Steroid-converting enzymes in human ovarian carcinomas

Justin C. Chura, Hyung S. Ryu, Marc Simard, Donald Poirier, Yves Tremblay, Doris C. Brooker, Charles H. Blomquist, Peter A Argenta

Research output: Contribution to journalArticlepeer-review

18 Scopus citations


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

Original languageEnglish (US)
Pages (from-to)51-58
Number of pages8
JournalMolecular and Cellular Endocrinology
Issue number1-2
StatePublished - Mar 25 2009


  • 17β-Hydroxysteroid dehydrogenase
  • 3α-Hydroxysteroid dehydrogenase
  • 3β-Hydroxysteroid dehydrogenase
  • Estrone sulfatase
  • Ovarian cancer
  • Steroid metabolism

Fingerprint Dive into the research topics of 'Steroid-converting enzymes in human ovarian carcinomas'. Together they form a unique fingerprint.

Cite this