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Amyloid Precursor Protein Metabolism in Primary Cell Cultures of Neurons, Astrocytes, and Microglia
Author(s) -
LeBlanc Andréa C.,
Xue Run,
Gambetti Pierluigi
Publication year - 1996
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1996.66062300.x
Subject(s) - microglia , amyloid precursor protein , senile plaques , p3 peptide , alzheimer's disease , immunoprecipitation , cerebral cortex , gene isoform , microbiology and biotechnology , biology , alpha secretase , amyloid beta , metabolism , astrocyte , amyloid (mycology) , biochemistry of alzheimer's disease , biochemistry , neuroscience , peptide , central nervous system , pathology , gene , immunology , medicine , inflammation , disease , botany
Amyloid precursor protein (APP) gives rise by proteolytic processing to the amyloid β peptide (Aβ) found abundantly in cerebral senile plaques of individuals with Alzheimer's disease. APP is highly expressed in the brain. To assess the source of cerebral Aβ, the metabolism of APP was investigated in the major cell types of the newborn rat cerebral cortex by pulse/chase labeling and immunoprecipitation of the APP and APP metabolic fragments. We describe a novel C‐terminally truncated APP isoform that appears to be made only in neurons. The synthesis, degradation, and metabolism of APP were quantified by phosphorimaging in neurons, astrocytes, and microglia. The results show that although little APP is metabolized through the amyloidogenic pathways in each of the three cultures, neurons appear to generate more Aβ than astrocytes or microglia.