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

Ahmad, Munirah, Takino, Takahisa, Miyamori, Hisashi, Yoshizaki, Tomokazu, Furukawa, Mitsuru, Sato, Hiroshi·2006·The Journal of Biochemistry
DOI 10.1093/jb/mvj054
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Abstract

Amyloid-beta 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-M464, N579-M580, H622-S623, and H685-Q686 peptide bonds, which included a cleavage site within the amyloid beta peptide region known to produce a C-terminal fragment. The Swedish-type mutant of APP, which produces a high level of amyloid beta peptide, was more effectively cleaved by MT3-MMP than wild-type APP in both the presence and absence of Fe65; however, amyloid beta 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.

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Metadata

Authors
Ahmad, M., Takino, T., Miyamori, H., Yoshizaki, T., Furukawa, M., & Sato, H.
Venue
The Journal of Biochemistry
Publisher
Oxford University Press (OUP)
Published
2006-03-01
Volume
139
Issue
3
Pages
517-526
ISSN
  • 1756-2651
  • 0021-924X
DOI
10.1093/jb/mvj054
Cited by
82
References
1
Language
en

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