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タイトル: Cleavage of amyloid-β precursor protein (APP) by membrane-type matrix metalloproteinases
著者: Ahmad, Munirah
Takino, Takahisa link image link image
Miyamori, Hisashi link image
Yoshizaki, Tomokazu link image link image
Furukawa, Mitsuru link image
Sato, Hiroshi link image
滝野, 隆久
吉崎, 智一
古川, 仭
佐藤, 博
発行日: 2006年 3月
出版社(者): 日本生化学会 = Japanese Biochemical Society
雑誌名: Journal of Biochemistry
ISSN: 0021-924X
巻: 139
号: 3
開始ページ: 517
終了ページ: 526
キーワード: Amyloid-β precursor protein
Cleavage
MMP
MT-MMP
抄録: 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.
DOI: 10.1093/jb/mvj054
URI: http://hdl.handle.net/2297/14537
関連URI: http://dx.doi.org/10.1093/jb/mvj054
資料種別: Journal Article
権利関係: © 2006 The Japanese Biochemical Society
版表示: publisher
出現コレクション:1. 査読済論文

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