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J Biol Chem, Vol. 274, Issue 18, 12933-12938, April 30, 1999
1 Induces Interleukin-6 Expression
via Activating Protein-1 Consisting of JunD Homodimers in Primary Human
Lung Fibroblasts
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From the Transforming growth factor (TGF)- Department of Research and Internal
Medicine, University Hospital, 4031 Basel, Switzerland and The
Netherlands Cancer Institute, Division of Molecular Biology,
Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands
1 induces
extracellular matrix deposition and proliferation of mesenchymal cells.
We recently reported that interleukin (IL)-6 is an essential mediator
of growth factor-induced proliferation of lung fibroblasts. Here, we
demonstrate by reverse transcriptase polymerase chain reaction and
enzyme-linked immunoassay that TGF-1 is a potent inducer of IL-6
mRNA and protein in primary human lung fibroblasts. Transient
transfections of fibroblasts with a luciferase reporter gene construct
containing nucleotides 
651 to +1 of the human IL-6 promoter revealed
that TGF-1 also potently activated IL-6 promoter activity.
Progressive 5'-deletions and site-directed mutagenesis of the parental
construct located the TGF-1-responsive cis-regulatory
element to a known activating protein-1 (AP-1) sequence (nucleotides
284 to 276). Gel shift analyses revealed that AP-1 DNA binding
activity in nuclear extracts was increased 30 min after stimulation
with TGF-1. In contrast, neither CCAAT enhancer-binding protein-,
NF-
B, nor Sp1 were activated by TGF-1. Supershift analyses
demonstrated that the AP-1 complex induced by TGF-1 was composed of
Jun isoforms and absent of Fos isoforms. Moreover, this complex was
found to be a JunD homodimer. Our data thus demonstrate that TGF-1
is a potent inducer of IL-6 in primary human lung fibroblasts. The TGF-1-activated JunD homodimer may be essential for a majority of
the biological effects induced by TGF-1 in this cell type, such as
proliferation and extracellular matrix synthesis.
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