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Journal of Biochemistry 2005 137(3):331-338; doi:10.1093/jb/mvi036
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© 2005 The Japanese Biochemical Society

Regular Paper

Involvement of Calpain in Osteoclastic Bone Resorption

Masami Hayashi1, Yasuko Koshihara2, Hideaki Ishibashi3, Seizo Yamamoto3, Satoshi Tsubuki4, Takaomi C. Saido4, Seiichi Kawashima5 and Mitsushi Inomata1,*

1 Biomembrane Research Group, and 2 Bone Research Group, Tokyo Metropolitan Institute of Gerontology, 35-2 Sakae-cho, Itabashi-ku, Tokyo 173-0015; 3 Department of Orthopedic Surgery, Tokyo Metropolitan Geriatric Medical Center, 35-2 Sakae-cho, Itabashi-ku, Tokyo 173-0015; 4 Laboratory for Proteolytic Neuroscience, RIKEN Brain Science Institute, 2-1 Hirosawa, Wako, Saitama 351-0198; and 5 Department of Molecular Biology, Tokyo Metropolitan Institute of Medical Science, Honkomagome, Bunkyo-ku, Tokyo 113-8613

* To whom correspondence should be addressed. Tel: +81-3-3964-3241 (Ext. 3068), Fax: 81-3-3579-4776, E-mail: minomata{at}tmig.or.jp

ABSTRACT

There is increasing evidence that calpain contributes to the reorganization of the cytoskeleton in the integrin-mediated signaling pathway. Osteoclastic bone resorption requires cell-matrix contact, an event mediated by integrin {alpha}vß3, and subsequent cytoskeletal reorganization to form characteristic membrane domains such as the sealing zone and ruffled border. In this study, therefore, we investigated whether calpain is involved in osteoclastic bone resorption. Membrane-permeable calpain inhibitors suppress the resorption activity of human osteoclasts, but an impermeable inhibitor does not. Upon the attachment of osteoclasts to bone, µ-calpain is translocated from the cytosolic to the cytoskeletal fraction and is autolytically activated. Both the activation of µ-calpain and the formation of actin-rings, the cytoskeletal structures essential for bone resorption, are inhibited by membrane-permeable calpain inhibitors. The activated µ-calpain in osteoclasts selectively cleaves talin, which links the matrix-recognizing integrin to the actin cytoskeleton. These findings suggest that calpain is a regulator of the bone resorption activity of osteoclasts through reorganization of the cytoskeleton related to actin-ring formation.


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