Intraneuronal compartments of the amyloid precursor protein

A. Ferreira, A. Caceres, K. S. Kosik*

*Corresponding author for this work

Research output: Contribution to journalArticle

124 Scopus citations

Abstract

The amyloid precursor protein (APP) is the parent molecule from which β- 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.

Original languageEnglish (US)
Pages (from-to)3112-3123
Number of pages12
JournalJournal of Neuroscience
Volume13
Issue number7
StatePublished - Jan 1 1993

Keywords

  • antisense
  • clathrin
  • endocytosis
  • endosomes
  • hippocampal neurons
  • kinesin

ASJC Scopus subject areas

  • Neuroscience(all)

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