Peptidylarginine deiminase and citrullination: Potential therapeutic targets for inflammatory diseases

Byungki Jang, Sung Jae Shin

Research output: Contribution to journalReview article

3 Citations (Scopus)


The multiple post-translational modifications of proteins display specific gain- or loss-of-function under normal and abnormal conditions. These modifications are precisely regulated by post-translational modification enzymes. The altered molecular status perturbs the pattern of gene expression and decides on a direction to signal transduction cascades as well as intrinsic properties of the proteins. Ultimately, it strictly maintains intracellular environment or results in disease manifestations. Recently, it has become that enzyme-dependent modification of arginine residue to citrulline exerts an important role in the induction of autoimmunity including rheumatoid arthritis, multiple sclerosis, and cancer. The modification of arginine residue to citrulline on proteins is called 'citrullination' or 'deimination' and is regulated by the calcium-dependent enzyme peptidylarginine deiminase (PAD). Now many effective PAD inhibitors (for example, Cl-amidine) have developed that ameliorates disease phenotypes. In this review, we discuss crucial roles of PAD enzyme and citrullination, the effectiveness of PAD inhibitors, and the implication in pathology.

Original languageEnglish
Pages (from-to)159-167
Number of pages9
JournalJournal of Bacteriology and Virology
Issue number3
Publication statusPublished - 2013


All Science Journal Classification (ASJC) codes

  • Microbiology
  • Immunology
  • Virology

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