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Originally published In Press as doi:10.1074/jbc.M202561200 on April 18, 2002

J. Biol. Chem., Vol. 277, Issue 27, 24571-24578, July 5, 2002
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Transforming Growth Factor-beta Stimulates Parathyroid Hormone-related Protein and Osteolytic Metastases via Smad and Mitogen-activated Protein Kinase Signaling Pathways*

Sanna-Maria KäkönenDagger , Katri S. SelanderDagger , John M. Chirgwin§, Juan Juan YinDagger , Suzanne Burns§, Wayne A. RankinDagger , Barry G. GrubbsDagger , Mark DallasDagger , Yong CuiDagger , and Theresa A. GuiseDagger

From the Dagger  Department of Molecular Medicine, University of Texas Health Science Center at San Antonio, Institute for Drug Development, Cancer Therapy and Research Center, and the § Veterans Administration Research Service, San Antonio, Texas 78245-3217

Transforming growth factor (TGF)-beta promotes breast cancer metastasis to bone. To determine whether the osteolytic factor parathyroid hormone-related protein (PTHrP) is the primary mediator of the tumor response to TGF-beta , mice were inoculated with MDA-MB-231 breast cancer cells expressing a constitutively active TGF-beta type I receptor. Treatment of the mice with a PTHrP-neutralizing antibody greatly decreased osteolytic bone metastases. There were fewer osteoclasts and significantly decreased tumor area in the antibody-treated mice. TGF-beta can signal through both Smad and mitogen-activated protein (MAP) kinase pathways. Stable transfection of wild-type Smad2, Smad3, or Smad4 increased TGF-beta -stimulated PTHrP secretion, whereas dominant-negative Smad2, Smad3, or Smad4 only partially reduced TGF-beta -stimulated PTHrP secretion. When the cells were treated with a variety of protein kinases inhibitors, only specific inhibitors of the p38 MAP kinase pathway significantly reduced both basal and TGF-beta -stimulated PTHrP production. The combination of Smad dominant-negative blockade and p38 MAP kinase inhibition resulted in complete inhibition of TGF-beta -stimulated PTHrP production. Furthermore, TGF-beta treatment of MDA-MB-231 cells resulted in a rapid phosphorylation of p38 MAP kinase. Thus, the p38 MAP kinase pathway appears to be a major component of Smad-independent signaling by TGF-beta and may provide a new molecular target for anti-osteolytic therapy.

* This work was supported by National Institutes of Health Grant CA69158 and United States Army Department of Defense Grant DAMD17-99-1-9401 (to T. A. G.); a grant from the Veterans Administration Research Service (to J. M. C.); and grants from the Academy of Finland, the Finnish Cultural Foundation, and Maud Kuistila Foundation and United States Army Department of Defense Grant DAMD17-99-1-9403 (to S. M. K.).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: Dept. of Molecular Medicine, University of Texas Health Science Center at San Antonio and Institute for Drug Development, Cancer Therapy and Research Center, 14960 Omicron Dr., San Antonio, TX 78245-3217. Tel.: 210-677-3855; Fax: 210-677-3889; E-mail: guise@uthscsa.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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