A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells
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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ADAM17 (TNF-α-converting enzyme) is of pivotal importance in the activation of TNF-α signaling.
“For example, ADAM17 (also known as TNF-α-converting enzyme) is of pivotal importance in the activation of TNF-α signaling32.”
From New insights into the genetic etiology of Alzheimer’s disease and related dementias (2022) · cites this paper as [32]
Release of mature TNF from the plasmalemma requires cleavage of the membrane-bound precursor by TACE.
“Finally, release of mature TNF from the plasmalemma requires cleavage of the membrane-bound precursor by the TNF-α-converting enzyme (TACE) (21).”
From Macrophage Cytokines: Involvement in Immunity and Infectious Diseases (2014) · cites this paper as [21]
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- 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.
- Venue
- Nature
- Published
- 1997-02
- Volume
- 385
- Issue
- 6618
- Pages
- 729-733
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- 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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