Details

Autor(en) / Beteiligte

• Tezuka, K
• Tezuka, Y
• Maejima, A
• Sato, T
• Nemoto, K
• Kamioka, H
• Hakeda, Y
• Kumegawa, M

Titel

Molecular cloning of a possible cysteine proteinase predominantly expressed in osteoclasts

Ist Teil von

• The Journal of biological chemistry, 1994-01, Vol.269 (2), p.1106-1109

Ort / Verlag

United States: American Society for Biochemistry and Molecular Biology

Erscheinungsjahr

1994

Quelle

Free E-Journal (出版社公開部分のみ）

Beschreibungen/Notizen

• Osteoclasts are multinucleate giant cells playing key roles in bone resorption. These cells solubilize mineralized bone matrix by means of acid and protease action; however, the precise mechanism of this process is not well known. Recently, we succeeded in the isolation of pure osteoclasts from rabbit bones and constructed a cDNA library. Using a differential screening procedure, two genes expressed predominantly in osteoclasts compared with spleen cells were isolated (Tezuka, K., Sato, T., Kamioka, H., Nijweide, P. J., Tanaka, K., Matsuo, T., Ohta, M., Kurihara, N., Hakeda, Y., and Kumegawa, M. (1992) Biochem. Biophys. Res. Commun. 186, 911-917). One of them, OC-2, was found to encode a possible cysteine proteinase structurally related to cathepsins L and S. By in situ hybridization, OC-2 was confirmed to be expressed in osteoclasts in vivo. By Northern blot analysis, OC-2 was highly and preferentially expressed in osteoclasts compared with other tissues such as kidney, liver, spleen, and lung. The predominant expression of OC-2 in osteoclasts may suggest that OC-2 encodes a protein, possibly a cysteine proteinase, that plays an important role in osteoclastic bone resorption.