Huang Shaoying, Zheng Fengping, Lin Hua, Zhou Xianqing, Xu Huixuan, Zhang Cantong, Dai Weier, Hocher Berthold, Zhang Xinzhou, Tang Donge, Dai Yong
Department of Clinical Medical Research Center, Guangdong Provincial Engineering Research Center of Autoimmune Disease Precision Medicine, The Second Clinical Medical College of Jinan University, The First Affiliated Hospital Southern University of Science and Technology, Shenzhen People's Hospital, Shenzhen, 518020, Guangdong, People's Republic of China.
Guangxi Key Laboratory of Metabolic Disease Research, Nephrology Department of Guilin NO. 924 Hospital, Guilin, 541002, People's Republic of China.
Clin Proteomics. 2021 Feb 8;18(1):7. doi: 10.1186/s12014-021-09314-0.
Protein posttranslational modification is an indispensable regulatory element that can fine-tune protein functions and regulate diverse cellular processes. Lysine 2-hydroxyisobutyrylation (Khib) is a protein posttranslational modification that was recently identified and is thought to play a role in a wide variety of active cellular functions.
In this report, for the first time, 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.
Altogether, 7405 proteins were identified and added to a Khib library. Of these proteins, we identified 111 with upregulated expression and 83 with downregulated expression. Furthermore, we identified 428 Khib modification sites on 290 Khib-modified proteins, including 171 sites with increased modification on 122 Khib-modified proteins and 257 specific sites with reduced modification on 168 Khib-modified proteins.
Importantly, the abundance of lipocalin 2 was increased in the differentially expressed proteins, and a KEGG-based functional enrichment analysis showed that Khib proteins clustered in the IL-17 signaling pathway and phagosome category, which may have important associations with IgAN. Our data enlighten our understanding of Khib in IgAN and indicate that Khib may have important regulatory roles in IgAN.
蛋白质翻译后修饰是一种不可或缺的调控元件,可微调蛋白质功能并调节多种细胞过程。赖氨酸2-羟基异丁酰化(Khib)是一种最近被发现的蛋白质翻译后修饰,被认为在多种活跃的细胞功能中发挥作用。
在本报告中,我们首次基于液相色谱-串联质谱法,对经活检证实的免疫球蛋白A肾病(IgAN)组和正常对照组外周血单个核细胞中的2-羟基异丁酰化蛋白质组进行了比较研究。
总共鉴定出7405种蛋白质并添加到Khib文库中。在这些蛋白质中,我们鉴定出111种表达上调的蛋白质和83种表达下调的蛋白质。此外,我们在290种Khib修饰的蛋白质上鉴定出428个Khib修饰位点,包括122种Khib修饰蛋白质上171个修饰增加的位点和168种Khib修饰蛋白质上257个修饰减少的特定位点。
重要的是,在差异表达的蛋白质中,lipocalin 2的丰度增加,基于KEGG的功能富集分析表明,Khib蛋白质聚集在IL-17信号通路和吞噬体类别中,这可能与IgAN有重要关联。我们的数据增进了我们对IgAN中Khib的理解,并表明Khib可能在IgAN中具有重要的调控作用。