PNNL

Abstract

Lysine carbamylation is a non-enzymatic protein post-translational modification (PTM) that plays important roles in regulating enzymatic activity as well as in diseases such as atherosclerosis, rheumatoid arthritis, and uremia. The progress of understanding the roles of carbamylation in biological systems has been delayed due to the lack of systematic assays to study its functions. To aggravate this scenario, carbamylation is a major artifact in proteomics analysis given urea used during sample preparation induces carbamylation. In addition, anti-acetyllysine antibodies co-purify carbamylated peptides with acetylated ones. In a recent paper, we leveraged co-purification with anti-acetyllysine antibodies to develop a method for analyzing carbamylated proteomes. Here, we discuss the opportunities brought by this method to characterize the physiological functions of carbamylation in humans and other biological models, and the establishment of novel disease biomarkers.