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Updated: Aug 11, 2026

Purification and Aggregation of the Amyloid Precursor Protein Intracellular Domain
Published on: August 28, 2012
Intraneuronal compartments of the amyloid precursor protein
A Ferreira1, A Caceres, K S Kosik
1Harvard Medical School, Department of Medicine (Division of Neurology), Brigham and Women's Hospital, Boston, Massachusetts 02115.
Abstract:
The amyloid precursor protein (APP) is the parent molecule from which beta-amyloid protein is cleaved and deposits as amyloid fibrils in the senile plaques of Alzheimer's disease. Its primary structure resembles a receptor; however, no ligand has been identified. In growing hippocampal neurons APP is localized to growth cones. APP immunoreactivity was highly enriched in the axons of mature cultured neurons, where it appears as a specialization of the axonal membrane. Its anterograde translocation occurs via a kinesin-based motor. Following cytosolic acidification, APP colocalizes with late endosomes that get redistributed from the neuronal cell body to the processes. APP colocalizes in cultured hippocampal neurons to clathrin-immunoreactive clusters of vesicular-like structures. The finding lends additional credence to the possibility that APP could function as a receptor.
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