The effect of acteoside on intracellular Ca2+ mobilization and phospholipase C activity in RBL-2H3 cells stimulated by melittin
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This study was performed to investigate the effects of acteoside on various cellular functions such as, intracellular Ca2+ mobilization, phospholipase C activity, and exocytosis induced by melittin. Melittin (0.1–1 μM) dose-dependently increased intracellular Ca2+ mobilization in the presence of extracellular Ca2+, but was not affected by 1 μM U73122, a specific PLC inhibitor. In the absence of extracellular Ca2+, melittin (1 μM) did not induce a change in intracellular Ca2+ mobilization, which suggests that melittin-induced intracellular Ca2+ mobilization may be dependent on the influx of extracellular Ca2+ rather than on the release of intracellular Ca2+ storage. Acteoside (10 μM) significantly inhibited 1 μM melittin-induced Ca2+ mobilization by 33 %. In [3H]inositol-labeled cells, 1 μM melittin did not increase inositol phosphate formation, but more than 5 μM melittin significantly increased inositol phosphate formation, which was significantly inhibited by acteoside. Melittin (1 μM) significantly increased histamine release from RBL 2H3 cells in the presence or absence of extracellular Ca2+. Acteoside significantly inhibited 1-μM-melittin-induced histamine release by 74 % in the presence of extracellular Ca2+ and by 71 % in the absence of extracellular Ca2+. These data suggest that the inhibitory effect of acteoside on 1 μM-melittin-induced histamine release may be related to blockage of the calcium-independent pathway. Taken together, these data suggest that melittin has an influence on cellular functions such as intracellular Ca2+ mobilization, the PLC pathway, and exocytosis via various independent signalling pathways in RBL-2H3 cells, and was significantly inhibited by acteoside.
KeywordsActeoside Histamine release Phospholipase C Ca2+ mobilization Melittin
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