Phosphoenolpyruvate and creatine phosphate augment ATP and magnesium-dependent, Fc epsilon RI-mediated activation of phospholipase C in RBL cell ghosts.

We have previously reported that Fc epsilon RI-mediated activation of PLC occurs in plasma membrane vesicles derived from RBL cells. This activity is dependent on ATP and magnesium, and is greatly enhanced by the addition of either PEP or CP. We undertook these studies to determine whether these compounds augment Fc epsilon RI-mediated activation of PLC because of their ability to form ATP. The specific findings were 1) the addition of increasing amounts of ATP to the ghost vesicles cannot substitute for the combination of ATP and either PEP or CP; 2) the addition of increasing amounts of ATP or a combination of ATP and either PEP or CP results in similar levels of intravesicular ATP; 3) many metabolically related compounds have some activity to support receptor-mediated PI hydrolysis, but only PEP, CP, and 3-PG give a maximal signal; and 4) the inability of ATP alone to support optimal receptor-mediated PI hydrolysis does not appear to be due to the accumulation of ADP is only modestly inhibitory. Taken together, these data are evidence that augmentation of Fc epsilon RI-mediated PI hydrolysis by PEP and CP is not explained simply by the ability of these compounds to generate intravesicular ATP.