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This article is part of the supplement: Proceedings of the 8th Global Arthritis Research Network (GARN) Meeting and 1st Bio-Rheumatology International Congress (BRIC)

Poster presentation

The functions of the post-translational modifications in rheumatoid arthritis

Satoko Aratani1*, Naoko Yagishita2, Teruhisa Kanazawa1, Fukami Nakajima1, Yoshihisa Yamano2, Kusuki Nishioka1 and Toshihiro Nakajima1

  • * Corresponding author: Satoko Aratani

Author Affiliations

1 Institute of Medical Science, Tokyo Medical University, Shinjuku-ku, Tokyo, 160-8402, Japan

2 Institute of Medical Science, St. Marianna University School of Medicine, Kawasaki, Kanagawa, 216-8512, Japan

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Arthritis Research & Therapy 2012, 14(Suppl 1):P45  doi:10.1186/ar3646

The electronic version of this article is the complete one and can be found online at: http://arthritis-research.com/content/14/S1/P45


Published:9 February 2012

© 2012 Aratani et al.; licensee BioMed Central Ltd.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Poster presentation

Rheumatoid Arthritis (RA) is a chronic inflammatory joint disease and characterized by synovial hyperplasia. We previously cloned an E3 ubiquitin ligase, Synoviolin, as a regulatory factor of cell proliferation [1]. It suggested that endoplasmic reticulum (ER) associated degradation system (ERAD) via Synoviolin has important roles for overgrowth of synoviocytes [2,3]. Meanwhile, it is known that autoantibodies to citrullinated proteins are specific for RA and good markers for RA. Peptidyl-Arginine Deiminases 4 (PADI4) is identified as the RA-susceptible gene [3]. However functions of citrulinated proteins are unclear. In this study, we hypothesize that the accumulation of citrullinated proteins in RA synoviocytes could associate for ER stress and explore the crosstalk of ubiquitination and citrullination.

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