Melittin exerts multiple effects on the release of free fatty acids from L1210 cells: lack of selective activation of phospholipase A2 by melittin.
Melittin exerts multiple effects on the release of free fatty acids from L1210 cells: lack of selective activation of phospholipase A2 by melittin.
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蜂毒肽对 L1210 细胞释放游离脂肪酸具有多种作用：蜂毒肽无法选择性激活磷脂酶 A2。
DOI：
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发表时间：
2001
影响因子：
3.9
通讯作者：
M. Choi
中科院分区：
文献类型：
--
作者：
Sang Yoon Lee;H. Park;Soo Jae Lee;M. Choi
蜂毒素是一种磷脂酶A2 （PLA2）激活剂，但其对PLA2的选择性作用尚不确定。我们使用不同的抑制剂检测了蜂毒素对L1210细胞游离脂肪酸（FFAs）释放的选择性。通过HPLC和GLC进行的全身脂质分析显示，蜂毒素诱导了多种游离脂肪酸的释放，包括饱和、单不饱和和多不饱和游离脂肪酸。各种PLA2抑制剂对蜂毒素诱导的花生四烯酸（AA）和棕榈酸（PAL）释放的影响微乎其微。特异性抑制剂磷脂酰肌醇-磷脂酶C （U73122）和二酰基甘油脂肪酶（RHC80267）对AA和PAL的释放均有显著的抑制作用。这些结果表明，蜂毒素诱导的FFA释放很可能是由于多种类型的脂肪酶的多重参与。由于BAPTA/AM是一种细胞内Ca2+螯合剂，不影响FFA的释放，因此蜂毒素注入的Ca2+似乎不是FFA释放的关键因素。洋地黄苷（一种膜渗透剂）对蜂毒素诱导的游离脂肪酸释放的模拟表明，蜂毒素的膜扰动作用可能是导致游离脂肪酸释放的原因。Melittin还诱导其他细胞系（包括P388D1和HL60）释放多种FFAs。在L1210细胞中观察到的快速蜂毒素刺激磷脂酶D （PLD）似乎与FFA的稳定释放没有直接关系，这一事实表明，PLD没有被RHC80267阻断。鉴于蜂毒素对细胞脂质组成的多重影响，我们得出结论，蜂毒素既不排他地释放任何单一的FFA，也不选择性地激活L1210细胞中的PLA2。讨论了蜂窝蜂素作为PLA2活化剂的问题。
Melittin is known as a phospholipase A2 (PLA2) activator, but the selectivity of its effect on PLA2 is uncertain. We examined the selectivity of melittin effect on the release of free fatty acids (FFAs) from L1210 cells using various inhibitors. A systemic lipid analysis by HPLC and GLC revealed that melittin induced release of various FFAs including saturated, monounsaturated, and polyunsaturated FFAs. Various PLA2 inhibitors examined exerted only minimal effects on the melittin-induced arachidonic acid (AA) and palmitic acid (PAL) releases. Specific inhibitors of phosphatidylinositol-phospholipase C (U73122) and diacylglycerol lipase (RHC80267) exerted significant inhibitory effects on both AA and PAL releases. These results suggest that melittin-induced FFA release is most likely due to multiple participations of various types of lipases. Since BAPTA/AM, an intracellular Ca2+ chelator, did not influence the FFA release, the Ca2+ influxed by melittin appeared not to be a key factor for the FFA release. The mimicking of the melittin-induced FFA release by digitonin, a membrane-permeabilizing agent, implies that the membrane-perturbing action of melittin is likely the cause of the FFA release. Melittin also induced release of multiple FFAs from other cell lines including P388D1 and HL60. The rapid melittin-stimulated phospholipase D (PLD) observed in L1210 cells appeared not directly related to the steady release of FFA, as indicated by the fact that the PLD was not blocked by RHC80267. In view of melittin's multiple effects on the composition of cellular lipids, we conclude that melittin does neither exclusively release any single FFA nor selectively activate PLA2 in L1210 cells. The problem of using melittin as a PLA2 activator is discussed.
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