Nucleic Acids Research, Vol 25, Issue 12 2424-2429, Copyright © 1997 by Oxford University Press
R Galien and T Garcia
Interleukin-6 (IL-6) is a multifunctional cytokine thought to be a key
factor in post-menopausal osteoporosis, given its ability to induce
osteoclast maturation and its down regulation by estrogens. We have
previously shown that the effects of TNFalphaand estradiol on the human
IL-6 promoter were dependent on a region of the promoter containing a C/EBP
site and a NF-kappaB site. To define the molecular mode of action of
estrogens, we performed gel shift assays with this DNA fragment as a probe,
and nuclear extracts from TNFalpha-induced HeLa, MCF7 and Saos2 cells.
Several induced complexes specifically bound the probe. The use of various
competitor DNA suggested that most of the complexes detected contained
NF-kappaB factors, and that C/EBP site binding factors were important for
the overall binding to the probe. Addition of in vitro translated human
estrogen receptor (hER) impaired the binding of three complexes in HeLa
cells and two complexes in MCF7 and Saos2 cells. Competition experiments
suggested that the NF-kappaB site was necessary for the effect of hER. The
use of antisera against NF-kappaB and C/EBP proteins showed that the target
complexes of hER contained the c-rel proto-oncogene product and to a lesser
extent, the RelA protein. Taken together, these data show that hER impairs
TNFalphainduction of IL-6 by preventing c-rel and, to a lesser extent, RelA
proteins binding to the NF-kappaB site of the IL-6 promoter.
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Estrogen receptor impairs interleukin-6 expression by preventing protein binding on the NF-kappaB site
Roussel Uclaf, 102 route de Noisy, 93235 Romainville Cedex, France. galien@mac.rousseluclaf.fr
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