Amyloid Precursor Protein Trafficking, Processing, and Function
Department of Neurobiology, The University of Chicago, Chicago, Illinois 60637, USA. Journal of Biological Chemistry
(Impact Factor: 4.57).
10/2008; 283(44):29615-9. DOI: 10.1074/jbc.R800019200
Intracellular trafficking and proteolytic processing of amyloid precursor protein (APP) have been the focus of numerous investigations
over the past two decades. APP is the precursor to the amyloid β-protein (Aβ), the 38–43-amino acid residue peptide that is
at the heart of the amyloid cascade hypothesis of Alzheimer disease (AD). Tremendous progress has been made since the initial
identification of Aβ as the principal component of brain senile plaques of individuals with AD. Specifically, molecular characterization
of the secretases involved in Aβ production has facilitated cell biological investigations on APP processing and advanced
efforts to model AD pathogenesis in animal models. This minireview summarizes salient features of APP trafficking and amyloidogenic
processing and discusses the putative biological functions of APP.
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