Document Detail

Estrogen and progesterone metabolism in the cervix during pregnancy and parturition.
MedLine Citation:
PMID:  18364378     Owner:  NLM     Status:  MEDLINE    
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.
Stefan Andersson; Debra Minjarez; Nicole P Yost; R Ann Word
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Publication Detail:
Type:  Comparative Study; Journal Article; Research Support, N.I.H., Extramural     Date:  2008-03-25
Journal Detail:
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:
Created Date:  2008-06-09     Completed Date:  2008-07-17     Revised Date:  2013-03-27    
Medline Journal Info:
Nlm Unique ID:  0375362     Medline TA:  J Clin Endocrinol Metab     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2366-74     Citation Subset:  AIM; IM    
Department of Obstetrics and Gynecology, University of Texas Southwestern Medical Center at Dallas, 5323 Harry Hines Boulevard, Dallas, TX 75390-9032, USA.
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MeSH Terms
17-Hydroxysteroid Dehydrogenases / metabolism
20-Hydroxysteroid Dehydrogenases / genetics,  metabolism
3-Hydroxysteroid Dehydrogenases / genetics,  metabolism
3-Oxo-5-alpha-Steroid 4-Dehydrogenase / genetics,  metabolism
Cervical Ripening / metabolism
Cervix Uteri / enzymology,  metabolism*,  physiology
Estradiol Dehydrogenases
Estrogens / metabolism*
Gene Expression Regulation, Enzymologic
Gestational Age
Hydroxyprostaglandin Dehydrogenases / genetics,  metabolism
Hydroxysteroid Dehydrogenases / genetics,  metabolism
Models, Biological
Myometrium / metabolism
Oxidoreductases / genetics,  metabolism
Parturition / genetics,  metabolism*
Progesterone / metabolism*
RNA, Messenger / metabolism
Grant Support
Reg. No./Substance:
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 Dehydrogenases; EC protein, human; EC,2-dihydrobenzene-1,2-diol dehydrogenase; EC 4-Dehydrogenase

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