Antiluteolytic actions of bovine interferon-tau (bIFN-τ) require suppression of prostaglandin F2α (PGF2α) production. Our objective was to test whether bIFN-τ could block PGF2α 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 PGF2α, 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 PGF2α 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, bIFN-τ suppressed PGF2α 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 PGF2α production after 1 h. Bovine IFN-τ inhibited intracellular mechanisms responsible for PGF2α production in BEND cells, and this could be through both cytosolic and nuclear actions.
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