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Molecular cloning of a possible cysteine proteinase predominantly expressed in osteoclasts.
Open accessAbstract
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.
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Citations
Cited by
Impaired osteoclastic bone resorption leads to osteopetrosis in cathepsin-K-deficient mice
Saftig, P., Hunziker, E., Wehmeyer, O., Jones, S., Boyde, A., Rommerskirch, W., Moritz, J. D., Schu, P., & von Figura, K. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.23.13453 · Cited by 913
Hruska, K. A., & Teitelbaum, S. L. (1995) · New England Journal of Medicine · doi:10.1056/nejm199507203330307 · Cited by 404
Matrix metalloproteinases (MMP) and cathepsin K contribute differently to osteoclastic activities
Delaissé, J., Andersen, T. L., Engsig, M. T., Henriksen, K., Troen, T., & Blavier, L. (2003) · Microscopy Research and Technique · doi:10.1002/jemt.10374 · Cited by 341
Proteinases in bone resorption: obvious and less obvious roles
Delaissé, J.-M., Engsig, M. T., Everts, V., del Carmen Ovejero, M., Ferreras, M., Lund, L., Vu, T. H., Werb, Z., Winding, B., Lochter, A., et al. (2000) · Clinica Chimica Acta · doi:10.1016/s0009-8981(99)00230-2 · Cited by 227
Identification of the membrane-type matrix metalloproteinase MT1-MMP in osteoclasts
Sato, T., Ovejero, M. D. C., Hou, P., Heegaard, A.-M., Kumegawa, M., Tækker Foged, N., & Delaissé, J.-M. (1997) · Journal of Cell Science · doi:10.1242/jcs.110.5.589 · Cited by 214
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Metadata
- Authors
- Tezuka, K., Tezuka, Y., Maejima, A., Sato, T., Nemoto, K., Kamioka, H., Hakeda, Y., & Kumegawa, M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1994-01
- Volume
- 269
- Issue
- 2
- Pages
- 1106-1109
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1583830460
- Cited by
- 341
- References
- 0
- FWCI
- 5.52
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Tezuka, K., Tezuka, Y., Maejima, A., Sato, T., Nemoto, K., Kamioka, H., Hakeda, Y., & Kumegawa, M. (1994). Molecular cloning of a possible cysteine proteinase predominantly expressed in osteoclasts. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(17)42227-7
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