Studies on Human Porin

Winkelbach H., Walter G., Moryswortmann C., Paetzold G., Hesse D., Zimmermann B., Florke H., Reymann S., Stadtmuller U., Thinnes F.P., Hilschmann N.
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引用次数: 52

Abstract

Eight mouse monoclonal antibodies directed against the acetylated N-terminal part of the type 1 human VDAC Porin 31HL clearly discriminate type 1 and type 2 mammalian porin channels. This is shown by comparing synthetic N-terminal peptides of either channel type in Western dot blots or by ELISA. The data support the specificity of the anti-Porin 31HL antibodies and thus give further support to our recent observations on extramitochondrial expression of VDAC. In the plasmalemma of different mammalian cells VDAC forms part of an ubiquitous chloride channel complex, which in patch clamp measurements may figure as the outwardly rectifying depolarization-induced chloride channel that is affected in cystic fibrosis.

人类孔蛋白的研究
针对1型人VDAC孔蛋白31HL乙酰化n端部分的8种小鼠单克隆抗体可明显区分1型和2型哺乳动物孔蛋白通道。这是通过比较两种通道类型的合成n端肽(Western dot blots或ELISA)来证明的。这些数据支持了抗porin 31HL抗体的特异性,从而进一步支持了我们最近对VDAC的线粒体外表达的观察。在不同哺乳动物细胞的质膜中,VDAC形成了无处不在的氯离子通道复合物的一部分,在膜片钳测量中,它可能被认为是囊性纤维化中受影响的向外整流去极化诱导的氯离子通道。
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