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[Deimination or citrullination, a post-translational modification with many physiological and pathophysiological
Marie-Claire Méchin1, Rachida Nachat, Fanny Coudane
1UMR 5165 CNRS/ Université Paul Sabatier, Hôpital Purpan, place du Docteur Baylac, TSA 40031, 31059 Toulouse Cedex 9, France. marie-claire.mechin@ udear.cnrs.fr
Abstract:
Deimination or citrullination, is a post-translational modification with many facets. It is involved in several basic cellular processes, including gene regulation, embryonic development and terminal differentiation, and also in various pathophysiological mechanisms linked to severe human diseases such as multiple sclerosis and rheumatoid arthritis. Deimination, the calcium-dependent enzymatic conversion of peptidyl-arginine to peptidyl-citrulline, induces a decrease in the charge of the modified proteins with major consequences on their conformation, stability and/or interactions, and therefore on their functions. Five isotypes of peptidylarginine deiminases (1-4 and 6), exist in humans with a variable tissue expression. These highly conserved enzymes are closely regulated at transcriptional and post-transcriptional levels, probably including auto-deimination.
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