Inhibition of Bax channel-forming activity by Bcl-2
Inhibition of Bax channel-forming activity by Bcl-2
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DOI：
10.1126/science.277.5324.370
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发表时间：
1997-07-18
期刊：
影响因子：
56.9
通讯作者：
Martinou, JC
中科院分区：
文献类型：
--
作者：
Antonsson, B;Conti, F;Martinou, JC
Bcl-2家族的蛋白质是细胞内膜相关蛋白质，其通过迄今未知的机制正向或负向调节程序性细胞死亡（凋亡）。Bax，Bcl-2家族的促凋亡成员，被证明在脂质膜中形成通道。Bax在中性和酸性条件下均可触发脂质体释放羧基荧光素，在生理pH条件下，Bcl-2、Bcl-2可阻断脂质体释放羧基荧光素，而在酸性条件下，脂质体释放羧基荧光素。在平面脂质双层中，Bax形成pH和电压依赖性离子传导通道。因此，Bax的促凋亡作用可能是通过Bcl-2可以拮抗的内在成孔活性引起的。
Proteins of the Bcl-2 family are intracellular membrane-associated proteins that regulate programmed cell death (apoptosis) either positively or negatively by as yet unknown mechanisms. Bax, a pro-apoptotic member of the Bcl-2 family, was shown to form channels in lipid membranes. Bax triggered the release of liposome-encapsulated carboxyfluorescein at both neutral and acidic pH. AS physiological pH, release could be blocked by Bcl-2, Bcl-2, in contrast, triggered carboxyfluorescein release at acidic pH only. In planar lipid bilayers, Bax formed pH- and voltage-dependent ion-conducting channels. Thus, the pro-apoptotic effects of Bax may be elicited through an intrinsic pore-forming activity that can be antagonized by Bcl-2.