Phospholipase D2 (PLD2)

Phosphatidylcholine (PC)-specific phospholipases D (PLDs) catalyze the hydrolysis of PC to produce phosphatidic acid and choline. Activation of PC-specific PLDs occurs as a consequence of agonist stimulation of both tyrosine kinase and G protein-coupled receptors. PC-specific PLDs have been proposed to function in regulated secretion, cytoskeletal reorganization, transcriptional regulation, and cell cycle control. Northern blot analysis demonstrated expression of an approximately 3.5-kb PLD2 transcript in various tissues including heart, placenta, pancreas, spleen, thymus, prostate, uterus, brain, lung, kidney, small intestine, and colon. Expression was relatively low in liver and skeletal muscle. An additional 3.8-kb transcript was expressed in peripheral blood leukocytes.