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Endocrinology Vol. 142, No. 7 3177-3186
Copyright © 2001 by The Endocrine Society

ARTICLES

Quantitative Analysis of Estrogen Receptor Proteins in Rat Mammary Gland1

Shigehira Saji2, Hideki Sakaguchi, Sandra Andersson, Margaret Warner and Jan-Åke Gustafsson

Department of Medical Nutrition (S.S., H.S., S.A., J.-Å.G.), Department of Bioscience (M.W., J.-Å.G.), Karolinska Institute, Novum, S141–86 Huddinge, Sweden

Address all correspondence and requests for reprints to: Dr. Jan-Åke Gustafsson, Department of Medical Nutrition, Karolinska Institute, F60, Novum, S141–86 Huddinge, Sweden. E-mail: jan-ake.gustafsson{at}mednut.ki.se

Estrogen receptor {alpha} and ß proteins (ER{alpha} and ERß) at various stages of development of the rat mammary gland were quantified by Western blotting. ER{alpha} and ERß recombinant proteins were used as standards, and their molar concentrations were measured by ligand binding assays. In 3-week-old pregnant, lactating, and postlactating rats the ER{alpha} content ranged from 0.30–1.55 fmol/µg total protein (mean values). The ERß content of the same samples ranged between 1.06–7.50 fmol/µg total protein. At every developmental stage, the ERß content of the mammary gland was higher than that of ER{alpha}. When receptor levels were normalized against ß-actin, it was evident that ER expression changed during development, with maximum expression of both receptors during the lactation period. With an antibody raised against the 18-amino acid insert of the ERß variant, originally called ERß2 but named ERßins in this paper, Western blots revealed that ERßins protein was up-regulated during the lactation period. RT-PCR showed that the levels of messenger RNA of ERßins paralleled those of the protein. Double immunohistochemical staining with anti-ER{alpha} and anti-ERßins antibodies revealed that ERßins protein colocalized with ER{alpha} in 70–80% of the ER{alpha}-expressing epithelial cells during lactation and with 30% of these cells during pregnancy. These observations indicate that expression of ERßins is regulated not only quantitatively, but also with regard to its cellular distribution. As ERßins acts as the dominant repressor of ER{alpha}, we suggest that its coexpression with ER{alpha} quenches ER{alpha} function and may be one of the factors that contribute to the previously described insensitivity of the mammary gland to estrogens during lactation.




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