Quantitative Proteomics Analysis Of Lysine 2-hydroxyisobutyrylation In IgA Nephropathy

Aims:Protein posttranslational modification is an indispensable regulatory element that can fine-tune protein functions and regulate diverse cellular processes.Lysine 2-hydroxyisobutyrylation(K_hib)is a protein posttranslational modification that is thought to play a role in a wide variety of active cellular functions.Methods:In this report,we comparatively studied the 2-hydroxyisobutyrylation proteome in peripheral blood mononuclear cells from a biopsy-proven immunoglobulin A nephropathy（IgAN）group and a normal control group based on liquid chromatography-tandem mass spectrometry.Results:Altogether,7405 proteins were identified and added to a K_hib library.We identified 111proteins with upregulated expression and 83 proteins with downregulated expression.Furthermore,122 K_hib-modified proteins containing 171 sites with increased K_hibmodification and 168 Khib-modified proteins containing 257 specific sites were detected.Conclusions:Importantly,the abundance of lipocalin 2 was increased in the differentially expressed proteins,and a KEGG-based functional enrichment analysis showed that K_hib proteins clustered in the IL-17 signaling pathway and phagosome category,which may have important associations with IgAN.Our data enlighten our understanding of K_hib in IgAN and indicate that K_hib may have important regulatory roles in IgAN.