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

doi:10.1016/j.mce.2008.07.015

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 journal › Article › peer-review

22 Scopus citations

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 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 (E₂) 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. E₂/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%. E₂ formation from estrone sulfate (E₁S) 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 language	English (US)
Pages (from-to)	51-58
Number of pages	8
Journal	Molecular and Cellular Endocrinology
Volume	301
Issue number	1-2
DOIs	https://doi.org/10.1016/j.mce.2008.07.015
State	Published - Mar 25 2009

Bibliographical note

Funding Information:
This project was supported by a grant from the Susan G. Komen Foundation, and the Gynecologic Cancer Foundation. The authors are grateful to Linda Sackett-Lundeen, B.S.M.T. and Doris Sackett for their help with the figures.

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

SDG 3 Good Health and Well-being

Keywords

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

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10.1016/j.mce.2008.07.015

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title = "Steroid-converting enzymes in human ovarian carcinomas",

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 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 (E2) 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. E2/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\%. E2 formation from estrone sulfate (E1S) 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.",

keywords = "17β-Hydroxysteroid dehydrogenase, 3α-Hydroxysteroid dehydrogenase, 3β-Hydroxysteroid dehydrogenase, Estrone sulfatase, Ovarian cancer, Steroid metabolism",

author = "Chura, \{Justin C.\} and Ryu, \{Hyung S.\} and Marc Simard and Donald Poirier and Yves Tremblay and Brooker, \{Doris C.\} and Blomquist, \{Charles H.\} and Argenta, \{Peter A.\}",

note = "Funding Information: This project was supported by a grant from the Susan G. Komen Foundation, and the Gynecologic Cancer Foundation. The authors are grateful to Linda Sackett-Lundeen, B.S.M.T. and Doris Sackett for their help with the figures. ",

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language = "English (US)",

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T1 - Steroid-converting enzymes in human ovarian carcinomas

AU - Chura, Justin C.

AU - Ryu, Hyung S.

AU - Simard, Marc

AU - Poirier, Donald

AU - Tremblay, Yves

AU - Brooker, Doris C.

AU - Blomquist, Charles H.

AU - Argenta, Peter A.

N1 - Funding Information: This project was supported by a grant from the Susan G. Komen Foundation, and the Gynecologic Cancer Foundation. The authors are grateful to Linda Sackett-Lundeen, B.S.M.T. and Doris Sackett for their help with the figures.

PY - 2009/3/25

Y1 - 2009/3/25

N2 - 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 (E2) 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. E2/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%. E2 formation from estrone sulfate (E1S) 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.

AB - 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 (E2) 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. E2/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%. E2 formation from estrone sulfate (E1S) 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.

KW - 17β-Hydroxysteroid dehydrogenase

KW - 3α-Hydroxysteroid dehydrogenase

KW - 3β-Hydroxysteroid dehydrogenase

KW - Estrone sulfatase

KW - Ovarian cancer

KW - Steroid metabolism

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VL - 301

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JO - Molecular and Cellular Endocrinology

JF - Molecular and Cellular Endocrinology

IS - 1-2

ER -

Steroid-converting enzymes in human ovarian carcinomas

Abstract

Bibliographical note

UN SDGs

Keywords

Publisher link

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