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PERSPECTIVE article

Front. Anal. Sci.
Sec. Omics
Volume 4 - 2024 | doi: 10.3389/frans.2024.1512573
This article is part of the Research Topic Thought Leaders in Analytical Science Research View all 8 articles

Protein carbamylation and proteomics: from artifacts to elucidation of biological functions

Provisionally accepted
Youngki You Youngki You Gina Many Gina Many Ernesto Satoshi Nakayasu Ernesto Satoshi Nakayasu *
  • Biological Sciences Division, Pacific Northwest National Laboratory (DOE), Richland, IN, United States

The final, formatted version of the article will be published soon.

    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.

    Keywords: Carbamylation, post-translational modification, Proteomics, function, Disease

    Received: 16 Oct 2024; Accepted: 06 Dec 2024.

    Copyright: © 2024 You, Many and Nakayasu. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

    * Correspondence: Ernesto Satoshi Nakayasu, Biological Sciences Division, Pacific Northwest National Laboratory (DOE), Richland, 49707, IN, United States

    Disclaimer: All claims expressed in this article are solely those of the authors and do not necessarily represent those of their affiliated organizations, or those of the publisher, the editors and the reviewers. Any product that may be evaluated in this article or claim that may be made by its manufacturer is not guaranteed or endorsed by the publisher.