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Cited by 3,149Protease and Inhibitor MechanismsBlood Coagulation and Thrombosis MechanismsNF-κB Signaling Pathways

The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.

A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells

Black, Roy A., Rauch, Charles T., Kozlosky, Carl J., Peschon, Jacques J., Slack, Jennifer L., Wolfson, Martin F., Castner, Beverly J., Stocking, Kim L., Reddy, Pranitha, Srinivasan, Subhashini, Nelson, Nicole, Boiani, Norman, Schooley, Kenneth A., Gerhart, Mary, Davis, Raymond, Fitzner, Jeffrey N., Johnson, Richard S., Paxton, Raymond J., March, Carl J., Cerretti, Douglas Pat·1997·Nature
DOI 10.1038/385729a0
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Abstract

Mammalian cells proteolytically release (shed) the extracellular domains of many cell-surface proteins. Modification of the cell surface in this way can alter the cell's responsiveness to its environment and release potent soluble regulatory factors. The release of soluble tumour-necrosis factor-alpha (TNF-alpha) from its membrane-bound precursor is one of the most intensively studied shedding events because this inflammatory cytokine is so physiologically important. The inhibition of TNF-alpha release (and many other shedding phenomena) by hydroxamic acid-based inhibitors indicates that one or more metalloproteinases is involved. We have now purified and cloned a metalloproteinase that specifically cleaves precursor TNF-alpha. Inactivation of the gene in mouse cells caused a marked decrease in soluble TNF-alpha production. This enzyme (called the TNF-alpha-converting enzyme, or TACE) is a new member of the family of mammalian adamalysins (or ADAMs), for which no physiological catalytic function has previously been identified. Our results should facilitate the development of therapeutically useful inhibitors of TNF-alpha release, and they indicate that an important function of adamalysins may be to shed cell-surface proteins.

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Metadata

Authors
Black, R. A., Rauch, C. T., Kozlosky, C. J., Peschon, J. J., Slack, J. L., Wolfson, M. F., Castner, B. J., Stocking, K. L., Reddy, P., Srinivasan, S., Nelson, N., Boiani, N., Schooley, K. A., Gerhart, M., Davis, R., Fitzner, J. N., Johnson, R. S., Paxton, R. J., March, C. J., & Cerretti, D. P.
ORCID
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
1997-02
Volume
385
Issue
6618
Pages
729-733
ISSN
  • 0028-0836 (ISSN-L)
  • 1476-4687
DOI
10.1038/385729a0
OpenAlex
W2074881372
Cited by
3,149
References
30
Citations by year
2026: 47 · 2025: 45 · 2024: 52 · 2023: 58 · 2022: 97 · 2021: 105 · 2020: 100 · 2019: 88 · 2018: 95 · 2017: 98 · 2016: 97 · 2015: 92 · 2014: 114 · 2013: 124 · 2012: 115
FWCI
60.23
Type
journal article
Language
en
Open access
closed
Licence
www.springer.com/tdm (tdm)
Locations
  • Nature (publishedVersion)
  • PubMed (publishedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
  • Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
Keywords
TNF-α, TNF-alpha converting enzyme, transarterial chemoembolization, metalloproteinases, ADAMS, protein shedding, soluble TNF-alpha, hydroxamate inhibitors, gene inactivation, cytokine production, inflammatory cytokines
MeSH terms
ADAM17 Protein, Amino Acid Sequence, Animals, Cattle, Cell Membrane, Cloning, Molecular, Enzyme Precursors, Humans, Metalloendopeptidases, Mice, Inbred C57BL, Molecular Sequence Data, Solubility, T-Lymphocytes, Tumor Cells, Cultured, Tumor Necrosis Factor-alpha, Zinc, Polymerase Chain Reaction, Gene Targeting, Disintegrins, Mice, ADAM Proteins

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