title: Intraneuronal compartments of the amyloid precursor protein.
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.
authors.affiliation: Harvard Medical School, Department of Medicine (Division of Neurology), Brigham and Women's Hospital, Boston, Massachusetts 02115.
authors.forename: A
authors.initials: A
authors.lastname: Ferreira
authors.forename: A
authors.initials: A
authors.lastname: Caceres
authors.forename: K S
authors.initials: KS
authors.lastname: Kosik
mesh_terms: D016564:Amyloid beta-Protein Precursor / Q000032:analysis / Q000096:biosynthesis / Q000378:metabolism*; D000818:Animals; D001369:Axons / Q000378:metabolism* / Q000648:ultrastructure; D001483:Base Sequence; D002478:Cells, Cultured; D004622:Embryo, Mammalian; D006624:Hippocampus / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D016547:Kinesins / Q000378:metabolism; D008969:Molecular Sequence Data; D009474:Neurons / Q000378:metabolism* / Q000648:ultrastructure*; D016376:Oligonucleotides, Antisense; D015388:Organelles / Q000378:metabolism* / Q000648:ultrastructure; D051381:Rats
chemical_list: D016564:Amyloid beta-Protein Precursor; D016376:Oligonucleotides, Antisense; D016547:Kinesins