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Distinct phospholipase A2 enzymes regulate prostaglandin E2 and F2alpha production by bovine endometrial epithelial cells

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BioMed Central
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PMC
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  • Research
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  • Biology

Abstract

1477-7827-5-16.fm ral Reproductive Biology and ss BioMed CentEndocrinology Open AcceResearch Distinct phospholipase A2 enzymes regulate prostaglandin E2 and F2alpha production by bovine endometrial epithelial cells Patricia K Tithof1, Mary P Roberts2, Wei Guan1, Mona Elgayyar1 and James D Godkin*2 Address: 1The University of Tennessee College of Veterinary Medicine, TN, USA and 2The University of Tennessee, Department of Animal Science, Knoxville, TN, USA Email: Patricia K Tithof - [email protected]; Mary P Roberts - [email protected]; Wei Guan - [email protected]; Mona Elgayyar - [email protected]; James D Godkin* - [email protected] * Corresponding author Abstract Background: The rate-limiting step in prostaglandin (PG) biosynthesis is catalyzed by phospholipase A2 (PLA2) enzymes which hydrolyze arachidonic acid from membrane phospholipids. Despite their importance in uterine PG production, little is known concerning the specific PLA2 enzymes that regulate arachidonic acid liberation in the uterine endometrium. The objectives of this study were to evaluate the expression and activities of calcium-independent Group VI and Group IVC PLA2 (PLA2G6 and PLA2G4C) and calcium-dependent Group IVA PLA2 (PLA2G4A) enzymes in the regulation of bovine uterine endometrial epithelial cell PG production. Methods: Bovine endometrial epithelial cells in culture were treated with oxytocin, interferon-tau and the PLA2G6 inhibitor bromoenol lactone, alone and in combination. Concentrations of PGF2alpha and PGE2 released into the medium were analyzed. Western blot analysis was performed on cellular protein to determine the effects of treatments on expression of PLA2G4A, PLA2G6 and PLA2G4C. Group-specific PLA2 activity assays were performed on cell lysates following treatment with oxytocin, interferon-tau or vehicle (control), alone and in combination. To further evaluate the role of specific PLA2 enzymes in uterine cell PG biosynthesis, cells were transfected with cDNAs encoding human PLA2G6 an

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