Cysteine protease production by human osteosarcoma cells (MG63, SAOS2) andits modulation by soluble factors

Citation
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
Citations number
15
Categorie Soggetti
Cell & Developmental Biology
Journal title
CYTOKINE
ISSN journal
10434666 → ACNP
Volume
12
Issue
5
Year of publication
2000
Pages
539 - 542
Database
ISI
SICI code
1043-4666(200005)12:5<539:CPPBHO>2.0.ZU;2-L
Abstract
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.