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Biochem Biophys Res Commun. 2009 Jul 10;384(4):450-4. doi: 10.1016/j.bbrc.2009.04.139. Epub 2009 May 5.

Estrogen receptor alpha interacts with 17beta-hydroxysteroid dehydrogenase type 10 in mitochondria.

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  • 1Laboratory of Molecular Cardiology, Department of Medicine, University Clinics Wuerzburg, Josef-Schneider-Strasse 2, D20, 97080 Wuerzburg, Germany. Jazbutyte_V@klinik.uni-wuerzburg.de

Abstract

Estrogen receptor alpha (ERalpha) is present in the nucleus, the cytosol and in mitochondria. The rat ERalpha ligand binding domain was employed as bait in a bacterial two-hybrid screening of a human heart cDNA library to detect novel protein-protein interaction partners of ERalpha in the heart. 17beta-Hydroxysteroid dehydrogenase type 10 (17beta-HSD10), which converts potent (17beta-estradiol) to less potent estrogens (estrone), co-localized with 17beta-HSD10 in the mitochondria of rat cardiac myocytes. GST pull-down experiments confirmed the interaction of ERalpha and 17beta-HSD10. These findings suggest that the ERalpha estrogen receptor might be involved in regulating intracellular estrogen levels by modulating 17beta-HSD10 activity.

PMID:
19422801
[PubMed - indexed for MEDLINE]
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