Tuyển tập các báo cáo nghiên cứu về y học được đăng trên tạp chí y học General Psychiatry cung cấp cho các bạn kiến thức về ngành y đề tài: Bacterial and human peptidylarginine deiminases: targets for inhibiting the autoimmune response in rheumatoid arthritis? | Mangat et al. Arthritis Research Therapy 2010 12 209 http content 12 3 209 REVIEW Bacterial and human peptidylarginine deiminases targets for inhibiting the autoimmune response in rheumatoid arthritis Pamela Mangat 1 Natalia Wegner1 Patrick J Venables 1 and Jan Potempa2-3 Abstract Peptidylarginine deiminases PADs convert arginine within a peptide peptidylarginine into peptidylcitrulline. Citrullination by human PADs is important in normal physiology and inflammation. Porphyromonasgingivalis a major pathogen in periodontitis is the only prokaryote described to possess PAD. P gingivalis infection may generate citrullinated peptides which trigger anti-citrullinated peptide antibodies. In susceptible individuals host protein citrullination by human PADs in the joint probably perpetuates antibody formation paving the way for the development of chronic arthritis. Blockades of bacterial and human PADs may act as powerful novel therapies by inhibiting the generation of the antigens that trigger and sustain autoimmunity in rheumatoid arthritis. Introduction Arginine is a positively charged hydrophilic amino acid that is often found on the surface of proteins where it participates in ionic interactions with other amino acid side chains and forms stabilizing hydrogen bonds with both the peptide backbone and amino acid side chains. These characteristics make it a key amino acid in the three-dimensional organization of proteins and in the interaction with other biological molecules. Hence post-translational modification of arginine can alter the threedimensional protein structure and function and potentially expose previously hidden epitopes to the immune system. Deimination citrullination of arginine side chains peptidylarginine to form peptidylcitrulline is one Correspondence 1The Kennedy Institute of Rheumatology Division Imperial College 65 Aspenlea Road London W6 8LH UK Full list of author information is available at the end
