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Cleavage of amyloid-β precursor protein (APP) by membrane-type matrix metalloproteinases
https://doi.org/10.24517/00027538
https://doi.org/10.24517/00027538fc7757c2-f611-4fd2-9362-88663004cff9
名前 / ファイル | ライセンス | アクション |
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CA-PR-SATO-H-517.pdf (364.6 kB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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公開日 | 2017-10-05 | |||||
タイトル | ||||||
タイトル | Cleavage of amyloid-β precursor protein (APP) by membrane-type matrix metalloproteinases | |||||
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 | |||||
ID登録 | ||||||
ID登録 | 10.24517/00027538 | |||||
ID登録タイプ | JaLC | |||||
著者 |
Ahmad, Munirah
× Ahmad, Munirah× Takino, Takahisa× Miyamori, Hisashi× Yoshizaki, Tomokazu× Furukawa, Mitsuru× Sato, Hiroshi |
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著者別表示 |
滝野, 隆久
× 滝野, 隆久× 宮森, 久志× 吉崎, 智一× 古川, 仞× 佐藤, 博 |
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提供者所属 | ||||||
内容記述タイプ | Other | |||||
内容記述 | 金沢大学がん研究所がん病態制御 | |||||
書誌情報 |
Journal of Biochemistry 巻 139, 号 3, p. 517-526, 発行日 2006-03-01 |
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ISSN | ||||||
収録物識別子タイプ | ISSN | |||||
収録物識別子 | 0021-924X | |||||
NCID | ||||||
収録物識別子タイプ | NCID | |||||
収録物識別子 | AA00694073 | |||||
DOI | ||||||
関連タイプ | isIdenticalTo | |||||
識別子タイプ | DOI | |||||
関連識別子 | 10.1093/jb/mvj054 | |||||
出版者 | ||||||
出版者 | 日本生化学会 = Japanese Biochemical Society | |||||
抄録 | ||||||
内容記述タイプ | Abstract | |||||
内容記述 | Amyloid-β precursor protein (APP) was identified on expression cloning from a human placenta cDNA library as a gene product that modulates the activity of membrane-type matrix metalloproteinase-1 (MT1-MMP). Co-expression of MT1-MMP with APP in HEK293T cells induced cleavage and shedding of the APP ectodomain when co-expressed with APP adaptor protein Fe65. Among the MT-MMPs tested, MT3-MMP and MT5-MMP also caused efficient APP shedding. The recombinant APP protein was cleaved by MT3-MMP in vitro at the A463-M 464, N579-M580, H622-S 623, and H685-Q686 peptide bonds, which included a cleavage site within the amyloid β peptide region known to produce a C-terminal fragment. The Swedish-type mutant of APP, which produces a high level of amyloid β peptide, was more effectively cleaved by MT3-MMP than wild-type APP in both the presence and absence of Fe65; however, amyloid β peptide production was not affected by MT3-MMP expression. Expression of MT3-MMP enhanced Fe65-dependent transactivation by APP fused to the Gal4 DNA-binding and transactivation domains. These results suggest that MT1-MMP, MT3-MMP and MT5-MMP should play an important role in the regulation of APP functions in tissues including the central nervous system. © 2006 The Japanese Biochemical Society. | |||||
権利 | ||||||
権利情報 | © 2006 The Japanese Biochemical Society | |||||
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 | |||||
関連URI | ||||||
識別子タイプ | DOI | |||||
関連識別子 | http://dx.doi.org/10.1093/jb/mvj054 |