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J. Biol. Chem., Vol. 269, Issue 40, 24546-24549, Oct, 1994
AJ Baukal, L Hunyady, KJ Catt and T Balla
Angiotensin II (AII) receptors are known to interact with two distinct
guanine nucleotide binding proteins, Gq/11 and Gi, in rat adrenal
glomerulosa cells to activate phospholipase C and to inhibit adenylate
cyclase, respectively. However, in cultured bovine glomerulosa cells AII
potentiates rather than inhibits the stimulatory effect of
adrenocorticotropin (ACTH) on cAMP levels. This effect of AII was partially
mimicked by phorbol 12-myristate 13-acetate (PMA) and was partially
inhibited by staurosporine or depletion of protein kinase C but was
unaffected by pertussis toxin treatment. No potentiation was detectable in
disrupted cells or in membrane preparations. In intact glomerulosa cells,
treatment with cyclosporin A or FK506 completely inhibited AII- or
PMA-induced potentiation of cAMP production without affecting the response
to ACTH. In COS-7 cells transfected with the rat AT1 receptor, AII caused
2-3-fold enhancement of the ACTH-induced cAMP response, an effect that was
partially reproduced by PMA. These potentiating actions of AII and PMA were
prevented by preincubation with cyclosporin A or FK506, and the latter
effect was abolished by rapamycin. These results implicate the Ca2+- and
calmodulin-dependent protein phosphatase, calcineurin, in AII-induced
enhancement of adenylate cyclase activity in both adrenal glomerulosa and
transfected COS-7 cells. The finding that AII enhances ACTH-stimulated
production of cAMP by a second messenger-mediated mechanism that involves
the participation of calcineurin reveals an additional mode of cross-talk
between pathways activated by Ca(2+)-mobilizing and cAMP-generating
receptors.
Evidence for participation of calcineurin in potentiation of agonist- stimulated cyclic AMP formation by the calcium-mobilizing hormone, angiotensin II
Endocrinology and Reproduction Research Branch, NICHD, National Institutes of Health, Bethesda, Maryland 20892.
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