Inhibition of bone resorption in culture by inhibitors of thiol proteinases
- 15 October 1980
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 192 (1) , 365-368
- https://doi.org/10.1042/bj1920365
Abstract
Leupeptin, antipain, tosyl-lysylchloromethane (Tos-Lys-CH2Cl) and benzyloxycarbonylphenylalanylalanyldiazomethane (Z-Phe-Ala-CHN2) inhibit reversibly the resorption induced by parathyroid hormone or heparin in cultured mouse bones. Leupeptin and antipain do not affect collagenase production and activity or the enhanced secretion of .beta.-glucuronidase induced by the bone-resorbing agents. They might thus act by a direct (extracellular?) inhibition of lysosomal thiol proteinases.This publication has 9 references indexed in Scilit:
- The inhibition of macrophage protein turnover by a selective inhibitor of thiol proteinasesBiochemical Journal, 1980
- Collagenase, procollagenase and bone resorption effects of heparin, parathyroid hormone and calcitoninBiochimica et Biophysica Acta (BBA) - General Subjects, 1979
- Purification of Bovine Spleen Collagenolytic Cathepsin (Cathepsin N)Biochemical Society Transactions, 1978
- Proteolytic Enzymes, Cell Surface Changes, and Viral TransformationPublished by Elsevier ,1976
- Cathepsin B1. A lysosomal enzyme that degrades native collagenBiochemical Journal, 1974
- The release of collagenase as an inactive proenzyme by bone explants in cultureBiochemical Journal, 1972
- ON THE MECHANISMS OF BONE RESORPTIONThe Journal of cell biology, 1968
- Glycosidases in the nervous system. I. Assay, some properties, and distribution of beta-galactosidase, beta-glucoronidase, and beta-glucosidase.1968
- Excretion of acid and of lysosomal hydrolytic enzymes during bone resorption induced in tissue culture by parathyroid extractExperimental Cell Research, 1965