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Journal of Clinical Endocrinology & Metabolism, Vol 58, 368-373, Copyright © 1984 by Endocrine Society


ARTICLES

Estrogen sulfoconjugation by human endometrial cancer cells (RL95-2) in culture

DS Grosso and BR Larsen

Estrogen metabolism was studied in a newly established cell line (RL95- 2) derived from a human endometrial carcinoma. Estradiol and estrone were metabolized to water-soluble derivatives by cells under in vitro culture conditions. Between 80-90% of the added steroids were metabolized, with nearly quantitative recovery of the products from the incubation medium. Arylsulfatase treatment converted the metabolites to ether-soluble forms, whereas beta-glucuronidase had no effect on the aqueous solubility of these compounds. Butanol extracts of the water- soluble estradiol metabolites cochromatographed on high performance liquid chromatography with 17 beta-estradiol-3-sulfate (93.6%) or estrone-3-sulfate (3.5%). No more than 6% of the estradiol added to the incubation medium was recovered in the form of estrone, either as estrone or estrone sulfate. After arylsulfatase treatment of the estradiol conjugates, 92% of the ether-soluble radioactivity cochromatographed with estradiol, and 3.8% cochromatographed with estrone. Estrogen-sulfurylating activity was localized in the cytosol of subcellular fractions of RL95-2 cells. The sulfoconjugation of estrogens by RL95-2 cells may prove useful as a model for the investigation of estrogen metabolism in endometrial carcinoma cells.


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J. Clin. Endocrinol. Metab.Home page
X.-H. Li, H. Li, Z.-J. Xiao, and Y.-S. Piao
Divergent Effects of Retinoic Acids on the Expression of ER{alpha} and 17{beta}-Hydroxysteroid Dehydrogenase Type 2 in Endometrial Carcinoma Cells (RL 95-2)
J. Clin. Endocrinol. Metab., February 1, 2002; 87(2): 640 - 649.
[Abstract] [Full Text] [PDF]




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