Citrullination in tumor immunity and therapy.
review · Level V
Where this comes from
- Record sourced from PubMed, PMID 41090352.
- Also identified by DOI 10.1172/JCI196348 and PMC identifier 12520671.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Peptidyl arginine deiminases (PADs) catalyze the conversion of arginine residues into peptidyl citrulline, a posttranslational modification known as protein citrullination (or arginine deimination). This process alters the charge of proteins from positive to neutral, thereby affecting their folding, stability, conformation, and function. PAD2 and PAD4 can translocate into the nucleus and citrullinate both cytoplasmic and nuclear proteins. In this Review, we focus on PAD2- and PAD4-mediated citrullination in immune cell subsets within the tumor microenvironment. We discuss how citrullination regulates immune cell function and tumor immunity and explore the potential of targeting citrullination as a strategy for cancer immunotherapy.
Medical subject headings
- Neoplasms
- Citrullination
- Tumor Microenvironment
- Immunotherapy
- Protein Processing, Post-Translational
- Citrulline
- Neoplasm Proteins