An optimized Western blot assay provides a comprehensive assessment of the physiological endoproteolytic processing of the prion protein.

ABSTRACT: The prion protein (PrP^C) is subjected to several conserved endoproteolytic events producing bioactive fragments that are of increasing interest for their physiological functions and their implication in the pathogenesis of prion diseases and other neurodegenerative diseases. However, systematic and comprehensive investigations on the full spectrum of PrP^C proteoforms have been hampered by the lack of methods able to identify all PrP^C-derived proteoforms. Building on previous knowledge of PrP^C endoproteolytic processing, we thus developed an optimized Western blot assay able to obtain the maximum information about PrP^C constitutive processing and the relative abundance of PrP^C proteoforms in a complex biological sample. This

SUBMITTER: Vanni I 

PROVIDER: S-EPMC9867980 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature