Document Detail


The human sperm acrosome reaction does not depend on arachidonic acid metabolism via the cyclooxygenase and lipoxygenase pathways.
MedLine Citation:
PMID:  1338069     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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)
Authors:
S R Mack; H L Han; J De Jonge; R A Anderson; L J Zaneveld
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Journal of andrology     Volume:  13     ISSN:  0196-3635     ISO Abbreviation:  J. Androl.     Publication Date:    1992 Nov-Dec
Date Detail:
Created Date:  1993-04-06     Completed Date:  1993-04-06     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  8106453     Medline TA:  J Androl     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  551-9     Citation Subset:  IM    
Affiliation:
Department of Obstetrics and Gynecology, Rush University, Rush-Presbyterian-St. Luke's Medical Center, Chicago, Illinois 60612.
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MeSH Terms
Descriptor/Qualifier:
5,8,11,14-Eicosatetraynoic Acid / 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:
HD 19555/HD/NICHD NIH HHS
Chemical
Reg. No./Substance:
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

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