Cleavage of Amyloid-β Precursor Protein (APP) by Membrane-Type Matrix Metalloproteinases

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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.

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  • The journal of biochemistry  

    The journal of biochemistry 139(3), 517-526, 2006-03-01 

    日本生化学会 = Japanese Biochemical Society

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各種コード

  • NII論文ID(NAID)
    10018846859
  • NII書誌ID(NCID)
    AA00694073
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    0021924X
  • NDL 記事登録ID
    7878792
  • NDL 雑誌分類
    ZR2(科学技術--生物学--生化学)
  • NDL 請求記号
    Z53-B472
  • データ提供元
    CJP書誌  CJP引用  NDL  IR 
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