| Estrogen and progesterone metabolism in the cervix during pregnancy and parturition. | |
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MedLine Citation:
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PMID: 18364378 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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CONTEXT: Experimental and clinical studies in a variety of nonprimate species demonstrate that progesterone withdrawal leads to changes in gene expression that initiate parturition at term. Mice deficient in 5alpha-reductase type I fail to undergo cervical ripening at term despite the timely onset of luteolysis and progesterone withdrawal in blood. OBJECTIVE: Our objective was to test the hypothesis that estrogen and progesterone metabolism is regulated in cervical tissues during pregnancy, even in species in which parturition is not characterized by progesterone withdrawal in blood. DESIGN: Estradiol and progesterone metabolism was quantified in intact cervical tissues from nonpregnant and pregnant women at term before or after labor. SETTING: The study was conducted at a university hospital. PATIENTS: Tissues were obtained from five nonpregnant and 21 pregnant women (nine before labor and 12 in labor). MAIN OUTCOME MEASURES: Enzyme activity measurements, Northern blot analysis, quantitative real-time RT-PCR, and immunohistochemistry were used to quantify steroid hormone metabolizing enzymes in cervical and myometrial tissues. RESULTS: During pregnancy, 17beta-hydroxysteroid dehydrogenase type 2 was induced in glandular epithelial cells to catalyze the conversion of estradiol to estrone and stroma-derived 20alpha-hydroxyprogesterone to progesterone. During parturition, 17beta-hydroxysteroid dehydrogenase type 2 was down-regulated in endocervical cells, thereby creating a microenvironment favorable for cervical ripening. CONCLUSIONS: Together, the data indicate that cervical ripening during parturition involves localized regulation of estrogen and progesterone metabolism through a complex relationship between cervical epithelium and stroma, and that steroid hormone metabolism in cervical tissues from pregnant women is unique from that in mice. |
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Authors:
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Stefan Andersson; Debra Minjarez; Nicole P Yost; R Ann Word |
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Publication Detail:
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Type: Comparative Study; Journal Article; Research Support, N.I.H., Extramural Date: 2008-03-25 |
Journal Detail:
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Title: The Journal of clinical endocrinology and metabolism Volume: 93 ISSN: 0021-972X ISO Abbreviation: J. Clin. Endocrinol. Metab. Publication Date: 2008 Jun |
Date Detail:
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Created Date: 2008-06-09 Completed Date: 2008-07-17 Revised Date: 2013-03-27 |
Medline Journal Info:
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Nlm Unique ID: 0375362 Medline TA: J Clin Endocrinol Metab Country: United States |
Other Details:
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Languages: eng Pagination: 2366-74 Citation Subset: AIM; IM |
Affiliation:
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Department of Obstetrics and Gynecology, University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, TX 75390-9032, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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17-Hydroxysteroid Dehydrogenases
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metabolism 20-Hydroxysteroid Dehydrogenases / genetics, metabolism 3-Hydroxysteroid Dehydrogenases / genetics, metabolism 3-Oxo-5-alpha-Steroid 4-Dehydrogenase / genetics, metabolism Animals Cervical Ripening / metabolism Cervix Uteri / enzymology, metabolism*, physiology Estradiol Dehydrogenases Estrogens / metabolism* Female Gene Expression Regulation, Enzymologic Gestational Age Humans Hydroxyprostaglandin Dehydrogenases / genetics, metabolism Hydroxysteroid Dehydrogenases / genetics, metabolism Mice Models, Biological Myometrium / metabolism Oxidoreductases / genetics, metabolism Parturition / genetics, metabolism* Pregnancy Progesterone / metabolism* RNA, Messenger / metabolism |
| Grant Support | |
ID/Acronym/Agency:
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DK 52167/DK/NIDDK NIH HHS; HD 11149/HD/NICHD NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Estrogens; 0/RNA, Messenger; 57-83-0/Progesterone; EC 1.-/Oxidoreductases; EC 1.1.-/17-Hydroxysteroid Dehydrogenases; EC 1.1.-/3-Hydroxysteroid Dehydrogenases; EC 1.1.-/Hydroxysteroid Dehydrogenases; EC 1.1.1.-/20-Hydroxysteroid Dehydrogenases; EC 1.1.1.-/3 alpha-beta, 20 beta-hydroxysteroid dehydrogenase; EC 1.1.1.-/AKR1C2 protein, human; EC 1.1.1.-/AKR1C3 protein, human; EC 1.1.1.-/Hydroxyprostaglandin Dehydrogenases; EC 1.1.1.62/Estradiol Dehydrogenases; EC 1.1.1.62/HSD17B2 protein, human; EC 1.3.1.20/trans-1,2-dihydrobenzene-1,2-diol dehydrogenase; EC 1.3.99.5/3-Oxo-5-alpha-Steroid 4-Dehydrogenase |
| Comments/Corrections | |
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