In vivo and in vitro evidence for the involvement of cysteine proteinases in bone resorption.
J M Delaissé, Y Eeckhout, G Vaes
Index: Biochem. Biophys. Res. Commun. 125 , 441, (1984)
Full Text: HTML
Abstract
The excretion of cathepsin B, a lysosomal cysteine proteinase, by parathyroid hormone-stimulated embryonic mouse calvaria in culture, correlates closely with the extent of bone resorption evaluated by the loss of hydroxyproline and calcium and by the extension of resorption lacunae. E-64, a specific inhibitor of cysteine proteinases, inhibits reversibly the resorption of cultured bones without affecting the hormone-induced secretion of lysosomal hydrolases. Given in vivo to rats, the proteinase inhibitors, E-64 and leupeptin, both induce a concomitant fall in the serum calcium level and in the urinary excretion of hydroxyproline. These results provide evidence that cysteine proteinases, possibly lysosomal cathepsins, are necessary for bone resorption.
Related Compounds
Related Articles:
A simple, economical method for staining gels for cathepsin B-like activity.
1982-01-01
[Anal. Biochem. 119 , 148, (1982)]