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钙调蛋白对草履虫分离膜片中钙依赖性钠通道的激活作用。

Calmodulin activation of calcium-dependent sodium channels in excised membrane patches of Paramecium.

作者信息

Saimi Y, Ling K Y

机构信息

Laboratory of Molecular Biology, University of Wisconsin-Madison 53706.

出版信息

Science. 1990 Sep 21;249(4975):1441-4. doi: 10.1126/science.2169650.

Abstract

Calmodulin is a calcium-binding protein that participates in the transduction of calcium signals. The electric phenotypes of calmodulin mutants of Paramecium have suggested that the protein may regulate some calcium-dependent ion channels. Calcium-dependent sodium single channels in excised patches of the plasma membrane from Paramecium were identified, and their activity was shown to decrease after brief exposure to submicromolar concentrations of calcium. Channel activity was restored to these inactivated patches by adding calmodulin that was isolated from Paramecium to the cytoplasmic surface. This restoration of channel activity did not require adenosine triphosphate and therefore, probably resulted from direct binding of calmodulin, either to the sodium channel itself or to a channel regulator that was associated with the patch membrane.

摘要

钙调蛋白是一种参与钙信号转导的钙结合蛋白。草履虫钙调蛋白突变体的电表型表明,该蛋白可能调节一些钙依赖性离子通道。在草履虫质膜的切除膜片中鉴定出了钙依赖性钠单通道,并且在短暂暴露于亚微摩尔浓度的钙后,其活性降低。通过将从草履虫中分离出的钙调蛋白添加到细胞质表面,这些失活膜片的通道活性得以恢复。通道活性的这种恢复不需要三磷酸腺苷,因此,可能是由于钙调蛋白直接与钠通道本身或与膜片膜相关的通道调节剂结合所致。

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