Recombinant human interleukin-1 beta, a mediator of osteoblastic cell function, was found to regulate the expression of the cell adhesion receptors, integrins, on human osteosarcoma cells. Interleukin-1 beta (IL-1 beta) at picomolar concentrations, specifically elevated approximately six- to tenfold
Recombinant human interleukin-1 inhibits the induction by dexamethasone of alkaline phosphatase activity in murine capillary endothelial cells
✍ Scribed by Mary A. Mulkins; Anthony C. Allison
- Publisher
- John Wiley and Sons
- Year
- 1987
- Tongue
- English
- Weight
- 645 KB
- Volume
- 133
- Category
- Article
- ISSN
- 0021-9541
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✦ Synopsis
A mutual antagonism exists between interleukin-Is (IL-Is) as pro-inflammatory and glucocorticoids as anti-inflammatory mediators. This report examines the effects of IL-1 on the induction by dexamethasone of alkaline phosphatase in LEI1 murine endothelial cells. Dexamethasone increases the specific activity of alkaline phosphatase in a time-and dose-dependent fashion (maximum 14fold induction at M), and this induction can be completely inhibited by simultaneous incubation with picomolar concentrations of recombinant human IL-la or IL-10. This IL-I-mediated antagonism of dexamethasone activity is not due to a down-regulation of glucocorticoid receptors in t h e cell line used, because the number of receptors and their affinity for dexamethasone is unchanged in IL-I-treated cells. However, induction of alkaline phosphatase by dexamethasone in LEI1 cells is receptor-mediated, since it can also be inhibited by glucocorticoid-receptor antagonists.
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