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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
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-citationThe 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-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
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
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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Francois, A., Terro, F., Quellard, N., Fernandez, B., Chassaing, D., Janet, T., Bilan, A. R., Paccalin, M., & Page, G. (2014) · Molecular Brain · doi:10.1186/s13041-014-0056-z · Cited by 62
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Dinarello, C. A. (2005) · PubMed · Cited by 73
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Cousin, H., Gaultier, A., Bleux, C., Darribère, T., & Alfandari, D. (2000) · Developmental Biology · doi:10.1006/dbio.2000.9871 · Cited by 74
Mueller, C., Corazza, N., Trachsel-Løseth, S., Eugster, H., Bühler-Jungo, M., Brunner, T., & Imboden, M. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.53.38112 · Cited by 73
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Lorenzen, I., Lokau, J., Düsterhöft, S., Trad, A., Garbers, C., Scheller, J., Rose‐John, S., & Grötzinger, J. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.03.012 · Cited by 72
Garbin, U., Baggio, E., Stranieri, C., Pasini, A., Manfro, S., Mozzini, C., Vallerio, P., Lipari, G., Merigo, F., Guidi, G. C., et al. (2012) · Cardiovascular Research · doi:10.1093/cvr/cvs301 · Cited by 74
de Meijer, V. E., Sverdlov, D., Popov, Y. V., Le, H. D., Meisel, J. A., Nosé, V., Schuppan, D., & Puder, M. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011256 · Cited by 73
Edwardson, D. W., Boudreau, J., Mapletoft, J., Lannér, C., Kovala, A. T., & Parissenti, A. M. (2017) · PLoS ONE · doi:10.1371/journal.pone.0183662 · Cited by 74
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Gupta, S. P. (2007) · Chemical Reviews · doi:10.1021/cr030448t · Cited by 72
Roberts, C. M., Tani, P. H., Bridges, L. C., Laszik, Z. G., & Bowditch, R. D. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.41.29251 · Cited by 75
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Dong, J., & Wiley, H. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.1.557 · Cited by 74
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Kong, Q., Peterson, T. S., Baker, O. J., Stanley, E., Camden, J. M., Seye, C. I., Erb, L., Simonyi, Á., Wood, W. G., Sun, G. Y., et al. (2009) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2009.06048.x · Cited by 69
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Yang, X. P., Mattagajasingh, S. N., Su, S., Chen, G., Cai, Z. P., Fox-Talbot, K., Irani, K., & Becker, L. C. (2007) · Circulation Research · doi:10.1161/circresaha.107.160812 · Cited by 72
Albrechtsen, R., Kveiborg, M., Stautz, D., Vikeså, J., Noer, J. B., Kotzsh, A., Nielsen, F. C., Wewer, U. M., & Fröhlich, C. (2013) · Journal of Cell Science · doi:10.1242/jcs.129510 · Cited by 69
Kanzaki, H., Makihira, S., Suzuki, M., Ishii, T., Movilă, A., Hirschfeld, J., Mawardi, H. H., Lin, X., Han, X., Taubman, M. A., et al. (2016) · The Journal of Immunology · doi:10.4049/jimmunol.1601114 · Cited by 69
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Moss, M. L., Powell, G., Miller, M. A., Edwards, L. L., Qi, B., Sang, Q. A., Strooper, B. D., Tesseur, I. C., Lichtenthaler, S. F., Taverna, M., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.280495 · Cited by 68
Iwata, M., Enciso, J. S., & Greenberg, B. (2009) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00036.2009 · Cited by 69
Zhao, L., Shey, M. R., Farnsworth, M., & Dailey, M. O. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103748200 · Cited by 68
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Sprowl, J. A., Reed, K., Armstrong, S., Lannér, C., Guo, B., Kalatskaya, I., Stein, L. D., Hembruff, S. L., Tam, A., & Parissenti, A. M. (2012) · Breast Cancer Research · doi:10.1186/bcr3083 · Cited by 67
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Lisi, S., Sisto, M., Lofrumento, D. D., & D’Amore, M. (2011) · Laboratory Investigation · doi:10.1038/labinvest.2011.190 · Cited by 69
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Costa, E. P., Clissa, P. B., Teixeira, C., & Moura-da-Silva, A. M. (2002) · Inflammation · doi:10.1023/a:1014465611487 · Cited by 67
Harrison, L. M., van Haaften, W. C. E., & Tesh, V. L. (2004) · Infection and Immunity · doi:10.1128/iai.72.5.2618-2627.2004 · Cited by 67
Montero, J. C., Yuste, L., Dı́az-Rodrı́guez, E., Esparı́s-Ogando, A., & Pandiella, A. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3630211 · Cited by 67
Loeb, J. A., Susanto, E. T., & Fischbach, G. D. (1998) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.1998.0676 · Cited by 67
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Hahn, D., Pischitzis, A., Rösmann, S., Hansen, M. K., Leuenberger, B., Luginbuehl, U., & Sterchi, E. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211169200 · Cited by 66
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Deng, M., Loughran, P., Zhang, L., Scott, M. J., & Billiar, T. R. (2015) · Science Signaling · doi:10.1126/scisignal.2005548 · Cited by 66
Satoh, M., Nakamura, M., Satoh, H., Saitoh, H., Segawa, I., & Hiramori, K. (2000) · Journal of the American College of Cardiology · doi:10.1016/s0735-1097(00)00827-5 · Cited by 66
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Markers of inflammation as predictors in cardiovascular disease
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A Continuous Fluorimetric Assay for Tumor Necrosis Factor-α Converting Enzyme
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Effenberger, T., von der Heyde, J., Bartsch, K., Garbers, C., Schulze‐Osthoff, K., Chalaris, A., Murphy, G., Rose‐John, S., & Rabe, B. (2014) · The FASEB Journal · doi:10.1096/fj.14-254565 · Cited by 54
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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