Abstract

Young Researchers' Sessions

Day 1, June 10（Mon.）　15:30-15:45　Room B (Convention Hall 200)

Glycosylation is involved in various biological processes and diseases. Recently, O-GlcNAcylation was suggested to be associated with Parkinson's disease (PD). However, t the role of O-GlcNAc in PD remains unclear due to the limited quantity of O-GlcNAcylated proteins and the difficulty of comprehensive and quantitative analysis without an enrichment process. Data-independent acquisition LC/MS/MS (DIA-MS) has garnered attention as a quantitative proteomic method for post-translational modification. The challenge in O-GlcNAc proteomics is to obtain human O-GlcNAcylated peptides and construct a spectral library. In this study, we aimed to identify PD-related O-GlcNAcylated proteins in PD model cells using DIA-MS. A library was constructed using iPSC-derived O-GlcNAcylated proteins, and O-GlcNAc proteomics was performed on PD model cells generated through genome editing of iPSC. First, O-GlcNAcylated proteins were enriched from iPSC using wheat germ agglutinin and its trypsin digests were analyzed by data-dependent acquisition LC/MS/MS. Forty-three O-GlycNAcylated peptides were identified and listed in a library using Skyline analysis software. Next, trypsin digests in the PD model cells and WT cells were analyzed by DIA-MS. Several O-GlcNAcylated proteins were higher in PD model neural progenitor cells (NPCs) than in WT-NPCs but lower in PD model Neurons (NCs) than in WT-NCs.

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