Protein carbamylation and proteomics: from artifacts to elucidation of biological functions
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 bi...
Saved in:
| Main Authors: | , , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Frontiers Media S.A.
2025-01-01
|
| Series: | Frontiers in Analytical Science |
| Subjects: | |
| Online Access: | https://www.frontiersin.org/articles/10.3389/frans.2024.1512573/full |
| Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
| _version_ | 1841561176565088256 |
|---|---|
| author | Youngki You Gina Many Ernesto S. Nakayasu |
| author_facet | Youngki You Gina Many Ernesto S. Nakayasu |
| author_sort | Youngki You |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-3d0c6d6eff614cdca6e7d89215d336c8 |
| institution | Kabale University |
| issn | 2673-9283 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Analytical Science |
| spelling | doaj-art-3d0c6d6eff614cdca6e7d89215d336c82025-01-03T05:10:26ZengFrontiers Media S.A.Frontiers in Analytical Science2673-92832025-01-01410.3389/frans.2024.15125731512573Protein carbamylation and proteomics: from artifacts to elucidation of biological functionsYoungki YouGina ManyErnesto S. NakayasuLysine 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.https://www.frontiersin.org/articles/10.3389/frans.2024.1512573/fullcarbamylationpost-translational modificationproteomicsfunctiondisease |
| spellingShingle | Youngki You Gina Many Ernesto S. Nakayasu Protein carbamylation and proteomics: from artifacts to elucidation of biological functions Frontiers in Analytical Science carbamylation post-translational modification proteomics function disease |
| title | Protein carbamylation and proteomics: from artifacts to elucidation of biological functions |
| title_full | Protein carbamylation and proteomics: from artifacts to elucidation of biological functions |
| title_fullStr | Protein carbamylation and proteomics: from artifacts to elucidation of biological functions |
| title_full_unstemmed | Protein carbamylation and proteomics: from artifacts to elucidation of biological functions |
| title_short | Protein carbamylation and proteomics: from artifacts to elucidation of biological functions |
| title_sort | protein carbamylation and proteomics from artifacts to elucidation of biological functions |
| topic | carbamylation post-translational modification proteomics function disease |
| url | https://www.frontiersin.org/articles/10.3389/frans.2024.1512573/full |
| work_keys_str_mv | AT youngkiyou proteincarbamylationandproteomicsfromartifactstoelucidationofbiologicalfunctions AT ginamany proteincarbamylationandproteomicsfromartifactstoelucidationofbiologicalfunctions AT ernestosnakayasu proteincarbamylationandproteomicsfromartifactstoelucidationofbiologicalfunctions |