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Papers In Press, published online ahead of print April 30, 2002
J. Biol. Chem, 10.1074/jbc.M203039200
Submitted on March 28, 2002
Revised on April 26, 2002
Accepted on April 30, 2002

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 Qi, Rocky Pramanik, Jintang Wang, Richard M. Schultz, Ratan K. Maitra, Jiahuai Han, Hector F. DeLuca, and Guan Chen

Department of Radiation Oncology, Loyola University Medical Center, Maywood, IL 60153

Corresponding Author: gchen1{at}lumc.edu

The signaling connection between 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 (MKK6) 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 MKK6 also activates VDR and sensitizes MCF-7 cells to vitamin D3-dependent growth inhibition. Both the p38 and JNK MAPK pathways, and the down-stream 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 a 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 in regulation of cell growth by the MAPK pathways through their regulation of vitamin D3/VDR activity.


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