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N-terminal acetylation for identification of cleavage sites on immunoprecipitated PrP

ABSTRACT: In-gel N-terminal acetylation of immunoprecipitated prion protein for identification of cleavage sites. Mouse expressing either WT or mutant (S3) form of PrP were used in this study. Three replicates from single brains were included in this experiment.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Mus Musculus (ncbitaxon:10090)

SUBMITTER: Olivier Julien

PROVIDER: MSV000092543 | MassIVE | Thu Jul 27 13:06:00 BST 2023

REPOSITORIES: MassIVE

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Publications

Application of N-Terminal Labeling Methods Provide Novel Insights into Endoproteolysis of the Prion Protein in Vivo.

Gomez-Cardona Erik E Eskandari-Sedighi Ghazaleh G Fahlman Richard R Westaway David D Julien Olivier O

ACS chemical neuroscience 20231214 1

Alternative α- and β-cleavage events in the cellular prion protein (PrPC) central region generate fragments with distinct biochemical features that affect prion disease pathogenesis, but the assignment of precise cleavage positions has proven challenging. Exploiting mouse transgenic models expressing wild-type (WT) PrPC and an octarepeat region mutant allele (S3) with increased β-fragmentation, cleavage sites were defined using LC-MS/MS in conjunction with N-terminal enzyma ...[more]

PMID: 38095594

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