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Laboratoire de Chimie Physiologique, Universite de Louvain, and International Institute of Cellular and Molecular Pathology B-1200 Bruxelles, Belgium
Address requests for reprints to: Dr. Jean-Marie Delaisse, UCL 75.39, Avenue Hippocrate, 75, B-1200 Bruxelles, Belgium.
Abstract
The participation of collagenase in bone resorption has been investigated by assaying the procollagenase extracted from fetal mouse calvaria cultured under a variety of conditions, and by evaluating its ability to degrade bone collagen. Procollagenase was found in two separate pools, one requiring demineralization for its extraction, the other not. Culturing the bones with PTH, 1,25-dihydroxyvitamin D3, prostaglandin E2, interleukin-1, tumor necrosis factor-
, catabolin, retinoic acid, or endotoxin (but not with heparin) induced resorption, enhanced lysosomal enzyme release, and markedly increased the procollagenase content of the second pool. The PTH-induced increase in procollagenase was dose dependent and paralleled the extent of calcium loss and lysosomal enzyme release. The increase in procollagenase was found in bone, periosteum, and sutures, where its distribution was similar to that of nonmineralized collagen. The increase in procollagenase was abolished by cycloheximide, but not by indomethacin, hydroxyurea, glucocorticoids, acetazolamide, bisphosphonates, or calcitonin. Calcitonin and bisphosphonates almost completely inhibited the PTH-induced Ca loss and lysosomal enzyme release, but only partially inhibited the PTH-induced loss of collagen. The latter was, however, completely prevented by the collagenase inhibitor, CI-1. CI-1 also partially inhibited the PTH-induced Ca loss. Moreover, collagen degradation occurred in PTH-precultured calvaria (but not in noncultured controls) when incubated in a buffer under nonviable and nondemineralizing conditions. This degradation was inhibited by collagenase inhibitors, either CI-1 or the natural tissue inhibitor of metalloproteinases. This work thus indicates that the resorption of fetal bone explants proceeds along with an accumulation of procollagenase, primarily within their nonmineralized matrix. Moreover the results suggest that collagenase is likely to participate in the degradation of the nonmineralized collagen of the bone explants. Whether it also participates in the degradation of the collagen of the mineralized matrix remains to be elucidated. (Endocrinology 123: 264–276, 1988)
Footnotes
* A von Recklinghausen Prize (1987) of the German Society for Endocrinology was awarded to J. M. Delaisse for a preliminary draft of this paper which was communicated also at the 1987 Annual Meeting of the American Society for Bone and Mineral Research Indianapolis, IN (J Bone Miner Res 2 [Suppl 1]:49 (Abstract). This work was supported by the National Fund for Scientific Medical Research (Belgium).
Research Associate of the National Fund for Scientific Research (Belgium).
Received December 27, 1987.
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