Involvement of protein kinase C in prostaglandin E2-induced catecholamine release from cultured bovine adrenal chromaffin cells.

摘要: We recently reported that prostaglandin (PG) E2 stimulated phosphoinositide metabolism in cultured bovine adrenal chromaffin cells and PGE2 ouabain induced a gradual secretion of catecholamines from the (Yokohama, H., Tanaka, T., Ito, S., Negishi, M., Hayashi, Hayaishi, O. (1988) J. Biol. Chem. 263, 1119-1122). Here we examined involvement two signal pathways, Ca2+ mobilization protein kinase C activation resulting metabolism, PGE2-induced catecholamine release. Either ionophore ionomycin or 12-O-tetradecanoylphorbol 13-acetate (TPA) could enhance release presence ouabain, ionomycin-induced was additive to release, but TPA-induced not additive. dose-dependently formation diacylglycerol caused translocation 4% total activity become membrane-bound within 5 min. These effects were specific for PGE1 among PGs tested (PGE2 = greater than PGF2 alpha PGD2). Furthermore, phosphoinositide-specific phospholipase inhibitor neomycin inhibited accumulation inositol phosphates, formation, C, also stimulation Both PGE2- by depletion prolonged exposure TPA, inhibited. found amiloride-sensitive Na+, H+-antiport participates PGE2-evoked (Tanaka, Yokohama, (1990) Neurochem. 54, 86-95). In agreement with our recent report, TPA sustained increase intracellular pH abolished staurosporine calmodulin W-7. Ionomycin marked pH, this W-7 staurosporine. results demonstrate H(+)-antiport are mediated rather mobilization, metabolism.