Peptidylarginine deiminases in citrullination, gene regulation, health and pathogenesis

Shu Wang, Yanming Wang

Research output: Contribution to journalReview articlepeer-review

221 Scopus citations


Peptidylarginine deiminases are a family of enzymes that mediate post-translational modifications of protein arginine residues by deimination or demethylimination to produce citrulline. In vitro, the activity of PADs is dependent on calcium and reductive reagents carrying a free sulfhydryl group. The discovery that PAD4 can target both arginine and methyl-arginine for citrullination about 10. years ago renewed our interest in studying this family of enzymes in gene regulation and their physiological functions. The deregulation of PADs is involved in the etiology of multiple human diseases, including cancers and autoimmune disorders. There is a growing effort to develop isoform specific PAD inhibitors for disease treatment. However, the regulation of the activity of PADs in vivo remains largely elusive, and we expect that much will be learned about the role of these enzymes in a normal life cycle and under pathology conditions.

Original languageEnglish (US)
Pages (from-to)1126-1135
Number of pages10
JournalBiochimica et Biophysica Acta - Gene Regulatory Mechanisms
Issue number10
StatePublished - Oct 2013

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics


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