Interferon-τ modulates phorbol ester-induced production of prostaglandin and expression of cyclooxygenase-2 and phospholipase-A2 from bovine endometrial cells

Abstract

Antiluteolytic actions of bovine interferon-tau (blFN-τ) require suppression of prostaglandin F2(α) (PGF2(α)) production. Our objective was to test whether bIFN-τ could block PGF2(α) production and synthesis of phospholipase A2 (PLA2) and cyclooxygenase-2 (COX-2) enzymes induced by a protein kinase C (PKC) stimulator (phorbol 12,13 dibutyrate; PDBu). Bovine endometrial epithelial (BEND) cells were treated with PDBu in the presence or absence of bIFN-τ. Medium samples were analyzed for concentrations of PGF2(α), whole-cell extracts were analyzed for abundance of PLA2 and COX-2 by immunoblotting, and RNA extracts were examined for steady-state levels of COX-2 mRNA by Northern blotting. The PDBu stimulated production of PGF2(α) between 3 and 12 h, levels of COX-2 mRNA by 3 h and protein expression of COX-2 and PLA2 by 6 and 12 h, respectively. Added concomitantly with PDBu, blFN-τ suppressed PGF2(α) production, steady-state levels of COX-2 mRNA, and expression of COX-2 and PLA2 proteins. Added after a 3-h stimulation with PDBu alone, bIFN-τ suppressed PGF2(α) production after 1 h. Bovine IFN-τ inhibited intracellular mechanisms responsible for PGF2(α) production in BEND cells, and this could be through both cytosolic and nuclear actions.