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J. Biol. Chem., Vol. 260, Issue 5, 2625-2628, Mar, 1985
JD Bell, IL Buxton and LL Brunton
Addition of 12-O-tetradecanoylphorbol-13-acetate (TPA) to S49 lymphoma
cells (wild type and a cyclic AMP-dependent protein kinase-lacking clone)
has little effect alone but doubles accumulation of cyclic AMP in response
to isoproterenol. The effect is immediate and has an apparent affinity and
order of potency characteristic of the activation of protein kinase C by
phorbol esters. Enhancement does not reflect an altered time course of the
beta-adrenergic response, enhanced affinity of the cellular beta-receptor
for agonist, or decreased degradation and export of cellular cyclic AMP.
Reduction of the beta-adrenergic response by somatostatin does not remove
the effect of TPA nor does TPA abolish the effect of somatostatin. Phorbol
ester enhances cyclic AMP accumulation in response to cholera toxin in wild
type and UNC clones but not in H21a or cyc-. TPA also enhances cAMP
accumulation in response to forskolin in wild type cells. The effect of TPA
is stable to rapid preparation of membranes. In adenylate cyclase assays on
membranes from cells treated with TPA, the activation by guanosine 5'-
(beta, gamma-imino)triphosphate is enhanced by 40% with no change in lag
time; the effect of beta-agonist plus Gpp(NH)p is similarly enhanced;
activation by Mn2+ is unchanged. We conclude that phorbol ester facilitates
the productive interaction of the alpha subunit of the transducer protein
Gs with the catalytic unit of adenylate cyclase, hypothetically via an
action of protein kinase C.
Enhancement of adenylate cyclase activity in S49 lymphoma cells by phorbol esters. Putative effect of C kinase on alpha s-GTP-catalytic subunit interaction
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