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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
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

このアイテムを引用あるいはリンクする場合は次の識別子を使用してください。 http://hdl.handle.net/2297/14537



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