Document Detail


Biosynthesis and catabolism of prostaglandin F2alpha (PGF2alpha) are controlled by progesterone in the rat uterus during pregnancy.
MedLine Citation:
PMID:  15336698     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Myometrial quiescence is a key factor in all species to accomplish a successful gestation. PGs play a crucial role in mediating parturition events, and their synthesis and metabolism are regulated by cyclooxygenases (COXs) and NAD(+)-dependent 15-hydroxy-PG dehydrogenase (PGDH), respectively. Progesterone (P(4)) is the hormone responsible for maintaining uterine smooth muscle quiescence during pregnancy. In this work, we have studied the effect of P(4) on the activity of COXs and PGDH, the uterine enzymes involved in the biosynthesis and metabolism of prostanoids in the rat. We found that during pregnancy PGF(2alpha) production and also protein levels of COX-1 and COX-2 were decreased. The exogenous administration of P(4) significantly inhibited the uterine production of PGF(2alpha) and also the protein level of COX-2. PGF(2alpha), metabolism was assessed by PGDH activity, which resulted high during pregnancy and increased as a result of P(4) administration. These results indicate that PGs levels were negatively modulated by P(4), which could be exerting its effect by increasing PGs metabolism through stimulation on PGDH activity and an inhibition on COX and that is a major mechanism for maintain uterine quiescence in pregnancy.
Authors:
M Farina; M L Ribeiro; C Weissmann; A Estevez; S Billi; C Vercelli; A Franchi
Related Documents :
21410408 - Diastolic forward flow in the fetal main pulmonary artery and its implication for fetal...
21388678 - Villous trophoblast abnormalities in extremely preterm deliveries with elevated second ...
21306328 - Association between five minute apgar scores and planned mode of delivery in diabetic p...
21308838 - The thymic-thoracic-ratio in fetal heart defects: a simple ratio for the identification...
3594348 - The effect of porcine relaxin on the fertilisation of mouse oocytes in vitro.
2242088 - Topical tolerability of salmon calcitonin assessed by mucociliary transport velocity in...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  The Journal of steroid biochemistry and molecular biology     Volume:  91     ISSN:  0960-0760     ISO Abbreviation:  J. Steroid Biochem. Mol. Biol.     Publication Date:  2004 Aug 
Date Detail:
Created Date:  2004-08-31     Completed Date:  2004-11-02     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9015483     Medline TA:  J Steroid Biochem Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  211-8     Citation Subset:  IM    
Affiliation:
Center of Pharmacological and Botanical Studies (CEFYBO), Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET), Serrano 669, Capital Federal, 1414 Buenos Aires, Argentina.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Abortifacient Agents, Nonsteroidal / metabolism*
Animals
Cyclooxygenase 1
Cyclooxygenase 2
Dinoprost / metabolism*
Female
Hydroxyprostaglandin Dehydrogenases / metabolism
Isoenzymes / metabolism
Membrane Proteins
Pregnancy
Progesterone / pharmacology*
Prostaglandin-Endoperoxide Synthases / metabolism
Rats
Rats, Wistar
Uterus / drug effects*,  metabolism
Chemical
Reg. No./Substance:
0/Abortifacient Agents, Nonsteroidal; 0/Isoenzymes; 0/Membrane Proteins; 551-11-1/Dinoprost; 57-83-0/Progesterone; EC 1.1.1.-/Hydroxyprostaglandin Dehydrogenases; EC 1.1.1.141/15-hydroxyprostaglandin dehydrogenase; EC 1.14.99.1/Cyclooxygenase 1; EC 1.14.99.1/Cyclooxygenase 2; EC 1.14.99.1/Prostaglandin-Endoperoxide Synthases; EC 1.14.99.1/Ptgs1 protein, rat

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Modulation of transcriptional sensitivity of mineralocorticoid and estrogen receptors.
Next Document:  The effects of betamethasone (BM) on endothelial nitric oxide synthase (eNOS) expression in adult ba...