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Dilysine retrieval signal-containing p24 proteins collaborate in inhibiting γ-cleavage of amyloid precursor protein.
http://hdl.handle.net/10422/2996
http://hdl.handle.net/10422/2996cd2ae50a-a596-4f13-b43e-d3950c8841a0
名前 / ファイル | ライセンス | アクション |
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j.1471-4159.2010.06977.x.pdf (1.9 MB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2013-03-19 | |||||
タイトル | ||||||
タイトル | Dilysine retrieval signal-containing p24 proteins collaborate in inhibiting γ-cleavage of amyloid precursor protein. | |||||
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 |
NISHIMURA, Masaki
× NISHIMURA, Masaki× LIU, Lei× HASEGAWA, Hiroshi |
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著者別名 |
西村, 正樹
× 西村, 正樹 |
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抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | γ-Secretase mediates intramembranous γ-cleavage and ε-cleavage of β-amyloid precursor protein (APP) to liberate β-amyloid peptide (Aβ) and APP intracellular domain respectively from the membrane. Although the regulatory mechanism of γ-secretase cleavage remains unresolved, a member of the p24 cargo protein family, named p24δ(1) or TMP21, has been identified as an activity-modulating component. The p24 family proteins are divided into four subfamilies (p24α, β, δ and γ). In contrast to p24δ(1), p24β(1) has reportedly no effect on γ-cleavage. In this study, we determined whether p24α(2), p24γ(3) or p24γ(4) modulates APP processing. Knockdown of cellular p24α(2) induced a significant increase in Aβ generation but not in APP intracellular domain production in cell-based and cell-free assays, whereas p24α(2) over-expression suppressed Aβ secretion. By contrast, Aβ secretion was not altered by p24γ(3) or p24γ(4) knockdown. Endogenous p24α(2) co-immunoprecipitated with core components of the γ-secretase complex, and the anti-p24α(2) immunoprecipitate exhibited γ-secretase activity. Mutational disruption of the conserved dilysine ER-retrieval motifs of p24α(2) and p24δ(1) perturbed inhibition of γ-cleavage. Simultaneous knockdown, or co-over-expression, of these proteins had no additive or synergistic effect on Aβ generation. Our findings suggest that dilysine ER-retrieval signal-containing p24 proteins, p24α(2) and p24δ(1), bind with γ-secretase complexes and collaborate in attenuating γ-cleavage of APP. | |||||
書誌情報 |
Journal of Neurochemistry 巻 115, 号 3, p. 771-781, 発行日 2010-11 |
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出版者 | ||||||
出版者 | Wiley-Blackwell | |||||
PMID | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | PMID | |||||
関連識別子 | 20807314 | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
識別子タイプ | DOI | |||||
関連識別子 | https://doi.org/10.1111/j.1471-4159.2010.06977.x | |||||
関連名称 | 10.1111/j.1471-4159.2010.06977.x | |||||
権利 | ||||||
権利情報 | © 2010 The Authors. Journal of Neurochemistry | |||||
権利 | ||||||
権利情報 | © 2010 International Society for Neurochemistry. | |||||
フォーマット | ||||||
内容記述タイプ | Other | |||||
内容記述 | ||||||
著者版フラグ | ||||||
出版タイプ | AM | |||||
出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
資源タイプ | ||||||
内容記述タイプ | Other | |||||
内容記述 | Journal Article |