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P1–395: The function of amyloid precursor protein (APP) in cholinergic system
Author(s) -
Wang Baiping,
Zheng Hui
Publication year - 2006
Publication title -
alzheimer's and dementia
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.713
H-Index - 118
eISSN - 1552-5279
pISSN - 1552-5260
DOI - 10.1016/j.jalz.2006.05.773
Subject(s) - cholinergic , acetylcholine , basal forebrain , cholinergic neuron , amyloid precursor protein , neurotransmitter , neuroscience , synapse , knockout mouse , neuromuscular junction , vesicular acetylcholine transporter , chemistry , microbiology and biotechnology , choline acetyltransferase , medicine , biology , alzheimer's disease , endocrinology , biochemistry , central nervous system , receptor , disease
Background: Basal forebrain cholinergic dysfunction is a early and consistent feature of Alzheimer’s disease (AD). The reason for this selective vulnerability of cholinergic neurons in AD is poorly understood. Genetic and biochemical studies have established a pivotal role of APP in the pathogenesis of AD. However, the physiological function of APP, particularly in cholinergic system, remains elusive. Objective(s): Our study is aimed at dissecting the function of APP in cholinergic system. Methods: Using neuromuscular synapse as a cholinergic synaptic model system, in which acetylcholine is the only neurotransmitter, several key molecules important for cholinergic function were examined in APP knockout and APP/APLP2 double knockout mice. Results: We found a profound mislocalization of High Affinity Choline Transporter (CHT), a molecule that mediates the rate-limiting step in choline uptake and acetylcholine synthesis, in the neuromuscular junction of APP and APP/APLP2 double knockout mice. A decreased choline uptake in the brains of APP/APLP2 double knockout mice has been demonstrated, suggesting a diminished cholinergic function in these animals. Conclusions: We conclude that APP family of proteins is required for maintaining normal cholinergic synaptic function via directly regulating the presynaptic CHT activity.

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