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Cited by 934

The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.

Evidence That Tumor Necrosis Factor α Converting Enzyme Is Involved in Regulated α-Secretase Cleavage of the Alzheimer Amyloid Protein Precursor

Open access
Buxbaum, Joseph D., Liu, Kang-Nian, Luo, Yuxia, Slack, Jennifer L., Stocking, Kim L., Peschon, Jacques J., Johnson, Richard S., Castner, Beverly J., Cerretti, Douglas Pat, Black, Roy A.·1998·Journal of Biological Chemistry
DOI 10.1074/jbc.273.43.27765
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Abstract

The amyloid protein, Abeta, which accumulates in the brains of Alzheimer patients, is derived by proteolysis of the amyloid protein precursor (APP). APP can undergo endoproteolytic processing at three sites, one at the amino terminus of the Abeta domain (beta-cleavage), one within the Abeta domain (alpha-cleavage), and one at the carboxyl terminus of the Abeta domain (gamma-cleavage). The enzymes responsible for these activities have not been unambiguously identified. By the use of gene disruption (knockout), we now demonstrate that TACE (tumor necrosis factor alpha converting enzyme), a member of the ADAM family (a disintegrin and metalloprotease-family) of proteases, plays a central role in regulated alpha-cleavage of APP. Our data suggest that TACE may be the alpha-secretase responsible for the majority of regulated alpha-cleavage in cultured cells. Furthermore, we show that inhibiting this enzyme affects both APP secretion and Abeta formation in cultured cells.

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Crossref · 10.1074/jbc.273.43.27765

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Metadata

Authors
Buxbaum, J. D., Liu, K.-N., Luo, Y., Slack, J. L., Stocking, K. L., Peschon, J. J., Johnson, R. S., Castner, B. J., Cerretti, D. P., & Black, R. A.
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1998-10
Volume
273
Issue
43
Pages
27765-27767
ISSN
0021-9258 (ISSN-L)
DOI
10.1074/jbc.273.43.27765
OpenAlex
W2019500453
Cited by
934
References
5
FWCI
31.72
Type
journal article
Language
en
Open access
hybrid

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