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Peptidylarginine deiminases and deiminated proteins at the epidermal barrier
Author(s) -
Cau Laura,
Méchin MarieClaire,
Simon Michel
Publication year - 2018
Publication title -
experimental dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.108
H-Index - 96
eISSN - 1600-0625
pISSN - 0906-6705
DOI - 10.1111/exd.13684
Subject(s) - citrullination , citrulline , chemistry , arginine , protein folding , biochemistry , microbiology and biotechnology , protein structure , leymus , biophysics , biology , amino acid , grassland , agronomy
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.