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Published online before print December 16, 2005, doi:10.1212/01.wnl.0000192107.17175.39)
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NEUROLOGY 2006;66:S69-S73
© 2006 American Academy of Neurology

Amyloidogenic processing of β-amyloid precursor protein in intracellular compartments

Kulandaivelu S. Vetrivel, PhD and Gopal Thinakaran, PhD

From the Department of Neurobiology, Pharmacology and Physiology, University of Chicago, Chicago, IL.

Address correspondence and reprint requests to Dr. Gopal Thinakaran, Department of Neurobiology, Pharmacology and Physiology, University of Chicago, Chicago, IL 60637; e-mail: gopal{at}uchicago.edu

Trafficking and proteolytic processing of amyloid precursor protein (APP) have been the focus of numerous investigations in the past two decades, since the identification of Aβ as the principal component of brain senile plaques and the cloning of APP cDNA. Tremendous progress has been made in the recent past toward the characterization of β- and {gamma}-secretases. Here, we review the salient features of Alzheimer disease amyloidogenesis, and discuss the current knowledge on APP trafficking and amyloidogenic processing of APP in intracellular membrane compartments and microdomains.

This article was previously published in electronic format as an Expedited E-Pub at www.neurology.org.

Supported by grants from the National Institutes of Health, Alzheimer’s Association, and American Health Assistance Foundation (G.T.), and a fellowship from the Alzheimer Disease Research Fund of Illinois Department of Public Health (K.S.V.).

Disclosure: The authors report no conflicts of interest.

Received June 22, 2005. Accepted in final form October 14, 2005.




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