Characterization and chemoproteomic profiling of protein O-GlcNAcylation in SOD1-G93A mouse model.

ABSTRACT:

Background

Amyotrophic lateral sclerosis (ALS) is a devastating motor neuron disease. Protein O-linked β-N-acetylglucosamine (O-GlcNAc) modification has been found to affect the processing of several important proteins implicated in ALS. However, the overall level and cellular localization of O-GlcNAc during ALS progression are incompletely understood, and large-scale profiling of O-GlcNAcylation sites in this context remains unexplored.

Methods

By using immunostaining analysis and chemoenzymatic labeling-based quantitative chemoproteomics, we assayed O-GlcNAcylation dynamics of lumbar spinal cords from SOD-G93A mice and their non-transgenic (NTG) littermates, the most widely used animal model for studying ALS pathogenesis.

Results

We discovered that the global O-GlcN

SUBMITTER: Hao Y 

PROVIDER: S-EPMC11871760 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature