Document Detail

Estrogen and lipopolysaccharide stimulation of prostacyclin production and the levels of cyclooxygenase and nitric oxide synthase in ovine uterine arteries.
MedLine Citation:
PMID:  9746755     Owner:  NLM     Status:  MEDLINE    
Several enzymes play a role in vasodilation, including cyclooxygenase, which converts arachidonic acid into prostaglandins, and nitric oxide synthase, which converts arginine to citrulline and yields nitric oxide. The effects of endogenous and exogenous estrogen and lipopolysaccharide on uterine artery production of prostacyclin, and levels of cyclooxygenase and nitric oxide synthase were examined. Uterine arteries collected from ewes during the follicular (Day -1 to 0, Day 0 = estrus) or luteal (Day 10) phase were treated in vitro with lipopolysaccharide. In addition, ovariectomized ewes were treated in vivo with estradiol-17beta (5 microg/kg; 120 min) or a vehicle control; arteries from the uteri were treated in vitro with lipopolysaccharide. After 24 h of lipopolysaccharide treatment, culture media were collected for measurement of 6-keto-prostaglandin F1alpha (the stable metabolite of prostacyclin). These uterine arteries were homogenized, and the level of cyclooxygenase and nitric oxide synthase was determined by Western analysis. Lipopolysaccharide stimulated (p < 0.02) prostacyclin production by uterine arteries from both follicular- and luteal-phase sheep although phase of the estrous cycle did not affect prostacyclin responses (p = 0.56) to lipopolysaccharide. In contrast, uterine arteries from ovariectomized sheep treated with estradiol-17beta produced more prostacyclin (p < 0.001) in response to lipopolysaccharide than did uterine arteries from ovariectomized sheep treated with the vehicle control. There was no effect of phase (follicular or luteal) of the estrous cycle on either cyclooxygenase-1 or -2 gene expression. Lipopolysaccharide increased (p = 0.0002) gene expression of cyclooxygenase-2, but not cyclooxygenase-1, in both follicular- and luteal-phase ewes, which was significantly correlated (r2 = 0.91, p = 0.003) with uterine artery production of prostacyclin. Uterine arteries from follicular-phase sheep expressed significantly more nitric oxide synthase-III after lipopolysaccharide exposure than did uterine arteries from luteal-phase ewes (p = 0.03). In contrast, nitric oxide synthase-II was not detected in uterine arteries after lipopolysaccharide exposure. These results suggest that estrogen plays a role in regulating uterine artery responses to lipopolysaccharide.
K E Vagnoni; R R Magness
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Biology of reproduction     Volume:  59     ISSN:  0006-3363     ISO Abbreviation:  Biol. Reprod.     Publication Date:  1998 Oct 
Date Detail:
Created Date:  1998-12-07     Completed Date:  1998-12-07     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  0207224     Medline TA:  Biol Reprod     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  1008-15     Citation Subset:  IM    
Department of Animal, Dairy, and Veterinary Sciences, Utah State University, Logan, Utah 84322, USA.
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MeSH Terms
6-Ketoprostaglandin F1 alpha / metabolism
Arteries / drug effects,  enzymology,  metabolism
Blotting, Western
Cyclooxygenase 1
Cyclooxygenase 2
Epoprostenol / biosynthesis*
Estradiol / pharmacology
Estrogens / pharmacology*,  physiology
Estrus / metabolism
Isoenzymes / biosynthesis
Lipopolysaccharides / pharmacology*
Nitric Oxide Synthase / biosynthesis*
Nitric Oxide Synthase Type II
Prostaglandin-Endoperoxide Synthases / biosynthesis*
Regional Blood Flow / physiology
Uterus / blood supply,  drug effects,  enzymology*
Grant Support
Reg. No./Substance:
0/Estrogens; 0/Isoenzymes; 0/Lipopolysaccharides; 35121-78-9/Epoprostenol; 50-28-2/Estradiol; 58962-34-8/6-Ketoprostaglandin F1 alpha; EC Oxide Synthase; EC Oxide Synthase Type II; EC 1; EC 2; EC Synthases

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

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