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J Biol Chem, Vol. 274, Issue 10, 6783-6789, March 5, 1999
From the Platelet-derived growth factor (PDGF) BB, a
mitogen that stimulates bone resorption, increases the expression of
interleukin-6 (IL-6), a cytokine that induces osteoclast recruitment.
The mechanisms involved in IL-6 induction by PDGF BB are poorly
understood. We examined the effect of PDGF BB on IL-6 expression in
cultures of osteoblasts from fetal rat calvariae (Ob cells). PDGF BB
increased IL-6 mRNA and heterogeneous nuclear RNA levels, the rate
of transcription, and the activity of base pairs (bp)
Platelet-derived Growth Factor Induces Interleukin-6
Transcription in Osteoblasts through the Activator Protein-1 Complex
and Activating Transcription Factor-2
,,, and¶
Departments of Research and Medicine, Saint
Francis Hospital and Medical Center, Hartford, Connecticut 06105 and
the ¶ University of Connecticut School of Medicine,
Farmington, Connecticut 06030
2906 to +20
IL-6 promoter fragments transiently transfected into Ob cells. Deletion
analysis revealed two responsive regions, one containing an activator
protein-1 (AP-1) site located between bp 276 and 257, and a second,
less well defined, downstream of 257. Targeted mutations of a cyclic AMP-responsive element (CRE), and nuclear factor-IL-6 and nuclear factor-
B binding sites in a bp 257 to +20 IL-6 construct that was
transfected into Ob cells, revealed that the CRE also contributed to
IL-6 promoter induction by PDGF BB. Electrophoretic mobility shift
assay revealed AP-1 and CRE nuclear protein complexes that were
enhanced by PDGF BB. Supershift assays revealed binding of Jun and Fos
to AP-1 and CRE sequences and binding of activating transcription
factor-2 to CRE. In conclusion, PDGF BB induces IL-6 transcription in
osteoblasts by regulating nuclear proteins of the AP-1 complex and
activating transcription factor-2.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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