Molecular cloning of human Fe65L2 and its interaction with the Alzheimer's β-amyloid precursor protein

被引：38

作者：

Tanahashi, H ^{[1
]}

Tabira, T ^{[1
]}

机构：

[1] Natl Inst Neurosci, Div Demyelinating Dis & Aging, Tokyo 1878502, Japan

来源：

NEUROSCIENCE LETTERS | 1999年 / 261卷 / 03期

关键词：

Alzheimer's disease; Fe65L2; beta-amyloid precursor protein; APP; APP-like proteins; PID/PTB element; WW domain;

D O I：

10.1016/S0304-3940(98)00995-1

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

We report the cDNA sequence of human Fe65L2. The human Fe65L2 encoded 486 amino acids; the deduced amino acid sequence was shorter by 18 amino acids than the rat protein and had 86% identity to the rat protein Three protein-protein interaction domains, a WW and two PID/PTB elements, were conserved among the Fe65 protein family. Human Fe65L2 mRNA was expressed in various tissues; a transcript of about 2.2 kb was mainly expressed in the brain. A splicing variant lacking two amino acids in the first PID/PTB element was detected. We also confirmed that the carboxyl-terminal region of PID/PTB of the Fe65L2 interacted with the intracellular domain of the Alzheimer's P-amyloid precursor protein (APP) and APP-like proteins. (C) 1999 Elsevier Science Ireland Ltd. All rights reserved.

引用

页码：143 / 146

页数：4

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