| The human sperm acrosome reaction does not depend on arachidonic acid metabolism via the cyclooxygenase and lipoxygenase pathways. | |
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MedLine Citation:
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PMID: 1338069 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The objective of this study was to determine whether the metabolism of arachidonic acid via the cyclooxygenase pathway, the lipoxygenase pathway, or both has a pivotal role in the human sperm acrosome reaction. To do so, the stimulatory effect of arachidonic acid and a number of its metabolites, as well as the inhibitory effect of cyclooxygenase and lipoxygenase inhibitors on the acrosome reaction, was evaluated. Arachidonic acid, prostaglandin E2, and prostacyclin (PGI2) induced the acrosome reaction when added to 3-hour preincubated (capacitated) spermatozoa. The arachidonic acid-induced acrosome reaction was dependent upon extracellular calcium. Leukotriene B4 and 15-HPETE only induced the acrosome reaction when present throughout the preincubation period, indicating that they may enhance the capacitation process rather than the acrosome reaction. Thromboxane did not affect the acrosome reaction under any of the conditions tested. Inhibitors of cyclooxygenase (indomethacin, phenylbutazone) and lipoxygenase (phenidone, nordihydroguiaretic acid) or FPL 55712 (a leukotriene antagonist) did not prevent the arachidonic acid-stimulated acrosome reaction. Furthermore, 5, 8, 11, 14-eicosatetraynoic acid (ETYA), the acetylenic analog of arachidonic acid that inhibits arachidonic acid metabolism, induced an acrosome reaction equivalent to that of arachidonic acid. These results strongly suggest that the acrosome reaction induced by exogenous arachidonic acid is not mediated via either the cyclooxygenase pathway or the lipoxygenase pathway.(ABSTRACT TRUNCATED AT 250 WORDS) |
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Authors:
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S R Mack; H L Han; J De Jonge; R A Anderson; L J Zaneveld |
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Publication Detail:
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Type: Journal Article; Research Support, U.S. Gov't, P.H.S. |
Journal Detail:
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Title: Journal of andrology Volume: 13 ISSN: 0196-3635 ISO Abbreviation: J. Androl. Publication Date: 1992 Nov-Dec |
Date Detail:
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Created Date: 1993-04-06 Completed Date: 1993-04-06 Revised Date: 2007-11-14 |
Medline Journal Info:
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Nlm Unique ID: 8106453 Medline TA: J Androl Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 551-9 Citation Subset: IM |
Affiliation:
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Department of Obstetrics and Gynecology, Rush University, Rush-Presbyterian-St. Luke's Medical Center, Chicago, Illinois 60612. |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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5,8,11,14-Eicosatetraynoic Acid
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pharmacology Acrosome / drug effects, metabolism, physiology* Arachidonic Acids / metabolism*, physiology Bucladesine / pharmacology Calcimycin / pharmacology Calcium / pharmacology Chromones / pharmacology Cyclooxygenase Inhibitors / pharmacology Dinoprostone / pharmacology Eicosanoids / pharmacology Epoprostenol / pharmacology Humans Indomethacin / pharmacology Leukotriene B4 / pharmacology Leukotrienes / pharmacology Lipid Peroxides / pharmacology Lipoxygenase / physiology* Lipoxygenase Inhibitors / pharmacology Male Nordihydroguaiaretic Acid / pharmacology Phenylbutazone / pharmacology Prostaglandin-Endoperoxide Synthases / physiology* Pyrazoles / pharmacology SRS-A / antagonists & inhibitors Vasoconstrictor Agents / pharmacology |
| Grant Support | |
ID/Acronym/Agency:
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HD 19555/HD/NICHD NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Arachidonic Acids; 0/Chromones; 0/Cyclooxygenase Inhibitors; 0/Eicosanoids; 0/Leukotrienes; 0/Lipid Peroxides; 0/Lipoxygenase Inhibitors; 0/Pyrazoles; 0/SRS-A; 0/Vasoconstrictor Agents; 1191-85-1/5,8,11,14-Eicosatetraynoic Acid; 35121-78-9/Epoprostenol; 362-74-3/Bucladesine; 363-24-6/Dinoprostone; 40786-08-1/FPL 55712; 50-33-9/Phenylbutazone; 500-38-9/Nordihydroguaiaretic Acid; 52665-69-7/Calcimycin; 53-86-1/Indomethacin; 67675-14-3/15-hydroperoxy-5,8,11,13-eicosatetraenoic acid; 71160-24-2/Leukotriene B4; 7440-70-2/Calcium; 92-43-3/phenidone; EC 1.13.11.12/Lipoxygenase; 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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