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Physiological mouse brain Abeta levels are not related to the phosphorylation state of threonine-668 of Alzheimer's APP.
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| Title: | Physiological mouse brain Abeta levels are not related to the phosphorylation state of threonine-668 of Alzheimer's APP. |
| Authors: | Sano, Yoshitake Browse this author | | Nakaya, Tadashi Browse this author →KAKEN DB | | Pedrini, Steve Browse this author | | Takeda, Shizu Browse this author | | Iijima-Ando, Kanae Browse this author | | Iijima, Koichi Browse this author | | Mathews, Paul M Browse this author | | Itohara, Shigeyoshi Browse this author →KAKEN DB | | Gandy, Sam Browse this author | | Suzuki, Toshiharu Browse this author →KAKEN DB |
| Issue Date: | 2006 |
| Publisher: | The Public Library of Science |
| Journal Title: | PloS one |
| Volume: | 1 |
| Start Page: | e51 |
| Publisher DOI: | 10.1371/journal.pone.0000051 |
| PMID: | 17183681 |
| Abstract: | 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. |
| Rights: | http://creativecommons.org/licenses/by/3.0/ |
| Type: | article |
| URI: | http://hdl.handle.net/2115/51693 |
| Appears in Collections: | 薬学研究院 (Faculty of Pharmaceutical Sciences) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 鈴木 利治
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