PAD2: A potential target for tumor therapy

Biochim Biophys Acta Rev Cancer. 2023 Sep;1878(5):188931. doi: 10.1016/j.bbcan.2023.188931. Epub 2023 Jun 12.

Abstract

Peptide arginine deiminase 2(PAD2) catalyzes the conversion of arginine residues on target proteins to citrulline residues in the presence of calcium ions. This particular posttranslational modification is called citrullination. PAD2 can regulate the transcriptional activity of genes through histone citrullination and nonhistone citrullination. In this review, we summarize the evidence from recent decades and systematically illustrate the role of PAD2-mediated citrullination in tumor pathology and the regulation of tumor-associated immune cells such as neutrophils, monocytes, macrophages and T cells. Several PAD2-specific inhibitors are also presented to discuss the feasibility of anti-PAD2 therapy to treat tumors and the urgent problems to be solved. Finally, we review some recent developments in the development of PAD2 inhibitors.

Keywords: Citrullination; Peptide arginine deiminase 2; Tumor,therapy.

Publication types

  • Review
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Citrullination*
  • Citrulline / metabolism
  • Humans
  • Protein Processing, Post-Translational*

Substances

  • Citrulline