You Youngki, Many Gina, Nakayasu Ernesto S
Biological Sciences Division, Pacific Northwest National Laboratory, Richland, WA 99354, USA.
Front Anal Sci. 2024;4. doi: 10.3389/frans.2024.1512573. Epub 2025 Jan 2.
Lysine carbamylation is a non-enzymatic protein post-translational modification (PTM) that plays important roles in regulating enzymatic activity and the pathogenesis of diseases such as atherosclerosis, rheumatoid arthritis, and uremia. The progress of understanding the roles of carbamylation in biological systems has been delayed due to lack of systematic assays to study its functions. To aggravate this scenario, carbamylation is a major artifact in proteomics analysis given that urea, which is used during sample preparation induces carbamylation. In addition, anti-acetyllysine antibodies co-purify carbamylated and acetylated peptides. In a recent paper, we leveraged co-purification with anti-acetyllysine antibodies to develop a method for analyzing carbamylated proteomes. In this perspective article, we discuss how this method may be applied to characterize the physiological functions of carbamylation in humans and other biological models, as well as the utility of establishing novel disease biomarkers.
赖氨酸氨甲酰化是一种非酶促蛋白质翻译后修饰（PTM），在调节酶活性以及动脉粥样硬化、类风湿性关节炎和尿毒症等疾病的发病机制中发挥着重要作用。由于缺乏用于研究其功能的系统检测方法，人们对氨甲酰化在生物系统中作用的理解进展一直较为缓慢。更糟糕的是，鉴于样品制备过程中使用的尿素会诱导氨甲酰化，氨甲酰化是蛋白质组学分析中的一个主要假象。此外，抗乙酰赖氨酸抗体可共同纯化氨甲酰化和乙酰化肽段。在最近的一篇论文中，我们利用与抗乙酰赖氨酸抗体的共同纯化技术开发了一种分析氨甲酰化蛋白质组的方法。在这篇观点文章中，我们讨论了该方法如何应用于表征人类和其他生物模型中氨甲酰化的生理功能，以及建立新型疾病生物标志物的效用。
