The role of guanyl nucleotide binding proteins in the formation of inositol phosphates in adrenal glomerulosa cells.

A non-hydrolysable GTP analogue enhanced the formation of [3H]inositol polyphosphates in permeabilized adrenal glomerulosa cells. Pertussis toxin, which ADP-ribosylated Ni, failed to influence angiotensin-induced formation of 3H-labelled inositol phosphates and the incorporation of [32F]phosphate into phosphatidylinositol and phosphatidic acid. These results show that Ni is present and a G-protein activates phospholipase C also in glomerulosa cells, however, it is not Ni which couples angiotensin receptors to the enzyme.