Peptidylarginine deiminases and deiminated proteins at the epidermal barrier

Exp Dermatol. 2018 Aug;27(8):852-858. doi: 10.1111/exd.13684. Epub 2018 Jun 29.

Abstract

Deimination or citrullination is a post-translational modification catalysed by a family of calcium-dependent enzymes called peptidylarginine deiminases (PADs). It corresponds to the transformation of arginine residues within a peptide sequence into citrulline residues. Deimination induces a decreased net charge of targeted proteins; therefore, it alters their folding and changes intra- and intermolecular ionic interactions. Deimination is involved in several physiological processes (inflammation, gene regulation, etc.) and human diseases (rheumatoid arthritis, neurodegenerative diseases, cancer, etc.). Here, we describe the PADs expressed in the epidermis and their known substrates, focusing on their role in the epidermal barrier function.

Keywords: S100-fused type proteins; citrullination; deimination; filaggrin; keratinocyte differentiation; peptidylarginine deiminase; post-translational modification.

Publication types

  • Review

MeSH terms

  • Animals
  • Arginine / metabolism
  • Arthritis, Rheumatoid / metabolism
  • Calcium / metabolism
  • Citrulline / metabolism
  • Epidermal Cells / metabolism
  • Epidermis / enzymology*
  • Filaggrin Proteins
  • Gene Expression Profiling
  • Gene Expression Regulation
  • Humans
  • Hydrolases / metabolism
  • Inflammation
  • Mice
  • Neoplasms / metabolism
  • Neurodegenerative Diseases / metabolism
  • Protein Processing, Post-Translational
  • Protein-Arginine Deiminases / metabolism*

Substances

  • FLG protein, human
  • Filaggrin Proteins
  • Citrulline
  • Arginine
  • Hydrolases
  • Protein-Arginine Deiminases
  • Calcium