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Papers In Press, published online ahead of print July 24, 2000
J. Biol. Chem, 10.1074/jbc.M003880200
Submitted on May 8, 2000
Revised on July 18, 2000
Accepted on July 24, 2000

Identification and characterization of a novel factor that regulates quinone reductase gene transcriptional activity

Monica M. Montano, Bryan M. Wittmann, and Nicole R. Bianco

Department of Pharmacology, Case Western Reserve University School of Medicine, Cleveland, OH 44106

Corresponding Author: mxm126{at}po.cwru.edu

The regulation of the Quinone Reductase (QR) gene, as well as other genes involved in detoxification, is known to be mediated by an electrophile/antioxidant response element (EpRE/ARE). We have previously observed that QR is up-regulated by the antiestrogen trans-hydroxytamoxifen in breast cancer cells. QR gene regulation by the antiestrogen-occupied estrogen receptor (ER) is mediated by the EpRE-containing region of the human QR gene and the ER is one of the complex of proteins that binds to the EpRE. In an effort to further understand the mechanism for ER regulation of QR gene we identified other protein factors that regulate QR gene transcriptional activity in breast cancer cells. One of these protein factors, hPMC2 (human homolog of Xenopus gene which Prevents Mitotic Catastrophe), directly binds to the EpRE and interacts with the ER in yeast genetic screening and in vitro assays. Interestingly hPMC2 interacts more strongly to ERbeta when compared to ERalpha . In transient transfection assays using reporter constructs containing the EpRE, hPMC2 alone can slightly activate reporter in estrogen receptor (ER)-negative MDA-MB-231 breast cancer cells. The activation of QR gene activity by hPMC2 is enhanced in the presence of ERbeta .


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