若手研究者セッション
第1日 6月10日（月） 15:30～15:45 B会場（中ホール200）
- 1B-O1-1530（1P-30）
DIA-MSによるパーキンソン病特異的変動を示すO-GlcNAc修飾タンパク質の網羅的定量解析
(横市大院生命医)
o保科隼佑・ 芳﨑雅人・ 高倉大輔・ 菅原亨・ 川崎ナナ
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.