Mol Cell Endocrinol. 2009 Mar 25;301(1-2):51-8. doi: 10.1016/j.mce.2008.07.015. Epub 2008 Aug 3.

Steroid-converting enzymes in human ovarian carcinomas.

Chura JC, Ryu HS, Simard M, Poirier D, Tremblay Y, Brooker DC, Blomquist CH, Argenta PA.

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Department of Obstetrics, Gynecology and Women's Health, University of Minnesota, Minneapolis, MN, USA.

Abstract

Anti-estrogen therapies for treating ovarian carcinoma have had mixed outcomes suggesting some tumors may be estrogen-dependent. We assayed the activity levels of 17beta-hydroxysteroid dehydrogenase (17beta-HSD), 3beta-hydroxysteroid dehydrogenase (3beta-HSD), 3alpha-hydroxysteroid dehydrogenase (3alpha-HSD/3-KSR) and estrone sulfatase in a series of ovarian epithelial carcinomas. 17beta-HSD activity ratios with estradiol (E(2)) and testosterone (T), and inhibition by isoform-specific inhibitors were used to estimate the contributions of 17beta-HSD isoforms. Activity levels were highest for estrone sulfatase, followed, respectively by 17beta-HSD, 3alpha-HSD/3-KSR, and 3beta-HSD. E(2)/T activity ratios varied widely between samples. A 17beta-HSD type 1 inhibition pattern was observed in 23% of the samples and a type 2 pattern in 25%. E(2) formation from estrone sulfate (E(1)S) was detected in 98% (47/48) of the samples. 17beta-HSD type 1, type 2 and type 5 mRNA was detected in matched primary tumor and metastases. Evaluation of 17beta-HSD and sulfatase activity levels, activity ratios and inhibition patterns may help predict tumor response to endocrine therapy.

PMID:: 18723074; [PubMed - indexed for MEDLINE]

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Steroid-converting enzymes in human ovarian carcinomas.
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Mol Cell Endocrinol. 2009 Mar 25 ;301(1-2):51-8. doi: 10.1016/j.mce.2008.07.015. Epub 2008 Aug 3 .

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