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17 beta-estradiol dehydrogenase (E2DH) activity in T47D cells.
1Department of Endocrinology and Reproductive Medicine, Hôpital Necker, Paris, France.
The Journal of Steroid Biochemistry and Molecular Biology
|November 1, 1991
Summary
NAD-dependent 17 beta-hydroxysteroid dehydrogenase (E2DH) activity in breast cancer cells is progesterone-dependent. Assaying E2DH alongside hormone receptors may help evaluate breast cancer hormone dependence.
Area of Science:
- Endocrinology
- Molecular Biology
- Oncology
Background:
- NAD-dependent 17 beta-hydroxysteroid dehydrogenase (E2DH) interconverts estradiol (E2) and estrone (E1).
- E2DH activity is higher in breast epithelial cells than fibroblasts and is progesterone-dependent.
- E2DH's role in hormone-dependent breast cancer warrants further investigation.
Purpose of the Study:
- To investigate E2DH activity in progesterone receptor (PR)-rich T47D breast cancer cells.
- To assess E2DH as a potential marker for hormone dependence in breast cancer.
Main Methods:
- Characterization of E2DH activity in T47D cells.
- Measurement of [3H]E2 to E1 conversion in the presence of NAD.
- Treatment of T47D cells with the progestin R5020 to assess E2DH stimulation.
Main Results:
- T47D cells exhibit limited E2 to E1 conversion, with a preference for E1 to E2 metabolism.
- NAD cofactor increased E2 to E1 conversion.
- Progestin R5020 treatment stimulated E2DH activity 2- to 3-fold, indicating PR operability.
Conclusions:
- E2DH activity in T47D cells is influenced by PR presence and function.
- E2DH assay may complement existing receptor assays for evaluating breast cancer hormone dependence.