Physiological mouse brain Abeta levels are not related to the phosphorylation state of threonine-668 of Alzheimer's APP.
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概要
- 論文の詳細を見る
Amyloid-beta peptide species ending at positions 40 and 42 (Abeta40, Abeta42) are generated by the proteolytic processing of the Alzheimer's amyloid precursor protein (APP). Abeta peptides accumulate in the brain early in the course of Alzheimer's disease (AD), especially Abeta42. The cytoplasmic domain of APP regulates intracellular trafficking and metabolism of APP and its carboxyl-terminal fragments (CTFalpha, CTFbeta). The role of protein phosphorylation in general, and that of the phosphorylation state of APP at threonine-668 (Thr668) in particular, has been investigated in detail by several laboratories (including our own). Some investigators have recently proposed that the phosphorylation state of Thr668 plays a pivotal role in governing brain Abeta levels, prompting the current study.
- The Public Library of Scienceの論文
著者
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Suzuki Toshiharu
北海道大学 薬学研究科
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Nakaya Tadashi
Graduate School Of Pharmaceutical Sciences Hokkaido University
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Suzuki Toshiharu
Graduate School Of Pharmaceutical Sciences Hokkaido University
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- Increased amyloidogenic processing of transgenic human APP in X11-like deficient mouse brain
- Physiological mouse brain Abeta levels are not related to the phosphorylation state of threonine-668 of Alzheimer's APP.
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