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J. Biol. Chem., Vol. 283, Issue 44, 29615-29619, October 31, 2008

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Minireview

Amyloid Precursor Protein Trafficking, Processing, and Function^*

Gopal Thinakaran¹ and Edward H. Koo²

From the Departments of Neurobiology, Neurology, and Pathology, The University of Chicago, Chicago, Illinois 60637 and the Department of Neurosciences, University of California, San Diego, La Jolla, California 92093

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.

^* This work was supported, in whole or in part, by National Institutes of Health Grants AG019070 and AG021495 (to G. T.) and AG12376 and AG032179 (to E. H. K.) from NIA. This work was also supported by the American Health Assistance Foundation Alzheimer's Disease Research Program and the Alzheimer's Association (to G. T.) and by the Glenn Foundation for Medical Research (to E. H. K.). This is the first article of eleven in the Thematic Minireview Series on the Molecular Basis of Alzheimer Disease. This minireview will be reprinted in the 2008 Minireview Compendium, which will be available in January, 2009.

¹ To whom correspondence may be addressed. E-mail: gopal{at}uchicago.edu. ² To whom correspondence may be addressed. E-mail: edkoo{at}ucsd.edu.

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