Activation of phospholipases D and A by amphiphilic cations of cultured LA-N-2 cells is G protein- and protein kinase C-independent.

Journal of lipid mediators Pub Date : 1993-05-01
I N Singh, R Massarelli, J N Kanfer
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引用次数: 0

Abstract

Several amphiphilic cations such as mepacrine, desipramine, didodecyldimethylamine, chlorpromazine, oleylamine and W-7 activated the phospholipase D (PLD) activity of cultured LA-N-2 cells. These compounds, except for oleylamine, provoked the release of fatty acids, suggesting phospholipase A activation. Melittin, a PLA2 stimulator, caused the robust release of the free fatty acids but was a poor PLD activator. Although PLD could be activated by GTP gamma S, the stimulation by these amphiphilic cations was not abolished by GDP beta S, an inhibitor of G protein function. There was no change in the PLD activation by these amphiphilic cations by DiC8, a PKC activator, or by H-7, a PKC inhibitor or in PKC down-regulated cells.

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两亲性阳离子对培养的LA-N-2细胞的磷脂酶D和A的激活与G蛋白和蛋白激酶c无关。
甲帕辛、去西帕明、二十二烷基二甲胺、氯丙嗪、油胺和W-7等两亲性阳离子可激活培养的LA-N-2细胞的磷脂酶D (PLD)活性。这些化合物,除油胺外,刺激脂肪酸的释放,表明磷脂酶A被激活。Melittin是一种PLA2刺激剂,可以引起游离脂肪酸的强烈释放,但PLD激活剂效果不佳。虽然GTP γ S可以激活PLD,但这些两亲性阳离子的刺激不会被GTP β S (G蛋白功能抑制剂)所消除。通过PKC激活剂DiC8或PKC抑制剂H-7或PKC下调细胞,这些两亲性阳离子对PLD的激活没有变化。
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