| Ascorbate-dependent lipid peroxidation in the human placenta and fetal membranes. | |
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MedLine Citation:
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PMID: 3921439 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The ascorbate-dependent lipid peroxidation in the microsomal fraction of at term placentas and fetal membranes were studied. In preliminary experiments, the optimum conditions for the measurement of this reaction were determined. Lipid peroxidation was significantly higher in the chorion and amnion compared to the placenta. In both fetal membranes, but not in the placenta, the reaction was enhanced by arachidonic acid and inhibited by indomethacin. The results indicate that the ascorbate-dependent lipid peroxidation in the fetal membranes is specific for prostaglandin synthetase activity and that these tissues are a major site of prostaglandin synthesis. |
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Authors:
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G Ohel; R Kisselevitz; E J Margalioth; J G Schenker |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Gynecologic and obstetric investigation Volume: 19 ISSN: 0378-7346 ISO Abbreviation: Gynecol. Obstet. Invest. Publication Date: 1985 |
Date Detail:
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Created Date: 1985-06-19 Completed Date: 1985-06-19 Revised Date: 2006-11-15 |
Medline Journal Info:
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Nlm Unique ID: 7900587 Medline TA: Gynecol Obstet Invest Country: SWITZERLAND |
Other Details:
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Languages: eng Pagination: 73-7 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Amnion
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metabolism* Arachidonic Acid Arachidonic Acids / pharmacology Ascorbic Acid / metabolism* Chorion / metabolism* Female Humans Indomethacin / pharmacology Lipid Peroxides / metabolism* Microsomes / metabolism Placenta / metabolism* Pregnancy Prostaglandin-Endoperoxide Synthases / metabolism Prostaglandins / biosynthesis* Time Factors |
| Chemical | |
Reg. No./Substance:
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0/Arachidonic Acids; 0/Lipid Peroxides; 0/Prostaglandins; 50-81-7/Ascorbic Acid; 506-32-1/Arachidonic Acid; 53-86-1/Indomethacin; EC 1.14.99.1/Prostaglandin-Endoperoxide Synthases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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