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肌动蛋白与肝细胞中整合素α1亚基的细胞质尾部结合。

Actin binds to the cytoplasmic tail of alpha 1 subunit of integrin in hepatocytes.

作者信息

Menon B, Sudhakaran P R

机构信息

Department of Biochemistry, University of Kerala, Kariavattom, Trivandrum, India.

出版信息

Indian J Biochem Biophys. 2000 Apr;37(2):81-5.

Abstract

alpha 1 beta 1-Integrin is a common receptor for laminin and collagen IV on hepatocytes. The interactions of intracellular domain of integrins with cytoplasmic elements are critical in the initiation and transduction of signals. In order to understand the nature of cytoplasmic components that can interact with cytoplasmic domain of alpha 1 integrin, cytoplasmic extracts of monolayers of rat hepatocytes were subjected to chromatography over an affinity column prepared by coupling a 60-mer synthetic cytoplasmic tail of alpha 1 subunit. SDS-PAGE analysis of the eluate showed the presence of a 47 kDa protein. Dot-Blot assay using radio-iodinated 47 kDa protein showed the binding of the protein to 60-mer C tail in a concentration dependent manner. Immunoblot analysis using specific antibodies showed that the 47 kDa protein is actin.

摘要

α1β1整合素是肝细胞上纤连蛋白和IV型胶原蛋白的共同受体。整合素细胞内结构域与细胞质成分的相互作用在信号的起始和转导中至关重要。为了了解能够与α1整合素细胞质结构域相互作用的细胞质成分的性质,将大鼠肝细胞单层的细胞质提取物通过连接α1亚基60聚体合成细胞质尾巴制备的亲和柱进行层析。洗脱液的SDS-PAGE分析显示存在一种47 kDa的蛋白质。使用放射性碘化的47 kDa蛋白质进行的点印迹分析表明该蛋白质以浓度依赖的方式与60聚体C尾巴结合。使用特异性抗体进行的免疫印迹分析表明47 kDa的蛋白质是肌动蛋白。

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