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Evidence for a secretory form of the cellular prion protein

Hay, Bruce and Prusiner, Stanley B. and Lingappa, Vishwanath R. (1987) Evidence for a secretory form of the cellular prion protein. Biochemistry, 26 (25). pp. 8110-8115. ISSN 0006-2960. https://resolver.caltech.edu/CaltechAUTHORS:20200505-123221748

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Abstract

The biogenesis of hamster brain prion protein (PrP) has been studied by expression of RNA transcribed from a full-length PrP cDNA in Xenopus oocytes and cell-free systems. Earlier studies in the wheat germ cell-free system showed that one form of PrP is a transmembrane protein that spans the bilayer at least twice [Hay, B., Barry, R. A., Lieberburg, I., Prusiner, S. B., & Lingappa, V. R. (1987) Mol. Cell. Biol. 7, 914-920]. We now report that PrP can also exist as a secreted protein. SP6 PrP RNA microinjected into Xenopus oocytes produced two forms of PrP: one that remained in the cell and another that was secreted into the medium. Cell-free translation studies in rabbit reticulocyte lysates supplemented with microsomal membranes gave similar results: while one form of PrP was found as an integral membrane protein spanning the membrane at least twice, another form of PrP was found to be completely translocated to the microsomal membrane vesicle lumen. Both the membrane and secretory forms of PrP appear to be generated from the same pool of nascent chains. The mechanism governing the alternative fates of nascent PrP remains to be elucidated but may have significance for understanding the pathogenesis of scrapie and other prion diseases.


Item Type:Article
Related URLs:
URLURL TypeDescription
https://doi.org/10.1021/bi00399a014DOIArticle
Additional Information:© 1987 American Chemical Society. Received June 2, 1987; Revised Manuscript Received August 11, 1987. This work was supported by research grants from the National Institutes of Health (AG02132 and NS14069) and by a grant from the Senator Jacob Javits Center of Excellence in Neuroscience (NS22786) as well as by gifts from RJR-Nabisco, Inc., and the Sherman Fairchild Foundation.
Funders:
Funding AgencyGrant Number
NIHAG02132
NIHNS14069
NIHNS22786
RJR-NabiscoUNSPECIFIED
Sherman Fairchild FoundationUNSPECIFIED
Issue or Number:25
Record Number:CaltechAUTHORS:20200505-123221748
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20200505-123221748
Official Citation:Evidence for a secretory form of the cellular prion protein. Bruce Hay, Stanley B. Prusiner, and Vishwanath R. Lingappa. Biochemistry 1987 26 (25), 8110-8115; DOI: 10.1021/bi00399a014
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:103002
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:05 May 2020 19:51
Last Modified:05 May 2020 19:51

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