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Journal of Neuroscience, Vol 13, 3112-3123, Copyright © 1993 by Society for Neuroscience
Intraneuronal compartments of the amyloid precursor protein
A Ferreira, A Caceres and KS Kosik
Harvard Medical School, Department of Medicine (Division of Neurology), Brigham and Women's Hospital, Boston, Massachusetts 02115.
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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