Estrogen biosynthesis and signaling in endometriosis.

13:45 EDT 28th July 2015 | BioPortfolio

Summary of "Estrogen biosynthesis and signaling in endometriosis."

Endometriosis is an estrogen-dependent gynecological disease where endometrium-like tissue grows outside uterine cavity. Endometriotic cell proliferation is stimulated by estrogens acting predominantly via their nuclear receptors. Estrogen receptors (ESR1, ESR2) are ligand activated transcription factors whose activation is dependent on the cell-specific dynamic expression of the receptors, on the interacting proteins and on the ligand availability. The different types of endometriotic lesions, peritoneal, deep, and ovarian endometriosis, may respond to estrogens differentially due to differences in the expression of the receptors and interacting proteins, and due to potential differences in the ligand availability regulated by the local estrogen synthesis. This review summarizes the current knowledge of estrogen synthesizing enzymes and estrogen receptors in different types of endometriosis lesions. Further studies are still needed to define the possible differences in steroid metabolism in different types of endometriotic lesions.

Affiliation

Department of Physiology, Institute of Biomedicine, University of Turku, 20014 Turku, Finland. kaisa.huhtinen@utu.fi

Journal Details

This article was published in the following journal.

Name: Molecular and cellular endocrinology
ISSN: 1872-8057
Pages: 146-54

Links

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Medical and Biotech [MESH] Definitions

Compounds which inhibit or antagonize the action or biosynthesis of estrogenic compounds.

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The use of hormonal agents with estrogen-like activity in postmenopausal or other estrogen-deficient women to alleviate effects of hormone deficiency, such as vasomotor symptoms, DYSPAREUNIA, and progressive development of OSTEOPOROSIS. This may also include the use of progestational agents in combination therapy.

One of the ESTROGEN RECEPTORS that has greater affinity for ISOFLAVONES than ESTROGEN RECEPTOR ALPHA does. There is great sequence homology with ER alpha in the DNA-binding domain but not in the ligand binding and hinge domains.


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