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Bacterial And Human Peptidylarginine Deiminases: Targets For Inhibiting The Autoimmune Response In Rheumatoid Arthritis?

P. Mangat, Natalia Wegner, P. Venables, J. Potempa
Published 2010 · Medicine

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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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Citrullination is an infl ammation-dependent process
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10.1002/ART.20584
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Bacterial and human peptidylarginine deiminases: targets for inhibiting the autoimmune response in rheumatoid arthritis?
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Synovial inflammation in active rheumatoid arthritis and psoriatic arthritis facilitates trapping of a variety of oral bacterial DNAs.
K. Moen (2006)
A fl uoroacetamidinebased inactivator of protein arginine deiminase 4: design, synthesis, and in vitro and in vivo evaluation
Y Luo (2006)
Association of periodontal disease and tooth loss with rheumatoid arthritis in the US population.
P. de Pablo (2008)
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10.1021/BI061180D
Inhibitors and inactivators of protein arginine deiminase 4: functional and structural characterization.
Y. Luo (2006)
A stereospecifi c , hemebinding inhibitor of nitricoxide synthases
C Frey (1994)
Treatment with Clamidine , a peptidyl arginine deiminase ( PAD ) inhibitor signifi cantly reduces collageninduced arthritis ( CIA ) [ abstract ]
V Willis (2009)
10.1021/BI051341Y
Inactivation of two diverse enzymes in the amidinotransferase superfamily by 2-chloroacetamidine: dimethylargininase and peptidylarginine deiminase.
E. Stone (2005)
10.1016/J.GENE.2003.12.038
Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6.
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Immunohistochemical Demonstration of Peptidylarginine Deiminase in Human Sweat Glands
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Levofloxacin Treatment in Patients with Rheumatoid Arthritis Receiving Methotrexate
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Effect of enzymatic deimination on the conformation of recombinant prion protein.
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10.1016/J.BMC.2007.10.021
Profiling Protein Arginine Deiminase 4 (PAD4): a novel screen to identify PAD4 inhibitors.
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Synovial inflammation in active rheumatoid arthritis and psoriatic arthritis facilitates trapping of a variety of oral bacterial DNAs.
K. Moen (2006)
10.1007/s00018-005-5196-y
The peptidylarginine deiminases expressed in human epidermis differ in their substrate specificities and subcellular locations
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10.1038/nrrheum.2009.28
Periodontitis in systemic rheumatic diseases
P. D. Pablo (2009)
10.1016/S0014-5793(98)01036-9
Cleavage and activation of proteinase‐activated receptor‐2 on human neutrophils by gingipain‐R from Porphyromonas gingivalis
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10.1016/J.GENE.2003.12.038
Comparative analysis of the mouse and human peptidylarginine deiminase gene clusters reveals highly conserved non-coding segments and a new human gene, PADI6.
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Haff ajee AD: Periodontal microbial ecology
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