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J. Biol. Chem., Vol. 277, Issue 9, 7255-7261, March 1, 2002
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From the Kolling Institute of Medical Research, University
of Sydney, Royal North Shore Hospital, St. Leonards 2065, New South
Wales, Australia
We previously demonstrated in T47D cells
transfected to express the transforming growth factor-
Signaling through the Smad Pathway by Insulin-like Growth
Factor-binding Protein-3 in Breast Cancer Cells
RELATIONSHIP TO TRANSFORMING GROWTH FACTOR-
1
SIGNALING*
receptor type
II (TGF-RII) that insulin-like growth factor binding protein-3
(IGFBP-3) could stimulate Smad2 and Smad3 phosphorylation, potentiate
TGF-1-stimulated Smad phosphorylation, and cooperate with exogenous
TGF-1 in cell growth inhibition (Fanayan, S., Firth, S. M.,
Butt, A. J., and Baxter, R. C. (2000) J. Biol.
Chem. 275, 39146-39151). This study further explores IGFBP-3
signaling through the Smad pathway. Like TGF-1, natural and
recombinant IGFBP-3 stimulated the time- and dose-dependent
phosphorylation of TGF-RI as well as Smad2 and Smad3. This effect
required the presence of TGF-RII. IGFBP-3 mutated in
carboxyl-terminal nuclear localization signal residues retained
activity in TGF-R1 and Smad phosphorylation, whereas IGFBP-5 was
inactive. Immunoneutralization of endogenous TGF-1 suggested that
TGF-1 was not essential for IGFBP-3 stimulation of this pathway,
but it increased the effect of IGFBP-3. IGFBP-3, like TGF-1,
elicited a rapid decline in immunodetectable Smad4 and
Smad4·Smad2 complexes. IGFBP-3 and nuclear localization signal mutant IGFBP-3 stimulated the activation of the plasminogen activator inhibitor-1 promoter but was not additive with TGF-, suggesting that
this end point is not a direct marker of the IGFBP-3 effect on cell
proliferation. This study defines a signaling pathway for IGFBP-3 from
a cell surface receptor to nuclear transcriptional activity, requiring
TGF-RII but not dependent on the nuclear translocation of IGFBP-3.
The precise mechanism by which IGFBP-3 interacts with the TGF-
receptor system remains to be established.
*
This work was supported in part by grants from the
Kathleen Cuningham Foundation for Breast Cancer Research and the Leo & Jenny Leukemia and Cancer Foundation of Australia.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.
To whom correspondence should be addressed. Tel.: 61-2-9926-8486;
Fax: 61-2-9926-8484; E-mail: robaxter@med.usyd.edu.au.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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