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钙调蛋白与两种C-CAM亚型的细胞质结构域结合的证据。

Evidence for calmodulin binding to the cytoplasmic domains of two C-CAM isoforms.

作者信息

Edlund M, Obrink B

机构信息

Department of Cell and Molecular Biology, Karolinska Institutet, Stockholm, Sweden.

出版信息

FEBS Lett. 1993 Jul 19;327(1):90-4. doi: 10.1016/0014-5793(93)81046-3.

Abstract

C-CAM (cell-CAM 105) is a transmembrane cell adhesion molecule, belonging to the immunoglobulin superfamily. It is expressed in epithelia, vessel endothelia and leukocytes, and mediates intercellular adhesion in rat hepatocytes by homophilic binding. Two major isoforms (C-CAM1 and C-CAM2) that differ in their cytoplasmic domains occur. A previous study demonstrated that C-CAM can bind calmodulin in a Ca(2+)-dependent manner. In this study we have expressed the cytoplasmic domains of C-CAM1 and C-CAM2 in fusion proteins and measured calmodulin binding by a gel overlay assay, using 125I-labelled calmodulin. Our results indicate that the cytoplasmic domains of both C-CAM1 and C-CAM2 can bind calmodulin.

摘要

C-CAM(细胞黏附分子105)是一种跨膜细胞黏附分子,属于免疫球蛋白超家族。它在上皮细胞、血管内皮细胞和白细胞中表达,并通过同源性结合介导大鼠肝细胞间的黏附。存在两种主要的异构体(C-CAM1和C-CAM2),它们的细胞质结构域不同。先前的一项研究表明,C-CAM能以Ca(2+)依赖的方式结合钙调蛋白。在本研究中,我们在融合蛋白中表达了C-CAM1和C-CAM2的细胞质结构域,并使用125I标记的钙调蛋白通过凝胶覆盖试验测量钙调蛋白结合情况。我们的结果表明,C-CAM1和C-CAM2的细胞质结构域都能结合钙调蛋白。

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