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J Biol Chem, Vol. 273, Issue 10, 5506-5513, March 6, 1998

Transforming Growth Factor-beta Stimulates Interleukin-11 Transcription via Complex Activating Protein-1-dependent Pathways

Weiliang TangDagger , Liu Yang§, Yu-Chung Yang§, Shawn X. LengDagger , and Jack A. EliasDagger

From the Dagger  Section of Pulmonary and Critical Care Medicine, Yale University School of Medicine, Department of Internal Medicine, New Haven, Connecticut 06520-8057 and § Indiana University School of Medicine, Departments of Medicine (Hematology/Oncology), and Biochemistry/Molecular Biology, Walther Oncology Center, Indianapolis, Indiana 46202

Studies were undertaken to characterize the mechanism by which transforming growth factor-beta 1 (TGF-beta 1) stimulates epithelial cell interleukin (IL)-11 production. Nuclear run-on studies demonstrated that TGF-beta 1 is a potent stimulator of IL-11 gene transcription. TGF-beta 1 also stimulated the luciferase activity in cells transfected with reporter gene constructs containing nucleotides -728 to +58 of the IL-11 promoter. Studies with progressive 5' deletion constructs and site-specific mutations demonstrated that this stimulation was dependent on 2 AP-1 sites between nucleotides -100 and -82 in the IL-11 promoter. Mobility shift assays demonstrated that TGF-beta 1 stimulated AP-1 protein-DNA binding to both AP-1 sites. Supershift analysis demonstrated that JunD was the major moiety contributing to AP-1-DNA binding in unstimulated cells and that c-Jun-, Fra-1-, and Fra-2-DNA binding were increased whereas JunD-DNA binding was decreased in TGF-beta 1-stimulated cells. The sequence in the IL-11 promoter that contains the AP-1 sites also conferred TGF-beta 1 responsiveness, in a position-independent fashion, on a heterologous minimal promoter. Thus, TGF-beta 1 stimulates IL-11 gene transcription via a complex AP-1-dependent pathway that is dependent on 2 AP-1 motifs between nucleotides -100 and -82 that function as an enhancer in the IL-11 promoter.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.


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