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Association of TrkA and APP Is Promoted by NGF and Reduced by Cell Death-Promoting Agents
https://oist.repo.nii.ac.jp/records/193
https://oist.repo.nii.ac.jp/records/1932997a31b-a8df-4fca-983e-b6b67bab1f2c
名前 / ファイル | ライセンス | アクション |
---|---|---|
fnmol-10-00015 (6.8 MB)
|
Creative Commons Attribution 4.0 International
(http://creativecommons.org/licenses/by/4.0/) |
Item type | 学術雑誌論文 / Journal Article(1) | |||||
---|---|---|---|---|---|---|
公開日 | 2017-12-26 | |||||
タイトル | ||||||
タイトル | Association of TrkA and APP Is Promoted by NGF and Reduced by Cell Death-Promoting Agents | |||||
タイトル | ||||||
言語 | en | |||||
タイトル | Association of TrkA and APP Is Promoted by NGF and Reduced by Cell Death-Promoting Agents | |||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | journal article | |||||
著者(英) |
Canu, Nadia
× Canu, Nadia× Pagano, Ilaria× La Rosa, Luca Rosario× Pellegrino, Marsha× Ciotti, Maria Teresa× Mercanti, Delio× Moretti, Fabiola× Sposato, Valentina× Triaca, Viviana× Petrella, Carla× Maruyama, Ichiro N.× Levi, Andrea× Calissano, Pietro |
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書誌情報 |
en : Frontiers in Molecular Neuroscience 巻 10, p. 15, 発行日 2017-01-31 |
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抄録 | ||||||
内容記述タイプ | Other | |||||
内容記述 | The amyloid precursor protein (APP) interacts with the tropomyosin receptor kinase A (TrkA) in normal rat, mouse, and human brain tissue but not in Alzheimer's disease (AD) brain tissue. However, it has not been reported whether the two proteins interact directly, and if so, which domains are involved. Clarifying these points will increase our understanding of the role and regulation of the TrkA/APP interaction in normal brain functioning as well as in AD. Here we addressed these questions using bimolecular fluorescence complementation (BiFC) and the proximity ligation assay (PLA). We demonstrated that exogenously expressed APP and TrkA associate through their juxtamembrane/transmembrane domains, to form a complex that localizes mainly to the plasma membrane, endoplasmic reticulum (ER) and Golgi. Formation of the complex was inhibited by p75NTR, ShcC and Mint-2. Importantly, we demonstrated that the association between endogenous APP and TrkA in primary septal neurons were modified by NGF, or by drugs that either inhibit ER-to-Golgi transport or perturb microtubules and microfilaments. Interestingly, several agents that induce cell death [amyloid beta (A beta)-peptide, staurosporine and rapamycin], albeit via different mechanisms, all caused dissociation of APP/TrkA complexes and increased production of C-terminal fragment (beta-CTF) APP fragment. These findings open new perspectives for investigating the interplay between these proteins during neurodegeneration and AD. | |||||
出版者 | ||||||
出版者 | Frontiers Media S.A | |||||
ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 1662-5099 | |||||
PubMed番号 | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | PMID | |||||
関連識別子 | info:pmid/28197073 | |||||
DOI | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | DOI | |||||
関連識別子 | info:doi/10.3389/fnmol.2017.00015 | |||||
権利 | ||||||
権利情報 | © 2017 Canu, Pagano, La Rosa, Pellegrino, Ciotti, Mercanti, Moretti, Sposato, Triaca, Petrella, Maruyama, Levi and Calissano. | |||||
関連サイト | ||||||
識別子タイプ | URI | |||||
関連識別子 | http://journal.frontiersin.org/article/10.3389/fnmol.2017.00015/full | |||||
著者版フラグ | ||||||
出版タイプ | VoR | |||||
出版タイプResource | http://purl.org/coar/version/c_970fb48d4fbd8a85 |