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人类E-钙黏蛋白的分子克隆表明钙黏蛋白超家族存在一个新的亚分类。

Molecular cloning of human E-cadherin suggests a novel subdivision of the cadherin superfamily.

作者信息

Rimm D L, Morrow J S

机构信息

Department of Pathology, Yale University School of Medicine, New Haven, CT 06510.

出版信息

Biochem Biophys Res Commun. 1994 May 16;200(3):1754-61. doi: 10.1006/bbrc.1994.1656.

DOI:10.1006/bbrc.1994.1656
PMID:8185635
Abstract

The gene encoding full-length human E-cadherin has been cloned and sequenced from liver and colon cDNA libraries (GenBank Accession #L08599). The predicted molecular mass of the unglycosylated and unprocessed protein is 97,000. The human protein conserves most features of the classical cadherins. In its cytoplasmic domain, two approximately 30-35 aminoacid conserved sequence motifs are recognized. These cadherin homology domains have been termed "CH2" and "CH3", and are characteristic of the classical cadherins, but absent or divergent in the more distantly related cadherins such as desmosomal cadherin, T-cadherin, fat, and the human ret oncogene. Given these findings and the importance of cytoplasmic interactions to cadherin function, a subclassification of the cadherin superfamily based on cytoplasmic domain homologies is proposed. This subclassification provides a framework in future studies for understanding the distinct down-stream signaling cascades associated with each cadherin.

摘要

已从肝脏和结肠cDNA文库中克隆并测序了编码全长人E-钙黏蛋白的基因(基因库登录号#L08599)。未糖基化和未加工蛋白质的预测分子量为97,000。人蛋白质保留了经典钙黏蛋白的大多数特征。在其细胞质结构域中,可识别出两个约30 - 35个氨基酸的保守序列基序。这些钙黏蛋白同源结构域被称为“CH2”和“CH3”,是经典钙黏蛋白的特征,但在关系更远的钙黏蛋白如桥粒钙黏蛋白、T-钙黏蛋白、脂肪和人ret癌基因中不存在或有差异。鉴于这些发现以及细胞质相互作用对钙黏蛋白功能的重要性,提出了基于细胞质结构域同源性的钙黏蛋白超家族的亚分类。这种亚分类为未来研究理解与每种钙黏蛋白相关的不同下游信号级联反应提供了一个框架。

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