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Epidermal adenylate cyclase system is regulated by diacylglycerol‐protein kinase C signal, but not by calcium signal
Author(s) -
IIZUKA H.,
SAKAI H.,
KINOUCHI M.
Publication year - 1990
Publication title -
british journal of dermatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.304
H-Index - 179
eISSN - 1365-2133
pISSN - 0007-0963
DOI - 10.1111/j.1365-2133.1990.tb14722.x
Subject(s) - diacylglycerol kinase , adenylate kinase , cyclase , protein kinase c , second messenger system , protein kinase a , inositol , inositol trisphosphate , calcium , ionophore , biochemistry , egta , forskolin , chemistry , signal transduction , biology , endocrinology , kinase , receptor , organic chemistry
SUMMARY The breakdown of inositol phospholipids is an important transmembrane signalling system that is composed of two kinds of signals: the diacylglycerol‐protein kinase C signal, and the inositol trisphosphate‐Ca 2+ signal. Using membrane‐permeable diacylglycerol, 1‐oleoy‐2‐acetylgly‐cerol (OAG), and calcium ionophore, A‐23187, the effects of these chemicals on the epidermal adenylate cyclase system were investigated. OAG increased forskolin‐ and cholera toxin‐induced cyclic AMP accumulations, but receptor adenylate cyclase responses were markedly decreased by treatment with OAG. The effects of OAG were inhibited by the protein kinase C inhibitor, H‐7. Calcium ionophore, A‐23187, had no effect on the epidermal adenylate cyclase responses. Combinations of OAG and A‐23187 (as well as the calcium chelator, EGTA), showed that the action of OAG was mostly unaffected by the modulation of intracellular and extracellular Ca 2+ concentrations. The results suggest that among the signals triggered by the breakdown of inositol phospholipids, only diacylglycerol‐protein kinase C signal is involved in the regulation of the epidermal adenylate cyclase system.