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Originally published In Press as doi:10.1074/jbc.M002188200 on May 17, 2000

J. Biol. Chem., Vol. 275, Issue 30, 22769-22779, July 28, 2000
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Inhibition of Vascular Endothelial Growth Factor Expression in HEC1A Endometrial Cancer Cells through Interactions of Estrogen Receptor alpha  and Sp3 Proteins*

Matthew StonerDagger , Fan WangDagger , Mark WormkeDagger , Thu NguyenDagger , Ismael SamudioDagger , Carrie VyhlidalDagger , Dieter MarmeDagger , Gunter Finkenzeller§, and Stephen SafeDagger

From the Dagger  Department of Veterinary Physiology and Pharmacology, Texas A&M University, College Station, Texas 77843-4466 and the § Institute of Molecular Medicine, Tumor Biology Center, D-79106 Freiburg, Germany

Treatment of HEC1A endometrial cancer cells with 10 nM 17beta -estradiol (E2) resulted in decreased vascular endothelial growth factor (VEGF) mRNA expression, and a similar response was observed using a construct, pVEGF1, containing a VEGF gene promoter insert from -2018 to +50. In HEC1A cells transiently transfected with pVEGF1 and a series of deletion plasmids, it was shown that E2-dependent down-regulation was dependent on wild-type estrogen receptor alpha  (ERalpha ) and reversed by the anti-estrogen ICI 182,780, and this response was not affected by progestins. Deletion analysis of the VEGF gene promoter identified an overlapping G/GC-rich site between -66 to -47 that was required for decreased transactivation by E2. Protein-DNA binding studies using electrophoretic mobility shift and DNA footprinting assays showed that both Sp1 and Sp3 proteins bound this region of the VEGF promoter. Coimmunoprecipitation and pull-down assays demonstrated that Sp3 and ERalpha proteins physically interact, and the interacting domains of both proteins are different from those previously observed for interactions between Sp1 and ERalpha proteins. Using a dominant negative form of Sp3 and transcriptional activation assays in Schneider SL-2 insect cells, it was confirmed that ERalpha -Sp3 interactions define a pathway for E2-mediated inhibition of gene expression, and this represents a new mechanism for decreased gene expression by E2.

* This work was supported by National Institutes of Health Grants CA76636 and ES09106 and a grant from the Texas Agricultural Experiment Station.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.

A Sid Kyle Professor of Toxicology. To whom correspondence should be addressed. Tel.: 409-845-5988; Fax: 409-862-4929; E-mail: ssafe@cvm.tamu.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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