Abstract: TH-PO0334
Serum Label-Free Quantitative Acetylated Proteomic Analysis in Patients with Idiopathic Membranous Nephropathy
Session Information
- Glomerular Diseases: Omics
October 22, 2026 | Location: Exhibit Hall A, Convention Center
Abstract Time: 10:00 AM - 12:00 PM
Category: Glomerular Diseases
- 1401 Glomerular Diseases: Mechanisms, including Podocyte Biology
Authors
- Ke, Yixi, Southern University of Science and Technology School of Medicine, Shenzhen, Guangdong, China
- Ma, Hualin, Shenzhen People's Hospital Department of Nephrology, Shenzhen, Guangdong, China
Background
Idiopathic membranous nephropathy (IMN) is a common autoimmune glomerular disease. Lysine acetylation is a key post-translational modification, yet its systemic acetylation changes in IMN remain unknown.
Methods
Serum from 12 treatment-naïve IMN patients and 10 healthy controls was pooled. After acetylated peptide enrichment, liquid chromatography–tandem mass spectrometry (LC–MS/MS) was performed. Data were analyzed with MaxQuant, and differentially acetylated sites (fold change >1.5, P < 0.05) were identified. Gene Ontology (GO), Kyoto Encyclopedia of Genes and Genomes (KEGG), and protein–protein interaction (PPI) network analyses were conducted.
Results
We identified 179 high-confidence lysine acetylation sites. IMN patients showed more acetylation sites (162 vs. 134) and unique sites (39 vs. 11) than controls. Twenty-eight sites were differentially acetylated. Bioinformatics analysis revealed that these proteins were enriched in lipoprotein metabolism, plasma lipoprotein particle assembly, and extracellular vesicle processes, and were involved in PPAR signaling, cholesterol metabolism, and fat/vitamin digestion and absorption. PPI network analysis identified apolipoproteins APOC3 and APOA1 as hub proteins in a lipid metabolism–associated module.
Conclusion
This study provides the first serum acetylome profile of IMN, demonstrating a strong link between acetylation dysregulation and lipid metabolism pathways. These findings offer novel insights into the metabolic-immune interactions in IMN pathogenesis, highlighting disease-specific acetylation sites as potential non-invasive biomarkers.
Funding
- Government Support – Non-U.S.