Molecular cloning and sequence analysis of a human brain cDNA of an Alzheimer amyloid precursor (APP) interacting protein
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Date
1999-05-01T00:00:00Z
Authors
Liang, Binhua
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Abstract
Alzheimer disease (AD) is the most common form of dementia. It is characterized by the accumulation of beta-amyloid peptides (B-AP) derived from Alzheimer amyloid precursor protein (APP) and neurofibrillary tangles in the human brain. Knowledge of the normal functions of APP will provide clues to our understanding of the pathogenesis of Alzheimer disease. The location of APP (membrane-bound) and its structural features are characteristics of plasma membrane receptors such as integrins and epidermal growth factor receptors. Analysis of a protein interaction network from its intracellular carboxyl-terminal domain (APP COOH) indicated that APP might be involved in signal transduction pathways. In order to understand the functions of APP, it is important to identify its effector binding proteins. To address this question, the yeast-two hybrid system was employed. This system is based on a Gal-4 transcriptional assay for detecting specific protein-protein interactions in yeast. This can be used to screen libraries for genes encoding proteins that interact with a known "bait" protein. (Abstract shortened by UMI.)