Preferential inhibition of phorbol ester-induced hydrolysis of phosphatidylethanolamine by N-acetylsphingosine in NIH 3T3 fibroblasts.

It has been reported that in rat fibroblasts cell-permeable ceramide analogs inhibit agonist-induced phospholipase D (PLD)-mediated hydrolysis of phosphatidylcholine (PtdCho). Here we demonstrate that relatively short (30 min) treatments of NIH 3T3 fibroblasts with 15-60 microM concentrations of N-acetylsphingosine result in preferential, although not exclusive, inhibition of phorbol 12-myristate 13-acetate-induced PLD-mediated hydrolysis of phosphatidylethanolamine (PtdEtn). The results suggest that in different cell types the PtdEtn- and PtdCho-hydrolyzing PLD activities are differentially sensitive to the inhibitory effect of ceramide.