epitope corresponding to phosphorylated within an internal region of PC-PLD1 of human origin
recommended for detection of Phospholipase D1 of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine and porcine
PC-PLD1 Background Information Virtually every cell uses phosphatidylcholine as a substrate to produce phosphatidic acid and choline. Phosphatidylcholine phospholipase D1 and D2 (PC-PLD1 and PC-PLD2) are phospholipid-specific phosphodiesterases that hydrolyze phosphatidylcholine. Unlike PC-PLD1, which associates with secretory granules, PC-PLD2 localizes to the plasma membrane, where it is implicated in the formation of endocytotic vesicles. Both PC-PLD1 and PC-PLD2 coordinately regulate macrophage phagocytosis. PC-PLD activity in mammalian cells is transiently stimulated upon activation by G protein-coupled and receptor tyrosine kinase cell surface receptors. For example, PC-PLD1 and PC-PLD2 participate in sphingosine 1-phosphate stimulation of ERK phosphorylation and IL-8 secretion in bronchial epithelial cells. In addition, tubulin binding to PC-PLD2 inhibits muscarinic receptor-linked PC-PLD2 activation. PC-PLD2 also enhances PKCzeta activity through direct interaction in a lipase activity-independent manner. PC-PLD1 and PC-PLD2 stimulate cell growth by repressing expression of p21 gene through p53-dependent and p53-independent pathways, respectively, which may ultimately lead to carcinogenesis.
