Phospholipase A2 regulation of bovine endometrial (BEND) cell prostaglandin production
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Phospholipase A2 regulation of bovine endometrial (BEND) cell prostaglandin production James D Godkin*1, Mary P Roberts1, Mona Elgayyar2, Wei Guan2 and Patricia K Tithof2 Address: 1Department of Animal Science, The University of Tennessee, Knoxville, TN, USA and 2The University of Tennessee College of Veterinary Medicine, Department of Pathology, Knoxville, TN, USA Email: James D Godkin* - [email protected]; Mary P Roberts - [email protected]; Mona Elgayyar - [email protected]; Wei Guan - [email protected]; Patricia K Tithof - [email protected] * Corresponding author
Published: 23 September 2008 Reproductive Biology and Endocrinology 2008, 6:44
doi:10.1186/1477-7827-6-44
Received: 10 July 2008 Accepted: 23 September 2008
This article is available from: http://www.rbej.com/content/6/1/44 © 2008 Godkin et al; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Abstract Background: Prostaglandins (PG), produced by the uterine endometrium, are key regulators of several reproductive events, including estrous cyclicity, implantation, pregnancy maintenance and parturition. Phospholipase A2 (PLA2) catalyzes the release of arachidonic acid from membrane phospholipids, the rate-limiting step in PG biosynthesis. The bovine endometrial (BEND) cell line has served as a model system for investigating regulation of signaling mechanisms involved in uterine PG production but information concerning the specific PLA2 enzymes involved and their role in regulation of this process is limited. The objectives of this investigation were to evaluate the expression and activities of calcium-dependent group IVA (PLA2G4A) and calciumindependent group VI (PLA2G6) enzymes in the regulation of BEND cell PG production. Methods: Cells were grown to near-confluence and treated with phorbol 12, 13 dibutyrate (PDBu), interferon-tau (IFNT), the PLA2G4A inhibitor pyrrolidine-1 (PYR-1), the PLA2G6 inhibitor bromoenol lactone (BEL) and combinations of each. Concentrations of PGF2alpha and PGE2 released into the medium were determined. Western blot analysis was performed on cellular protein to determine effects of treatment on expression of PLA2G4A, PLA2G6 and PLA2G4C. PLA2 assays were performed on intact cells by measuring arachidonic acid and linoleic acid release and group-specific PLA2 activity assays were performed on cell lysates. Results: BEND cells produced about 10-fold more PGE2 than PGF2alpha under resting conditions. Production of both PGs increased significantly in response to PDBu-stimulation. PYR-1 significantly diminished production of both PGs by resting cells and abolished the stimulatory effect of PDBu. BEL stimulated production of both PGs. IFNT reduced both PGE2 and PGF2alpha production by resting cells and diminished PDBu stimulation of PG production. Con
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