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Cited by 1,378

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α

Moss, Marcia L., Jin, S.-L. Catherine, Milla, Marcos E., Burkhart, William, Carter, H. Luke, Chen, Wen-Ji, Clay, William C., Didsbury, John R., Hassler, Daniel, Hoffman, Christine R., Kost, Thomas A., Lambert, Millard H., Leesnitzer, M. Anthony, McCauley, Philip, McGeehan, Gerard, Mitchell, Justin, Moyer, Mary, Pahel, Gregory, Rocque, Warren, Overton, Laurie K., Schoenen, Frank, Seaton, Theresa, Su, Jui-Lan, Warner, Janet, Willard, Derril, Becherer, J. David·1997·Nature
DOI 10.1038/385733a0
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Abstract

Tumour-necrosis factor-alpha (TNF-alpha) is a cytokine that contributes to a variety of inflammatory disease states. The protein exists as a membrane-bound precursor of relative molecular mass 26K which can be processed by a TNF-alpha-converting enzyme (TACE), to generate secreted 17K mature TNF-alpha. We have purified TACE and cloned its complementary DNA. TACE is a membrane-bound disintegrin metalloproteinase. Structural comparisons with other disintegrin-containing enzymes indicate that TACE is unique, with noteable sequence identity to MADM, an enzyme implicated in myelin degradation, and to KUZ, a Drosophila homologue of MADM important for neuronal development. The expression of recombinant TACE (rTACE) results in the production of functional enzyme that correctly processes precursor TNF-alpha to the mature form. The rTACE provides a readily available source of enzyme to help in the search for new anti-inflammatory agents that target the final processing stage of TNF-alpha production.

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Crossref · 10.1038/385733a0

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1 of 1 references verified0 citation errors · 0 not checkable

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Claims other papers make about this one

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  • ADAM17 is also referred to as TNFα-converting enzyme and is originally identified as a proteinase responsible for cleaving the transmembrane TNFα precursor.

    “ADAM17, also referred to as TNFα-converting enzyme, is originally identified as a proteinase responsible for cleaving the transmembrane TNFα precursor (27).”

    From ADAM17 mediates ectodomain shedding of the soluble VLDL receptor fragment in the retinal epithelium (2021) · cites this paper as [27]

Citations

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Research works printed but not linked: 24

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  4. Howard, L., Lu, X., Mitchell, S., Griffiths, S. & Glynn, P. Molecular cloning of MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell types. Biochem. J. 317, 45–50 (1996). · DOI
  5. Rooke, J., Pan, D., Xu, T. & Rubin, G. M. KUZ, a conserved metalloprotease-disintegrin protein with two roles in Drosophila neurogenesis. Science 273, 1227–1231 (1996). · DOI
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  7. Gearing, A. et al. Processing of tumor necrosis factor-α precursor by metalloproteases. Nature 370, 558–561 (1994). · DOI
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  12. Zhou, Q., Dangelmaier, C. & Smith, J. B. The hemorrhagin catrocollastatin inhibits collagen-induced platelet aggregatin by binding to collagen via its disintegrin-like domain. Biochem. Biophys. Res. Commun. 219, 720–726 (1996). · DOI
  13. Gould, R. J. et al. Disintegrins: a family of integrin inhibitory proteins from viper venoms. Proc. Soc. Exp. Biol. Med. 195, 168–171 (1990). · DOI
  14. Weskamp, G., Kratzschmar, J., Reid, M. S. & Blobel, C. P. MDC0, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains. J. Cell Biol. 132, 717–726 (1996). · DOI
  15. Suffys, P., Beyaert, R., Van Roy, F. & Fiers, W. Involvement of a serine protease in tumor necrosis factor-mediated cytotoxicity. Eur. J. Biochem. 178, 257–265 (1988). · DOI
  16. Bennett, T. A., Lynam, E. B., Sklar, L. A. & Rogelj, S. Hydroxamate-based metalloprotease inhibitor blocks shedding of L-selectin adhesion molecule from leukocytes. Functional consequences for neutrophil aggregation. J. Immunol. 156, 3093–3097 (1996). · DOI
  17. Mullberg, J. et al. A metalloprotease inhibitor blocks shedding of the IL-6 receptor and te p60 TNF receptor. J. Immunol. 155, 5198–5205 (1995). · DOI
  18. Arribas, J. et al. Diverse cell surface protein ectodomains are shed by a system sensitive to metalloprotease inhibitors. J. Biol. Chem. 271, 11376–11382 (1996). · DOI
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  20. Moyer, M., Rose, D. & Burkhart, W. Elutin of proteins from polyacrylamide gels onto the HP sequencing column. in Techniques in Protein Chemistry (ed. Crabb, J.) 195–204 (Academic, San Diego, 1994).
  21. Granados, R. R., Guoxun, L., Derksen, A. C. G. & McKenna, K. A. A new cell line from Trichoplusia ni (BTI-Tn-5BI-4) susceptible to Trichoplusia single enveloped nuclear polyhedrosis virus. J. Invert. Path. 64, 260–266 (1994). · DOI
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  24. O'Byren, E. M. et al. Oral administration of a matrix metalloprotease inhibitor, CGS 27023A, protects the cartilage proteoglycan matrix in a partial meniscectomy model of osteoarthritis in rabbits. Inflam. Res. 44 (suppl. 2), S117–S118 (1995). · DOI

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Metadata

Authors
Moss, M. L., Jin, S.-L. C., Milla, M. E., Burkhart, W., Carter, H. L., Chen, W.-J., Clay, W. C., Didsbury, J. R., Hassler, D., Hoffman, C. R., Kost, T. A., Lambert, M. H., Leesnitzer, M. A., McCauley, P., McGeehan, G., Mitchell, J., Moyer, M., Pahel, G., Rocque, W., Overton, L. K., Schoenen, F., Seaton, T., Su, J.-L., Warner, J., Willard, D., & Becherer, J. D.
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
1997-02
Volume
385
Issue
6618
Pages
733-736
ISSN
  • 0028-0836
  • 1476-4687
DOI
10.1038/385733a0
Cited by
1,378
References
1
Language
en
Update notices
correction (1997-04-17)
Licence
www.springer.com/tdm (tdm)

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