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
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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“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]
In the citing paper
“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]
Citations
Cites
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Self-citationThe Tumor Necrosis Factor Ligand and Receptor Families
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Processing of tumour necrosis factor-α precursor by metalloproteinases
Gearing, A. J. H., Beckett, P., Christodoulou, M., Churchill, M., Clements, J. M., Davidson, A. H., Drummond, A. H., GALLOWAY, W. A., Gilbert, R. J. C., Gordon, J. L., et al. (1994) · Nature · doi:10.1038/370555a0 · Cited by 1,194
Molecular Cloning of the Interleukin-1β Converting Enzyme
Cerretti, D. P., Kozlosky, C. J., Mosley, B., Nelson, N. C., Ness, K. V., Greenstreet, T. A., March, C. J., Kronheim, S. R., Druck, T., Cannizzaro, L. A., et al. (1992) · Science · doi:10.1126/science.1373520 · Cited by 1,147
Self-citationKriegler, M., Perez, C. F., DeFay, K., Albert, I., & Lu, S.-D. (1988) · Cell · doi:10.1016/0092-8674(88)90486-2 · Cited by 1,090
Soluble receptors for cytokines and growth factors: generation and biological function
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Mammalian subtilisins: The long-sought dibasic processing endoproteases
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Atherosclerosis--an inflammatory disease
Ross, R. (1999) · New England Journal of Medicine · doi:10.1056/nejm199901143400207 · Cited by 21,725
Signalling pathways of the TNF superfamily: a double-edged sword
Aggarwal, B. B. (2003) · Nature Reviews Immunology · doi:10.1038/nri1184 · Cited by 2,793
Macrophage Cytokines: Involvement in Immunity and Infectious Diseases
Arango Duque, G., & Descoteaux, A. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2014.00491 · Cited by 2,708
New insights into the genetic etiology of Alzheimer’s disease and related dementias
Bellenguez, C., Küçükali, F., Jansen, I. E., Kleineidam, L., Moreno-Grau, S., Amin, N., Naj, A. C., Campos-Martin, R., Grenier-Boley, B., Andrade, V., et al. (2022) · Nature Genetics · doi:10.1038/s41588-022-01024-z · Cited by 2,498
Tumor necrosis factor signaling
Wajant, H., Pfizenmaier, K., & Scheurich, P. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401189 · Cited by 2,422
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.
- 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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