Peptidyl arginine deiminases: detection and functional analysis of protein citrullination

Curr Opin Struct Biol. 2019 Dec:59:205-215. doi: 10.1016/j.sbi.2019.01.024. Epub 2019 Mar 1.

Abstract

Citrullination is a post-translational modification of arginine that is catalyzed by the protein arginine deiminases (PADs). Abnormal citrullination is observed in many autoimmune diseases and cancers. Anti-citrullinated protein antibodies (ACPA) are hallmarks of RA and used as diagnostic markers for disease diagnosis. Even though citrullination is associated with many different pathologies, its role remains unclear due to the challenges associated with the detection of citrullinated proteins since the mass change is only 0.984 Da. Moreover, the functional effects of protein citrullination remain mostly unknown. Herein, we discuss a brief overview of PAD structure and function, recent advances in the detection of citrullinated proteins in complex biological systems and the functional consequences of protein citrullination.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Catalysis
  • Chromatography, High Pressure Liquid
  • Citrullination*
  • Enzyme Activation
  • Humans
  • Mass Spectrometry
  • Models, Molecular
  • Protein Binding
  • Protein Processing, Post-Translational
  • Protein-Arginine Deiminases / chemistry*
  • Protein-Arginine Deiminases / metabolism*
  • Structure-Activity Relationship
  • Substrate Specificity

Substances

  • Protein-Arginine Deiminases