Pavlov P F, Glaser E
Arrhenius Laboratory for Natural Sciences, Stockholm University, Stockholm, 10691, Sweden.
Biochem Biophys Res Commun. 1998 Nov 9;252(1):84-91. doi: 10.1006/bbrc.1998.9590.
In this paper we describe for the first time the inhibitory effect of three amphiphilic cations, trifluoperazine, propranolol and dibucaine on mitochondrial protein import. The amphiphilic cations did not affect binding of mitochondrial precursor proteins to mitochondria. Import into mitoplasts was affected in a similar manner to intact mitochondria, indicating that the protein import machinery of the inner membrane of mitochondria was responsible for the observed effect. At concentrations which completely inhibited protein import, the amphiphilic cations did not affect the membrane potential (DeltaPsi) across the inner membrane. The inhibitory potency of amphiphilic cations reflects their lipid/water partition coefficient and relatively high concentrations of the drugs were required for complete inhibition, hence we propose that the mechanism of protein import inhibition by amphiphilic cations is due to membrane perturbing effects. We discuss the implications of our findings in view of the possible connection between various inner mitochondrial membrane channels and the protein import pore.
在本文中,我们首次描述了三种两亲性阳离子(三氟拉嗪、普萘洛尔和丁卡因)对线粒体蛋白质导入的抑制作用。这些两亲性阳离子并不影响线粒体前体蛋白与线粒体的结合。导入线粒体膜间腔的过程与导入完整线粒体的过程受到类似影响,这表明线粒体内膜的蛋白质导入机制是造成所观察到的效应的原因。在完全抑制蛋白质导入的浓度下,两亲性阳离子并不影响内膜两侧的膜电位(ΔΨ)。两亲性阳离子的抑制效力反映了它们的脂/水分配系数,并且完全抑制需要相对高浓度的药物,因此我们提出两亲性阳离子抑制蛋白质导入的机制是由于膜扰动效应。鉴于线粒体内膜各种通道与蛋白质导入孔之间可能存在的联系,我们讨论了我们研究结果的意义。