PAD2: A potential target for tumor therapy.

Yi Teng, Yuhang Chen, Xinyi Tang, Shengjun Wang, Kai Yin

Journal: Biochimica et biophysica acta. Reviews on cancer 2023;1878(5):188931

PMID: 37315720

Full Text on Elsevier Science View on PubMed

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.

Address: Department of General Surgery, Affiliated Hospital of Jiangsu University, Zhenjiang, China; Department of Immunology, Jiangsu Key Laboratory of Laboratory Medicine, School of Medicine, Jiangsu University, Zhenjiang, China.; Department of Immunology, Jiangsu Key Laboratory of Laboratory Medicine, School of Medicine, Jiangsu University, Zhenjiang, China.; Department of Laboratory Medicine, the Affiliated People's Hospital, Jiangsu University, Zhenjiang, China.; Department of Immunology, Jiangsu Key Laboratory of Laboratory Medicine, School of Medicine, Jiangsu University, Zhenjiang, China; Department of Laboratory Medicine, the Affiliated People's Hospital, Jiangsu University, Zhenjiang, China. Electronic address: [email protected].; Department of General Surgery, Affiliated Hospital of Jiangsu University, Zhenjiang, China. Electronic address: [email protected].

DOI: 10.1016/j.bbcan.2023.188931

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MeSH Terms: Humans, Citrullination, Protein Processing, Post-Translational, Citrulline