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J. Biol. Chem., Vol. 275, Issue 50, 39237-39245, December 15, 2000
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From the Transforming growth factor-
Synergistic Cooperation between Sp1 and Smad3/Smad4 Mediates
Transforming Growth Factor
1 Stimulation of 
2(I)-Collagen
(COL1A2) Transcription*
,,, and¶
Brookdale Center, Department of Biochemistry
and Molecular Biology, Mount Sinai School of Medicine, New York
University, New York, New York 10029 and the § Department of
Internal Medicine and Clinical Research Institute, National Kanazawa
Hospital, Kanazawa, 920-8650 Japan
1 (TGF) is a
strong activator of extracellular matrix accumulation. TGF
stimulates the gene coding for human 
2(I)-collagen (COL1A2) by
inducing binding of an Sp1-containing complex to an upstream promoter
element (TGF responsive element or TbRE) that contains a CAGA box.
Here we report that the CAGA box of the TbRE is the binding site of the Smad3/Smad4 complex, and that the binding of the complex is
required for TGF-induced COL1A2 up-regulation. Recombinant Smad3 and
Smad4 bind in vitro to the CAGA box of COL1A2; TGF
treatment of cultured fibroblasts induces Smad3/Smad4 binding to the
TbRE; transient overexpression of Smad3 and Smad4 in fibroblasts
transactivates TbRE-driven transcription; and COL1A2 gene up-regulation
by TGF is abolished in cells stably transfected with plasmids that
express dominant negative forms of Smad3 or Smad4. In Sp1-deficient
Drosophila Schneider cells, there was cooperative synergy
between Smad3/Smad4 and Sp1 at the TbRE site. The analysis also
emphasized the requirement of both Sp1- and Smad-binding sites for
optimal promoter transactivation. In cells stably transfected with a
plasmid expressing a dominant negative form of Sp1, the synergy was
shown to be promoter-specific and dependent on the binding of Sp1 to
the TbRE. Interestingly, overexpression of dominant negative Sp1 was
found to block the antagonistic signal of tumor necrosis factor- on
COL1A2 transcription, as well. These results provide the first linkage
between the Smad3 and Smad4 proteins and TGF stimulation of type I
collagen biosynthesis.
*
This work was supported by National Institutes of Health
Grants AR-386481 and AA12196 and the Arthritis Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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