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. 2011 Apr 28;6(1):27.
doi: 10.1186/1750-1326-6-27.

Biology and pathophysiology of the amyloid precursor protein

Hui Zheng  1 , Edward H Koo
Affiliations

Biology and pathophysiology of the amyloid precursor protein

Hui Zheng et al. Mol Neurodegener. .

Abstract

The amyloid precursor protein (APP) plays a central role in the pathophysiology of Alzheimer's disease in large part due to the sequential proteolytic cleavages that result in the generation of β-amyloid peptides (Aβ). Not surprisingly, the biological properties of APP have also been the subject of great interest and intense investigations. Since our 2006 review, the body of literature on APP continues to expand, thereby offering further insights into the biochemical, cellular and functional properties of this interesting molecule. Sophisticated mouse models have been created to allow in vivo examination of cell type-specific functions of APP together with the many functional domains. This review provides an overview and update on our current understanding of the pathobiology of APP.

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Figures

Figure 1
Figure 1
Comparison of protein sequences of C. elegans APL-1, Drosophila APPL, Zebrafish APPa, Xenopus APP-A and the human APP, APLP1 and APLP2. Purple sequences indicate identical homology while green references similar amino acids. Homologous regions include the E1 domain (light blue line), E2 domain (yellow line) and sequences within the C-terminus such as the conserved Thr site (arrow head) and YENPTY motif (black box). The transmembrane domain and Aβ sequence are noted by the blue and red boxes respectively.
Figure 2
Figure 2
Schematic diagram of APP processing pathways (not drawn to scale). Aβ domain is highlighted in red. For simplicity, only one cleavage site is shown for each enzyme. EC: extracellular; TM: transmembrane; IC: intracellular.
See this image and copyright information in PMC

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