Méchin Marie-Claire, Nachat Rachida, Coudane Fanny, Adoue Véronique, Arnaud Jacques, Serre Guy, Simon Michel
UMR 5165 CNRS/ Université Paul Sabatier, Hôpital Purpan, place du Docteur Baylac, TSA 40031, 31059 Toulouse Cedex 9, France. marie-claire.mechin@ udear.cnrs.fr
Med Sci (Paris). 2011 Jan;27(1):49-54. doi: 10.1051/medsci/201127149.
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.
脱氨或瓜氨酸化是一种具有多方面作用的翻译后修饰。它参与多种基本细胞过程,包括基因调控、胚胎发育和终末分化,还涉及与严重人类疾病如多发性硬化症和类风湿性关节炎相关的各种病理生理机制。脱氨作用,即肽基精氨酸在钙依赖的酶促作用下转化为肽基瓜氨酸,会导致修饰蛋白的电荷减少,对其构象、稳定性和/或相互作用产生重大影响,进而影响其功能。人类存在五种肽基精氨酸脱亚氨酶同型异构体(1 - 4和6),其组织表达各不相同。这些高度保守的酶在转录和转录后水平受到密切调控,可能包括自身脱氨作用。