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Journal of Biochemistry Advance Access published online on June 26, 2008
Journal of Biochemistry, doi:10.1093/jb/mvn079
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© 2008 The Japanese Biochemical Society

Citrullinated fibrinogen inhibits thrombin-catalyzed fibrin polymerization

Makiko Nakayama-Hamada1,*, Akari Suzuki2,*,{ddagger}, Hidehiko Furukawa1, Ryo Yamada2,3 and Kazuhiko Yamamoto2,4

1Daiichi-Sankyo Co., Ltd., 1-2-58 Hiromachi, Shinagawa-ku, Tokyo 140-8710, Japan
2Laboratory for Rheumatic Diseases, Center for Genomic Medicine, The Institute of Physical and Chemical Research, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045
3 Laboratory of Functional Genomics and Molecular Medicine, Human Genome Center, Institute of Medical Science, The University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan
4Department of Allergy and Rheumatology, Graduate School of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-8655, Japan

{ddagger}To whom correspondence should be addressed. Tel: +81-45-503-9569, Fax: +81-45-503-9590 E-mail: akaris{at}src.riken.jp

Received April 2, 2008; Accepted May 30, 2008


  Abstract

SUMMARY

Citrullination is the post-translational modification of arginine residues by peptidylarginine deiminases (PADIs). Fibrinogen is one substrate of PADIs under physiological conditions. Fibrinogen is an important factor for blood coagulation and inducing inflammation. The citrullinated form of fibrinogen appears in rheumatoid arthritis synovial tissue together with the production of autoantibodies that target self-peptides containing citrulline. However, whether the function of fibrinogen changes after citrullination remains unclear. We found that citrullinated fibrinogen markedly impairs the function of thrombin-catalyzed fibrin polymerization and also inhibits fibrin formation. Increased citrullinated fibrinogen might thus affect the balance between coagulation and fibrinolysis and alter antigenicity under physiological conditions. These data suggest that citrullination of proteins could physiologically change functions and subsequently generate proinflammatory conditions and autoimmune reactions.

Key Words: fibrinogen, citrullination, thrombin, fibrin formation, autoantigen

*Contributed equally to this work.


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