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- W2067407535 abstract "In order to investigate the regulation of presynaptic phospholipase D (PLD) activity by calcium and G proteins, we established a permeabilization procedure for rat cortical synaptosomes using Staphylococcus aureus α‐toxin (30–100 μg/ml). In permeabilized synaptosomes, PLD activity was significantly stimulated when the concentration of free calcium was increased from 0.1 μM to 1 μM. This activation was inhibited in the presence of KN‐62 (1 μM), an inhibitor of calcium/calmodulin‐dependent kinase II (CaMKII), but not by the protein kinase C inhibitor, Ro 31‐8220 (1–10 μM). Synaptosomal PLD activity was also stimulated in the presence of 1 μM GTPγS. When Rho proteins were inhibited by pretreatment of the synaptosomes with Clostridium difficile toxin B (TcdB; 1–10 ng/ml), the effect of GTPγS was significantly reduced; in contrast, brefeldin A (10–100 μM), an inhibitor of ARF activation, was ineffective. Calcium stimulation of PLD was inhibited by TcdB, but GTPγS‐dependent activation was insensitive to KN‐62. We conclude that synaptosomal PLD is activated in a pathway which sequentially involves CaMKII and Rho proteins." @default.
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- W2067407535 date "1998-12-04" @default.
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- W2067407535 title "Regulation of phospholipase D activity in synaptosomes permeabilized with<i>Staphylococcus aureus</i>α-toxin" @default.
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- W2067407535 doi "https://doi.org/10.1016/s0014-5793(98)01479-3" @default.
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