The Journal of Experimental Medicine
StemCell Technologies
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Published 21 April 2003. doi:10.1084/jem.20021321
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© Rockefeller University Press, 0022-1007/2003/4/1029 $5.00
The Journal of Experimental Medicine, Volume 197, Number 8, 1029-1035

Jun Dimerization Protein 2 (JDP2), a Member of the AP-1 Family of Transcription Factor, Mediates Osteoclast Differentiation Induced by RANKL

Reimi Kawaida1, Toshiaki Ohtsuka1, Junichi Okutsu1, Tohru Takahashi1, Yuho Kadono2, Hiromi Oda2, Atsuhiko Hikita2, Kozo Nakamura2, Sakae Tanaka2 and Hidehiko Furukawa1

1 Biomedical Research Laboratories, Sankyo Co., Ltd., Shinagawa-ku, Tokyo 140-8710, Japan
2 Department of Orthopaedic Surgery, Faculty of Medicine, The University of Tokyo, Bunkyo-ku, Tokyo 113-0033, Japan

Address correspondence to Toshiaki Ohtsuka, Biomedical Research Laboratories, Sankyo Co., Ltd., 1-2-58 Hiromachi, Shinagawa-ku, Tokyo 140-8710, Japan. Phone: 81-3-3492-3131; Fax: 81-3-5436-8587; E-mail: tosiak{at}shina.sankyo.co.jp

Osteoclasts are multinucleated cells that resorb bones, and are derived from hematopoietic cells of the monocyte/macrophage lineage. The receptor activator of NF-{kappa}B ligand (RANKL, also called ODF/TRANCE/OPGL) stimulates both osteoclast differentiation from osteoclast progenitors and activation of mature osteoclasts. To identify genes responsible for osteoclast differentiation, we used a molecular indexing technique. Here, we report a clone of one of these genes whose transcription is induced by soluble RANKL (sRANKL) in both the RAW264.7 cells of the mouse macrophage cell line and the mouse primary bone marrow cells. The predicted protein was found to be a mouse homologue of Jun dimerization protein 2 (JDP2), a member of the AP-1 family of transcription factors, containing a basic region-leucine zipper motif. Transient transfection experiments revealed that overexpression of JDP2 leads to activation of both tartrate-resistant acid phosphatase (TRAP) and cathepsin K gene promoters in RAW264.7 cells. Infection of mouse primary bone marrow cells with retroviruses expressing JDP2-facilitated sRANKL-mediated formation of TRAP-positive multinuclear osteoclasts. Importantly, antisense oligonucleotide to JDP2 strongly suppressed sRANKL-induced osteoclast formation of RAW264.7 cells. Our findings suggest that JDP2 may play an important role in the RANK-mediated signal transduction system, especially in osteoclast differentiation.

Key Words: bone resorption • signal transduction • osteoclastogenesis • molecular indexing • mitogen-activated protein kinase


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