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(Received for publication, August 31, 1996, and in revised form, March 24, 1997)
From the Department of Molecular and Cellular Biology, Roswell Park
Cancer Institute, Buffalo, New York 14263
Haptoglobin (HP) is one of the major acute phase
plasma proteins in the mouse, and its synthesis is additively induced
by interleukin (IL)-6 and glucocorticoids. STAT3 serves as the mediator of the IL-6 receptor signal and appears to contribute to the
transcriptional induction of acute phase protein genes. The
carboxyl-terminal region of STAT3, consisting of an acidic domain and
containing a serine phosphorylation site, has been proposed to
contribute to the induction process. To assess the role of STAT3 in the
transcriptional control of the HP promoter, we applied two mutant forms
of STAT3: one with a deletion of the carboxyl-terminal 55 amino acid
residues, STAT3
Volume 272, Number 23,
Issue of June 6, 1997
pp. 14571-14579
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
55C, and the other with a substitution of serine 727 to alanine, STAT3SA. Like the wild-type STAT3, both mutant STAT3 forms
are activated by the signal-transducing subunit of the IL-6 receptor,
gp130, or by co-transfected IL-3 receptor. Ectopic expression and
activation of wild-type STAT3 or STAT3SA in HepG2 hepatoma cells
similarly enhance transcription through the IL-6-response element of
the HP promoter. This enhancement is specific for STAT3 and cannot be
reproduced by STAT1 or STAT5. In contrast, STAT355C inhibits
IL-6-induced transcriptional activation. Interestingly, whereas
receptor-activated STAT3 also enhances stimulation of the haptoglobin
promoter by dexamethasone through the glucocorticoid receptor,
activated STAT355C reduces the regulation below the level achieved
by the glucocorticoid receptor alone. This transdominant action by
STAT355C is dependent on a functional IL-6-responsive element. The
data suggest that the carboxyl-terminal domain, but not its serine
phosphorylation site of STAT3, is required for transcription as part of
the hematopoietin receptor signaling as well as for cooperation with
other transcription factors such as the glucocorticoid receptor.
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