The study establishes the identity of major inositol phosphate products in AII-stimulated rat adrenal glomerulosa cells, confirming previous observations.
Preclinical rat cell data warrant no practice change; leaves open human translation of AII-inositol phosphate signaling.
[3H]Inositol-prelabelled isolated rat adrenal glomerulosa cells were stimulated with 25 nM-AII ([Asp1, Ile5]-angiotensin II) in the presence of 10 mM-Li+, and the resulting inositol monophosphate isomers were separated successfully by using a recently developed h.p.l.c. methodology. Two major peaks of radioactivity were detected which showed the same retention characteristics on h.p.l.c. as inositol 4-phosphate and inositol 1-phosphate and which increased 5-fold and 8-fold respectively on stimulation with AII. In addition, a relatively small peak with the retention characteristics of inositol 1:2-cyclic phosphate was seen to undergo a 1.5-fold increase on stimulation. This was not considered sufficient to suggest that cyclic phosphoinositols were a major product of AII-stimulated phosphoinositide turnover. No peaks of radioactive material were detected in the regions expected for inositol 2-phosphate (an acid hydrolysis product of inositol 1:2-cyclic phosphate) or inositol 5-phosphate. These results establish the identity of the major inositol phosphate products in AII-stimulated glomerulosa cells and confirm and extend the previous observations of Balla, Baukal, Guillemette, Morgan & Catt [(1986) Proc. Natl. Acad. Sci. 83, 9323-9327].
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Bird et al. (1987) studied this question.
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