Global Profiling of Lactylation Proteomics and Specific Lactylated Site Validation in Rheumatoid Arthritis Patients.

• Tác giả: Jie Gao, Ying Gao, Jiaqi Hu, Zhengyi Jin, Ruina Kong, Qilong Liu, Yiyi Yu, Dongbao Zhao
• Ngôn ngữ: eng
• Ký hiệu phân loại: 373.236 Lower level
• Thông tin xuất bản: United States : Journal of proteome research , 2025
• Bộ sưu tập: NCBI
• ID: 726225

Tóm tắt

 Protein lactylation is a novel post-translational modification that has rarely been investigated in rheumatoid arthritis (RA). This study aimed to explore lactylation proteomics in RA patients and validate sorted candidate lactylation sites. Synovial tissues from ten RA and six osteoarthritis (OA) patients were subjected to lactylation proteomics via affinity enrichment and LC-MS/MS. Four candidate lactylated modification sites were validated by immunoprecipitation. Totally, 566 sites and 250 proteins with lactylated modifications in RA patients and 548 sites and 220 proteins with lactylated modifications in OA patients were identified. By comparison, 24 upregulated but 2 downregulated lactylated modification sites and 18 upregulated but 1 downregulated lactylated modification protein were discovered in RA patients versus OA patients. The dysregulated lactylated proteins were mainly enriched in biological processes such as positive regulation of plasma membrane repair by GO analysis
  pathways such as neutrophil extracellular trap formation by KEGG analysis
  and two metabolism-related items by COG/KOG analysis. Immunoprecipitation confirmed that FTH1-K69la (