Abstract
Like numerous proteins of various structural and functional classes, the glycosylphosphatidylinositol (GPI)-anchored cellular prion protein (PrPC) has been recognized to undergo endoproteolytic processing for decades, a phenomenon observed in various cultured cell lines, as well as human and several animal tissue extracts. Despite this, the physiological significance of PrPC proteolytic cleavage has not yet been entirely elucidated. Experimental evidence suggests independent normal biological functions of the full-length and truncated PrPC species, as well as probable links of endoproteolysis to prion disease transmission susceptibility, pathogenesis, and toxicity. The accurate characterization of constitutive PrPC processing, through the method outlined in this chapter, is therefore an important tool in order to investigate the biological relevance of the alternative cleavage events.
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Acknowledgments
The author thanks Associate Professor Victoria Lawson for the 03R19 and 03R22 polyclonal antibodies, as well as the original RK13 cell line. This work was supported by an Australian Government National Health and Medical Research Council (NHMRC) program grant (#628946) and Training Fellowship (#567123) and a University of Melbourne Early Career Researcher Fellowship.
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Lewis, V. (2017). Analysis of Cellular Prion Protein Endoproteolytic Processing. In: Lawson, V. (eds) Prions. Methods in Molecular Biology, vol 1658. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-7244-9_10
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DOI: https://doi.org/10.1007/978-1-4939-7244-9_10
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