Skip Navigation



Journal of Biochemistry Advance Access published online on June 29, 2009
Journal of Biochemistry, doi:10.1093/jb/mvp097
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow All Versions of this Article:
146/4/471    most recent
mvp097v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Hojo-Nakashima, I.
Right arrow Articles by Yamada, M.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hojo-Nakashima, I.
Right arrow Articles by Yamada, M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The authors 2009. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Dynamic expression of peptidylarginine deiminase 2 in human monocytic leukemia THP-1 cells during macrophage differentiation

Ikuko Hojo-Nakashima, Ryo Sato, Katsuhiko Nakashima*,1, Teruki Hagiwara** and Michiyuki Yamada

International Graduate School of Arts and Sciences, Yokohama City University, Yokohama 236-0027, Japan

*Present address and 1correspondence to: Dr. Katsuhiko Nakashima, Division of Molecular Biomedicine for Pathogenesis, Center for Disease Biology and Integrative Medicine (CDBIM), Faculty of Medicine, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan, Tel: +81-3-5841-1437; Fax: +81-3-5841-1438, E-mail: nakashima{at}m.u-tokyo.ac.jp

Received May 11, 2009; Accepted June 6, 2009


  Abstract

Peptidylarginine deiminases (PADs) consist of five enzymes which are widely distributed in human and rodent tissues. The two types of enzymes are found in human peripheral blood cells; PAD4 mainly in granulocytes and monocytes and PAD2 in lymphocytes and macrophages. Little is known about the regulation of PAD expression in macrophages. Here we report that PAD2 is expressed in human monocytic leukemia THP-1 cells during differentiation into macrophages by 12-O-tetradecanoylphorbol-13-acetate. During this differentiation the levels of PAD2 mRNA and protein increased concomitantly, indicating the transcriptional regulation of PAD2 gene expression in the cells. The treatment of THP-1-derived macrophages with calcium ionophore A23187 [GenBank] generated vimentin deimination and resulted in the disruption of vimentin filament organization. We discuss the possible role of vimentin deimination in cell physiology.

Key Words: citrullinated proteins, protein deimination, vimentin, rheumatoid arthritis, monocytes

**Present address: Department of Life Science, School of Science and Engineering, Kinki University, 3-4-1 Kowakae, Higashi-Osaka 577-8502, Japan.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.