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Journal of Biochemistry Advance Access originally published online on June 29, 2009
Journal of Biochemistry 2009 146(4):471-479; doi:10.1093/jb/mvp097
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© 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 Leukaemia THP-1 Cells During Macrophage Differentiation

Ikuko Hojo-Nakashima, Ryo Sato, Katsuhiko Nakashima*,{dagger}, Teruki Hagiwara* and Michiyuki Yamada

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

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

{dagger}To whom correspondence should be addressed. 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 leukaemia 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, monocytes, protein deimination, rheumatoid arthritis, vimentin

Abbreviations: AMCA, anti-modified citrulline antibody; BA, N{alpha}-benzoyl-L-arginine; BAEE, N{alpha}-benzoyl-L-arginine ethyl ester; DIG, digoxigenin; DMSO, dimethylsulfoxide; GAPDH, glyceraldehyde-3-phosphate dehydrogenase; GST, glutathione S-transferase; kDa, kilodalton; knt, kilonucleotide; PAD, Peptidylarginine deiminase; PBS(-), Mg2+ and Ca2+-free phosphate-buffered saline; PMSF, phenylmethanesulfonyl fluoride; RT-PCR, reverse transcription-polymerase chain reaction; TPA, 12-O-tetradecanoylphorbol-13-acetate; 1{alpha}, 25-(OH)2 D3, 1{alpha}, 25-dihydroxyvitamin D3


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