Amyloidogenic processing of beta-amyloid precursor protein in intracellular compartments.

Kulandaivelu S Vetrivel, Gopal Thinakaran

Journal: Neurology 2006;66(2 Suppl 1):S69-73

PMID: 16432149

Abstract

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 Abeta 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 beta- 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.

Address: Department of Neurobiology, Pharmacology and Physiology, University of Chicago, Chicago, IL 60637, USA.

DOI: 10.1212/01.wnl.0000192107.17175.39

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MeSH Terms: Adult, Age of Onset, Aged, Alzheimer Disease, Amino Acid Sequence, Amyloid Precursor Protein Secretases, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Amyloidosis, Familial, Aspartic Acid Endopeptidases, Cell Compartmentation, Down Syndrome, Endocytosis, Endopeptidases, Endoplasmic Reticulum, Humans, Membrane Microdomains, Membrane Proteins, Middle Aged, Molecular Sequence Data, Plaque, Amyloid, Presenilin-1, Presenilin-2, Protein Processing, Post-Translational