title: Peptidylarginine deiminases and deimination in biology and pathology: relevance to skin homeostasis.
abstract: 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.
authors.affiliation: UMR 5165, CNRS-University Toulouse III, Faculty of Medicine Purpan, 37 allées J. Guesde, 31073 Toulouse, France.
authors.forename: Stéphane
authors.initials: S
authors.lastname: Chavanas
authors.forename: Marie-Claire
authors.initials: MC
authors.lastname: Méchin
authors.forename: Rachida
authors.initials: R
authors.lastname: Nachat
authors.forename: Véronique
authors.initials: V
authors.lastname: Adoue
authors.forename: Fanny
authors.initials: F
authors.lastname: Coudane
authors.forename: Guy
authors.initials: G
authors.lastname: Serre
authors.forename: Michel
authors.initials: M
authors.lastname: Simon
mesh_terms: 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
chemical_list: D006867:Hydrolases; D000076342:Protein-Arginine Deiminases