Isotopic Labeling-Enabled Chemical Proteomics Analysis Revealed Structural and Functional Features of Allysine Modifications in Mammalian Cells and Tissues.

ABSTRACT: Allysine is a pivotal protein post-translational modification that regulates protein interaction and activities. It is also recognized as a marker of oxidative stress under certain metabolic and physiological conditions. In this study, we developed a capture-and-release chemical proteomics workflow with heavy isotopic labeling that enables system-wide enrichment and site-specific identification of allysine as well as other carbonylated peptides, such as peptides containing glutamic semialdehyde derived from the oxidative damage of arginine and proline, with high confidence. The streamlined workflow led to the identification of 434 allysine sites on 349 proteins in human 293T and HCT116 cells and 317 allysine sites on 157 proteins in mouse muscle tissues without any treatment with an oxidat

SUBMITTER: Sin YC 

PROVIDER: S-EPMC12410100 | biostudies-literature | 2025 May

REPOSITORIES: biostudies-literature