Peptidylarginine deiminases and deimination in biology and pathology: relevance to skin homeostasis.
Deimination corresponds to the transformation of arginine residues within a peptide sequence into citrulline residues. Catalyzed by peptidylarginine deiminases, it decreases the net positive charge of proteins, alters intra and intermolecular ionic interactions and probably the folding of target proteins. Deimination has recently been implicated in several physiological and pathological processes. Here, we describe the enzymes involved in this post-translational modification, focusing on their expression, location and roles in skin, as well as their known protein substrates in the epidermis and hair follicles. We discuss also the potential involvement of deimination in human diseases including cutaneous disorders.
Chavanas
Stéphane
S
UMR 5165, CNRS-University Toulouse III, Faculty of Medicine Purpan, 37 allées J. Guesde, 31073 Toulouse, France.
Méchin
Marie-Claire
MC
Nachat
Rachida
R
Adoue
Véronique
V
Coudane
Fanny
F
Serre
Guy
G
Simon
Michel
M
D000818:Animals; D006706:Homeostasis / Q000502:physiology*; D006801:Humans; D006867:Hydrolases / Q000037:antagonists & inhibitors / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D051379:Mice; D000076342:Protein-Arginine Deiminases; D012871:Skin Diseases / Q000188:drug therapy / Q000201:enzymology* / Q000473:pathology* / Q000503:physiopathology; D012879:Skin Physiological Phenomena
D006867:Hydrolases; D000076342:Protein-Arginine Deiminases