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Lysosomal cysteine and aspartic proteinases, acid phosphatase, and an endogenous cysteine proteinase inhibitor, cystatin-beta, in rat osteoclasts

Y Ohsawa, T Nitatori, S Higuchi, E Kominami and Y Uchiyama

Department of Cell Biology and Neuroanatomy, School of Medicine, Iwate Medical University, Japan.

To understand the bone resorption and lysosomal proteinases in osteoclasts, we examined by immunohistochemistry the localization of lysosomal cysteine and aspartic proteinases, acid phosphatase, and cystatin-beta in the rat tibial bone. Immunoreactivity for cathepsins B, C, H, and L, cathepsin D, acid phosphatase, and cystatin-beta was demonstrated in various cells of the bone tissue; in particular, large multinucleated osteoclasts attached to the bone surface and chondroclasts in the proximal growth plate. These cells showed intense immunoreactivity for these lysosomal enzymes and cystatin-beta. Bone surface-lining osteoblasts displayed distinct immunoreactivity for cathepsins B, C, D, H, and acid phosphatase, while osteocytes often exhibited that for cathepsins D, H and acid phosphatase. Chondrocytes in the growth plate demonstrated intense immunoreactivity for cathepsins B, D, and acid phosphatase. Immunoreactivity for cystatin- beta was detected in osteoclasts and chondroclasts only. Large, round multinucleated cells free from the bone surface exhibited weak, faint, or no immunoreactivity for the lysosomal enzymes and cystatin-beta. These results suggest that lysosomal cysteine and aspartic proteinases may play a role in the degradation of organic constituents of the bone matrix. Moreover, cystatin-beta can serve as an excellent marker protein for osteoclasts.

Volume 41, Issue 7, pp. 1075-1083, 07/01/1993
Copyright © 1993 by The Histochemical Society


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