Review

The amyloid precursor protein: beyond amyloid

Hui Zheng^1,2 and Edward H Koo^1,2

¹Huffington Center on Aging and Department of Molecular & Human Genetics, Baylor College of Medicine, Houston, TX 77030, USA

²Department of Neurosciences, University of California, San Diego, La Jolla, CA 92093, USA

author email corresponding author email

Molecular Neurodegeneration 2006, 1:5doi:10.1186/1750-1326-1-5

Published:	3 July 2006

Abstract

The amyloid precursor protein (APP) takes a central position in Alzheimer's disease (AD) pathogenesis: APP processing generates the β-amyloid (Aβ) peptides, which are deposited as the amyloid plaques in brains of AD individuals; Point mutations and duplications of APP are causal for a subset of early onset of familial Alzheimer's disease (FAD). Not surprisingly, the production and pathogenic effect of Aβ has been the central focus in AD field. Nevertheless, the biological properties of APP have also been the subject of intense investigation since its identification nearly 20 years ago as it demonstrates a number of interesting putative physiological roles. Several attractive models of APP function have been put forward recently based on in vitro biochemical studies. Genetic analyses of gain- and loss-of-function mutants in Drosophila and mouse have also revealed important insights into its biological activities in vivo. This article will review the current understanding of APP physiological functions.