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Identification and Characterization of a Functionally Distinct Form of Human Estrogen Receptor ß

Department of Atherosclerosis and Endocrinology, Merck Research Laboratories (H.A.W., H.L., J.Y., S.C., J.M.S., S.W.M.), Rahway, New Jersey 07065; Karo Bio AB (J.D., S.N.), Novum, S-141 57 Huddinge, Sweden

Address all correspondence and requests for reprints to: Hilary Anne Wilkinson, Ph.D., Merck Research Laboratories, Department of Atherosclerosis and Endocrinology, RY80Y-305, 126 East Lincoln Avenue, Rahway, New Jersey 07065. E-mail: hilary_wilkinson{at}merck.com

Estrogen receptors are important for the development and maintenance of many different tissues in the body including the breast, uterus, brain and bone. There are two known genes encoding estrogen receptors, Estrogen Receptor alpha (ER) and Estrogen Receptor beta (ERß). These receptors are transcription factors with distinct functional domains involved in DNA binding, ligand binding and transcriptional regulation. A novel isoform of human ERß (ERß548) which includes an extended amino terminal domain has been identified. Isoform specific antibodies confirm the presence of this receptor in human tissue. Transactivation analysis with different estrogenic ligands indicates that ERß548 is functionally distinct from previously reported forms of ERß.

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