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Title: A new synthetic inhibitor of mammalian tissue collagenase inhibits bone resorption in culture. Author: Delaissé JM, Eeckhout Y, Sear C, Galloway A, McCullagh K, Vaes G. Journal: Biochem Biophys Res Commun; 1985 Dec 17; 133(2):483-90. PubMed ID: 3002346. Abstract: A specific and potent synthetic inhibitor of mammalian tissue collagenase and related metallo-proteinases inhibits the collagen matrix resorption induced by parathyroid hormone (PTH) in cultured embryonic mouse calvaria. The inhibition is reversible, dose-dependent and virtually complete at 50 microM inhibitor concentration whereas that due to a less potent stereoisomer is much weaker. The PTH-enhanced secretion of calvarial lysosomal enzymes and the small spontaneous leakage of lactate dehydrogenase are not affected by the inhibitor. These results suggest that collagenase plays a critical role in bone resorption. Its role is discussed in relation to that of cysteine-proteinases that have also been implicated in this process.[Abstract] [Full Text] [Related] [New Search]