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

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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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Matrix metalloproteinases and their inhibitors in connective tissue remodeling
Woessner, J. F. (1991) · The FASEB Journal · doi:10.1096/fasebj.5.8.1850705 · Cited by 3,281
Conditions controlling the proliferation of haemopoietic stem cells in vitro
Dexter, T. M., Allen, T., & Lajtha, L. G. (1977) · Journal of Cellular Physiology · doi:10.1002/jcp.1040910303 · Cited by 2,120
Early lymphocyte expansion is severely impaired in interleukin 7 receptor-deficient mice.
Peschon, J. J., Morrissey, P., Grabstein, K. H., Ramsdell, F. J., Maraskovsky, E., Gliniak, B., Park, L. S., Ziegler, S. F., Williams, D. E., Ware, C. B., et al. (1994) · The Journal of Experimental Medicine · doi:10.1084/jem.180.5.1955 · Cited by 1,553
Self-citation
The Tumor Necrosis Factor Ligand and Receptor Families
Bazzoni, F., & Beutler, B. (1996) · New England Journal of Medicine · doi:10.1056/nejm199606273342607 · Cited by 1,221
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-citation
A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein: Ramifications for the complex physiology of TNF
Kriegler, 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
Rose‐John, S., & Heinrich, P. C. (1994) · Biochemical Journal · doi:10.1042/bj3000281 · Cited by 777
Mammalian subtilisins: The long-sought dibasic processing endoproteases
Barr, P. J. (1991) · Cell · doi:10.1016/0092-8674(91)90129-m · Cited by 750
The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidases
Stöcker, W., Grams, F., Reinemer, P., Bode, W., Baumann, U., Gomis‐Rüth, F. X., & McKay, D. (1995) · Protein Science · doi:10.1002/pro.5560040502 · Cited by 725

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Role of ADAM17 in the ectodomain shedding of TNF-α and its receptors by neutrophils and macrophages
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Kieseier, B. C. (1998) · Brain · doi:10.1093/brain/121.1.159 · Cited by 163
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de Rouvroit, C. L., de Bergeyck, V., Cortvrindt, C., Bar, I., Eeckhout, Y., & Goffinet, A. M. (1999) · Experimental Neurology · doi:10.1006/exnr.1998.7007 · Cited by 161
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Zhang, Y., Jiang, J., Black, R. A., Baumann, G. P., & Frank, S. J. (2000) · Endocrinology · doi:10.1210/endo.141.12.7858 · Cited by 140
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Evolution of the inflammatory response in the brain following intracerebral hemorrhage and effects of delayed minocycline treatment
Wasserman, J. K., Zhu, X., & Schlichter, L. C. (2007) · Brain Research · doi:10.1016/j.brainres.2007.08.058 · Cited by 137
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Wang, Y., Herrera, A. H., Li, Y., Belani, K., & Walcheck, B. K. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0802770 · Cited by 136
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Contin‐Bordes, C., Pitard, V., Itai, T., Nagata, S., Moreau, J., & Déchanet‐Merville, J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m209993200 · Cited by 135
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Werner, M., Herbon, N., Gohlke, H., Altmüller, J., Knapp, M., Heinrich, J., & Wjst, M. (2004) · Clinical & Experimental Allergy · doi:10.1111/j.1365-2222.2004.01846.x · Cited by 130
Tumor Necrosis Factor-α Increases in the Brain after Intracerebral Hemorrhage and Thrombin Stimulation
Hua, Y., Wu, J., Keep, R. F., Nakamura, T., Hoff, J. T., & Xi, G. (2006) · Neurosurgery · doi:10.1227/01.neu.0000197333.55473.ad · Cited by 133
The ADAMs family: Coordinators of nervous system development, plasticity and repair
Yang, P., Baker, K. A., & Hagg, T. (2006) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2006.05.001 · Cited by 116
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Beckett, R. P., & Whittaker, M. A. (1998) · Expert Opinion on Therapeutic Patents · doi:10.1517/13543776.8.3.259 · Cited by 133
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Fleck, D., van Bebber, F., Colombo, A., Galante, C., Schwenk, B. M., Rabe, L., Hampel, H., Novak, B., Kremmer, E., Tahirovic, S., et al. (2013) · The Journal of Neuroscience · doi:10.1523/jneurosci.3372-12.2013 · Cited by 123
Quinolines: a new hope against inflammation
Mukherjee, S., & Pal, M. (2012) · Drug Discovery Today · doi:10.1016/j.drudis.2012.11.003 · Cited by 132
Functions of ‘A disintegrin and metalloproteases (ADAMs)’ in the mammalian nervous system
Hsia, H., Tüshaus, J., Brummer, T., Zheng, Y., Scilabra, S. D., & Lichtenthaler, S. F. (2019) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-019-03173-7 · Cited by 148
Metalloprotease-Disintegrin (ADAM) Genes Are Widely and Differentially Expressed in the Adult CNS
Kärkkäinen, I., Rybnikova, E. A., Pelto‐Huikko, M., & Huovila, A. J. (2000) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.2000.0848 · Cited by 132
Matrix Metalloproteinase Inhibition: From The Jurassic To The Third Millennium
Woessner, J. F. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb07697.x · Cited by 132
ADAM family proteins in the immune system
Yamamoto, S., Higuchi, Y., Yoshiyama, K., Shimizu, E., Kataoka, M., Hijiya, N., & Matsuura, K. (1999) · Immunology Today · doi:10.1016/s0167-5699(99)01464-4 · Cited by 132
Diverse regulatory roles for lysosomal proteases in the immune response
Colbert, J. D., Matthews, S. P., Miller, G., & Watts, C. (2009) · European Journal of Immunology · doi:10.1002/eji.200939650 · Cited by 131

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: Black, Roy A.
Johnson, Richard S.
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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A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells

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