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The protein kinase C activator phorbol‐12‐myristate‐13‐acetate enhances cyclic AMP accumulation in pheochromocytoma cells
Author(s) -
Hollingsworth Elizabeth B.,
Ukena Dieter,
Daly John W.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80227-7
Subject(s) - forskolin , activator (genetics) , protein kinase c , phosphatidylinositol , phorbol , chemistry , endocrinology , adenosine , protein kinase a , medicine , potency , tetradecanoylphorbol acetate , kinase , biochemistry , biology , in vitro , receptor
The protein kinase C activator, phorbol‐12‐myristate‐13‐acetate (PMA), augments the cyclic AMP accumulation induced by forskolin in pheochromocytoma (PC 12) cells with an EC 50 value of 14 nM, while having no effect on basal values. At a concentration of 100 nM PMA markedly augmented the magnitude of the forskolin response and, in addition, caused a slight increase in the potency of forskolin. PMA also enhanced the maximal cyclic AMP accumulation produced by 2‐chloroadenosine, and caused a slight increase in potency of the adenosine analog. Since PMA mimics the effect of diacylglycerols that form during the turnover of the membrane lipid, phosphatidylinositol, the results suggest an interrelationship between the systems involved in phosphatidylinositol turnover and cyclic AMP generation in PC 12 cells.