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Originally published In Press as doi:10.1074/jbc.M203039200 on April 30, 2002

J. Biol. Chem., Vol. 277, Issue 29, 25884-25892, July 19, 2002
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The p38 and JNK Pathways Cooperate to trans-Activate Vitamin D Receptor via c-Jun/AP-1 and Sensitize Human Breast Cancer Cells to Vitamin D3-induced Growth Inhibition*

Xiaomei QiDagger §, Rocky PramanikDagger §, Jintang WangDagger , Richard M. Schultz, Ratan K. Maitra||, Jiahuai Han**, Hector F. DeLucaDagger Dagger , and Guan ChenDagger §§

From the Dagger  Department of Radiation Oncology and the  Division of Biochemistry of the Department of Cell Biology, Neurobiology, and Anatomy, Loyola University of Chicago, Maywood, Illinois 60153, the || Department of Virology, The Cleveland Clinic Foundation, Cleveland, Ohio 44195, the ** Department of Immunology, The Scripps Research Institute, La Jolla, California 92037, and the Dagger Dagger  Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706-1544

The signaling connection between mitogen-activated protein kinases(MAPKs) and nuclear steroid receptors is complex and remains mostly unexplored. Here we report that stress-activated protein kinases p38 and JNK trans-activate nuclear steroid vitamin D receptor (VDR) gene and increase vitamin D3-dependent growth inhibition in human breast cancer cells. Activation of p38 and JNK by an active MAPK kinase 6 stimulates VDR promoter activity independently of the ligand vitamin D3 and estrogen receptor expression. Moreover, stimulation of the endogenous stress pathways by adenovirus-mediated delivery of recombinant MAPK kinase 6 also activates VDR and sensitizes MCF-7 cells to vitamin D3-dependent growth inhibition. Both the p38 and JNK MAPK pathways and the downstream transcription factor c-Jun/AP-1 are required for the VDR stimulation, as revealed by application of their dominant negatives, the specific p38 inhibitor SB203580, and site-directed mutagenesis of the AP-1 element in the VDR promoter. The essential role of the p38 and JNK stress pathways in up-regulation of VDR expression is further confirmed by using the chemical stimulator arsenite. These results establish a signaling connection between the stress MAPK pathways and steroid hormone receptor VDR expression and thereby offer new insights into regulation of cell growth by the MAPK pathways through regulation of vitamin D3/VDR activity.

* This work was supported in part by National Institutes of Health Grants CA91576 (to G. C.) and GM51417 (to J. H.).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.

§ Both authors contributed equally to this work.

§§ To whom correspondence should be addressed: Dept. of Radiation Oncology, Loyola University of Chicago, 114B-Bldg. 1 (Hines), 2160 S. First Ave., Maywood, IL 60153. Tel.: 708-202-8387 (ext. 23398); Fax: 708-202-2019; E-mail: gchen1@lumc.edu.

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