PT  - JOURNAL ARTICLE
AU  - A Ferreira
AU  - A Caceres
AU  - KS Kosik
TI  - Intraneuronal compartments of the amyloid precursor protein
AID  - 10.1523/JNEUROSCI.13-07-03112.1993
DP  - 1993 Jul 01
TA  - The Journal of Neuroscience
PG  - 3112--3123
VI  - 13
IP  - 7
4099  - http://www.jneurosci.org/content/13/7/3112.short
4100  - http://www.jneurosci.org/content/13/7/3112.full
SO  - J. Neurosci.1993 Jul 01; 13
AB  - 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.