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 [32P]phosphate into phosphatidyl inositol and phosphatidic acid. These results show that Ni, is prescot and a G-protein activates phospholipase C also in glomerulosa cells, however, it is not Ni which couples angiotensin receptors to the enzyme.
|Number of pages||7|
|Journal||Biochemical and biophysical research communications|
|Publication status||Published - Nov 14 1986|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology