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Expression of tau reduces secretion of Aβ without altering the amyloid precursor protein content in CHOsw cells
Author(s) -
Zhao Zhong,
Ksiezak-Reding Hanna,
Wang Jun,
Pasinetti Giulio Maria
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.02.067
Subject(s) - amyloid precursor protein , secretion , golgi apparatus , chemistry , amyloid precursor protein secretase , microbiology and biotechnology , insulin degrading enzyme , p3 peptide , microtubule , amyloid (mycology) , enzyme , biochemistry , alzheimer's disease , medicine , biology , cell , disease , inorganic chemistry
Insoluble deposits of tau and amyloid precursor protein (APP) peptides Aβ characterize Alzheimer's disease. We studied the role of tau in the metabolism of APP in cells stably expressing APP Swedish mutation (CHOsw). Transient expression of tau in CHOsw cells caused morphological changes, bundling of microtubules and perinuclear aggregation of Golgi‐derived vesicles. It also reduced the secretion of Aβ 1–40 and Aβ 1–42 without altering the APP steady state levels. This was accompanied by a reduction in the γ‐secretase and an increase in the insulin degrading enzyme activities. Our results suggest that tau may play an inhibitory role in the amyloidogenic activity of APP.