LH-stimulated adenylate cyclase activity in membrane preparations of bovine luteal cells could be enhanced by treating the cells with either phospholipase D or its hydrolysis product, phosphatidic acid. Similar augmentary effects were also produced following treatment of the cells with EGF. Moreover, EGF could stimulate the formation of [3H]phosphatidic acid in [3H]myristic acid preloaded cells, suggesting that EGF is able to activate cellular phospholipase D. Also, PMA was able to increase the phosphatidic acid formation with a parallel increase in the adenylate cyclase activity. We propose, therefore, that phosphatidic acid may act as an intracellular second messenger linking EGF-mediated activation of phospholipase D with the sensitization of LH receptor-coupled adenylate cyclase signalling system.