Investigating the Role of the Prion Protein Polybasic Domain in PrPSc Formation and Neuroprotection
Abstract
Prion diseases are characterized by the conformational conversion of the cellular prion protein (PrPC ) into the misfolded PrPSc isoform. However, both the normal, physiological function of PrPC and the mechanism of its conversion into PrPSc remain undefined. Several lines of evidence suggest that the expression of PrP can be neuroprotective, including its ability to abrogate the neurotoxic activity of PrP deletion mutants. In my thesis work, I characterized the role of the polybasic domain (residues 23-31) in the neuroprotective effect of WT PrP and examined the role of these residues in the formation of the infectious PrPSc protein.
Committee Chair
David Harris
Committee Members
Heather L. True-Krob, Kendall Blumer, David Holtzman, Jin-Moo Lee, Mark Sands
Degree
Doctor of Philosophy (PhD)
Author's Department
Biology & Biomedical Sciences (Molecular Cell Biology)
Document Type
Dissertation
Date of Award
Summer 8-15-2011
Language
English (en)
DOI
https://doi.org/10.7936/K7639MPZ
Recommended Citation
Turnbaugh, Jessie Aleksandra, "Investigating the Role of the Prion Protein Polybasic Domain in PrPSc Formation and Neuroprotection" (2011). Arts & Sciences Theses and Dissertations. 105.
The definitive version is available at https://doi.org/10.7936/K7639MPZ
Comments
Permanent URL: https://doi.org/10.7936/K7639MPZ