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W1978402076 abstract "The activation of beta-adrenergic receptors in rat parotid acinar cells causes intracellular cAMP elevation and appreciably stimulates the exocytotic release of amylase into saliva. The activation of Ca(2+)-mobilizing receptors also induces some exocytosis. We investigated the role of phospholipase D (PLD) in regulated exocytosis in rat parotid acinar cells. A transphosphatidylation assay detected GTPgammaS (a nonhydrolyzable analogue of GTP)-dependent PLD activity in lysates of rat parotid acinar cells, suggesting that PLD is activated by small molecular mass GTP-binding proteins. The PLD inhibitor, neomycin, suppressed cAMP-dependent exocytosis in saponin-permeabilized cells. Signaling downstream of PLD was disrupted by 1-butanol due to conversion of the PLD reaction product (phosphatidic acid) to phosphatidylbutanol. The stimulation of exocytosis by isoproterenol as well as by a Ca(2+)-mobilizing agonist (methacholine) was inhibited by 1-butanol. These results suggest that PLD is important for regulated exocytosis in rat parotid acinar cells." @default.
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W1978402076 date "2002-12-01" @default.
W1978402076 modified "2023-10-16" @default.
W1978402076 title "Involvement of phospholipase D in the cAMP-regulated exocytosis of rat parotid acinar cells" @default.
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W1978402076 doi "https://doi.org/10.1016/s0006-291x(02)02713-4" @default.
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