) PrP and protease-resistant PrP are encoded by the same endogenous gene, the nature of the disease-associated modification of PrP is not understood. To study the cellular events leading to the formation of protease-resistant PrP, we have compared its biosynthesis to that of its normal isoform in scrapie-infected mouse neuroblastoma cells. In pulse-chase labeling experiments, the protease-resistant PrP was synthesized and degraded much more slowly than the normal PrP, suggesting that protease-resistant PrP is made from a protease-sensitive precursor. More significantly, we found that the precursor of protease-resistant PrP was eliminated from intact cells by treatments with phosphatidylinositol-specific phospholipase C and trypsin. This demonstrated that, unlike the protease-resistant PrP itself, the precursor is phospholipase- and protease-sensitive and at least transiently found on the cell surface. By these criteria, the precursor of protease-resistant PrP is indistinguishable from the normal PrP isoform. These results indicate that the conversion of PrP to the protease- and phospholipase-resistant state is a post-translational event that occurs after the precursor reaches the cell surface.

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Metadata

Authors
Caughey, B., & Raymond, G. J.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1991-09
Volume
266
Issue
27
Pages
18217-18223
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(18)55257-1
OpenAlex
W1601881612
Cited by
637
References
1
FWCI
7.10
Type
journal article
Language
en
Open access
hybrid
Licence

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CoChat. (2026). Citation check: The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive. https://app.cochat.ai/papers/10.1016/s0021-9258(18)55257-1
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Caughey, B., & Raymond, G. J. (1991). The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)55257-1

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