C. Damiens et al., Cysteine protease production by human osteosarcoma cells (MG63, SAOS2) andits modulation by soluble factors, CYTOKINE, 12(5), 2000, pp. 539-542
The production of cysteine protease by two human osteosarcoma cell lines (M
G-63 and SaOS2) was analyzed, as well as their modulation by interleukin 1
beta (hIL-1 beta), interleukin 6 (hIL-6), insulin growth factor-1 (hIGF-1),
oncostatin M (hOSM), leukemia inhibitory factor (hLIF) and growth hormone
(hGH), Cysteine protease activities were detected using a synthetic substra
te. The protease activities (especially cathepsin L activity) of both cell
lines were increased significantly in the presence of hIL-1 beta, hIL-6 and
hOSM, In contrast, hIGF-1 and hGH decreased these activities, and no effec
t was detectable in the presence of hLIF. The addition of antibodies agains
t the gp-130 chain of the hIL-6 and hOSM receptors totally inhibited the st
imulating effect of these two cytokines on cysteine protease activities. In
increasing collagen type I degradation, hIL-1 beta, hIL-6 and hOSM could b
e involved in bone resorption, whereas the inhibitory action of hIGF-1 and
hGH on collagen type I degradation suggest that this factor could play a ro
le in bone formation. (C) 2000 Academic Press.