Bacterial and human peptidylarginine deiminases: targets for inhibiting the autoimmune response in rheumatoid arthritis?

被引：74
|
作者：
Mangat, Pamela [1 ]
Wegner, Natalia [1 ]
Venables, Patrick J. [1 ]
Potempa, Jan [2 ,3 ]
机构：
[1] Univ London Imperial Coll Sci Technol & Med, Kennedy Inst, Div Rheumatol, London W6 8LH, England
[2] Jagiellonian Univ, Dept Microbiol, Fac Biochem Biophys & Biotechnol, PL-30387 Krakow, Poland
[3] Univ Louisville, Sch Dent Oral Hlth & Syst Dis, Louisville, KY 40202 USA
来源：
ARTHRITIS RESEARCH & THERAPY | 2010年 / 12卷 / 03期
基金：
美国国家卫生研究院;
关键词：
PORPHYROMONAS-GINGIVALIS; CITRULLINATED PROTEINS; ARGININE DEIMINASE; DOUBLE-BLIND; POSTTRANSLATIONAL MODIFICATION; ANTIBODY-RESPONSES; STRUCTURAL BASIS; SYNOVIAL-FLUID; EXPRESSION; ENZYMES;
D O I：
10.1186/ar3000
中图分类号：
R5 [内科学];
学科分类号：
1002 ; 100201 ;
摘要：
Peptidylarginine deiminases (PADs) convert arginine within a peptide (peptidylarginine) into peptidylcitrulline. Citrullination by human PADs is important in normal physiology and inflammation. Porphyromonas gingivalis, 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.
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