A metalloproteinase disintegrin that releases tumour-necrosis factor-∅ from cells

Nature

Volumn 385, Issue 6618, 1997, Pages 729-733

  Black, Roy A ^a   Rauch, Charles T ^a   Kozlosky, Carl J ^a   Peschon, Jacques J ^a   Slack, Jennifer L ^a   Wolfson, Martin F ^a   Castner, Beverly J ^a   Stocking, Kim L ^a   Reddy, Pranitha ^a   Srinivasan, Subhashini ^a   Nelson, Nicole ^a   Boiani, Norman ^a   Schooley, Kenneth A ^a   Gerhart, Mary ^a   Davis, Raymond ^a   Fitzner, Jeffrey N ^a   Johnson, Richard S ^a   Paxton, Raymond J ^a   March, Carl J ^a   Cerretti, Douglas Pat ^a  

^a AMGEN INC   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE PROTEIN; DISINTEGRIN; METALLOPROTEINASE; TUMOR NECROSIS FACTOR ALPHA;

AMINO ACID SEQUENCE; ARTICLE; BASE PAIRING; CELL SURFACE; CELLULAR DISTRIBUTION; DNA LIBRARY; ENZYME ACTIVITY; ENZYME PURIFICATION; EXTRACELLULAR MATRIX; MAMMAL CELL; MOLECULAR CLONING; NORTHERN BLOTTING; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PROTEIN DEGRADATION; SOUTHERN BLOTTING;

ADAM PROTEINS; AMINO ACID SEQUENCE; ANIMALS; CATTLE; CELL MEMBRANE; CLONING, MOLECULAR; DISINTEGRINS; ENZYME PRECURSORS; GENE TARGETING; HUMANS; METALLOENDOPEPTIDASES; MICE; MICE, INBRED C57BL; MOLECULAR SEQUENCE DATA; POLYMERASE CHAIN REACTION; SOLUBILITY; T-LYMPHOCYTES; TUMOR CELLS, CULTURED; TUMOR NECROSIS FACTOR-ALPHA; ZINC;

MAMMALIA;

EID: 8044257704     PISSN: 00280836     EISSN: None     Source Type: Journal    
DOI: 10.1038/385729a0     Document Type: Article

References (30)

1. Rose-John, S. & Heinrich, P. C. Soluble receptors for cytokines and growth factors: generation and biological function. Biochem. J. 300, 281-290 (1994).
2. Walcheck, B. et al. Neutrophil rolling altered by inhibition of L-selectin shedding in vitro. Nature 380, 720-723 (1996).
3. Mohler, K. M. et al. Protection against a lethal dose of endotoxin by an inhibitor of tumour necrosis factor processing. Nature 370, 218-220 (1994).
4. Decker, T., Lohmann-Matthes, M. L. & Gifford, G. E. Cell-associated tumour necrosis factor (TNF) as A killing mechanism of activated cytotoxic macrophages. J. Immunol. 138, 957-962 (1987).
5. Kriegler, M., Perez, C., De Fay, K., Albert, I. & Lu, S. D. A novel form of TNF/cachectin is a cell surface cytotoxic transmembrane protein: ramifications for the complex physiology of TNF. Cell 53, 45-53 (1988).
6. Bazzoni, F. & Beutler, B. The tumor necrosis factor ligand and receptor families. N. Engl. J. Med. 334, 1717-1725 (1996).
7. Sherry, B. & Cerami, A. Cachectin/tumor necrosis factor exerts endocrine, paracrine, and autocrine control of inflammatory responses. J. Cell Biol. 107, 1269-1277 (1988).
8. McGeehan, G. M. et al. Regulation of tumour-necrosis factor-α processing by a metalloproteinase inhibitor. Nature 370, 558-561 (1994).
9. Gearing, A. J. et al. Processing of tumour-necrosis factor-α precursor by metalloproteinases. Nature 370,5 55-557 (1994).
10. Wolfsberg, T. G. & White, J. M. ADAMs in fertilization and development. Dev. Biol. 180, 389-401 (1996).
11. Black, R. A. et al. Relaxed specificity of matrix metalloproteinases (MMPs) and TIMP-insensitivity of tumor necrosis factor-α (TNF-α) production suggest the major TNF-α converting enzyme is not an MMP. Biochem. Biophys. Res. Commun. 225, 400-405 (1996).
12. Stocker, W. et al. The metzincins - topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci. 4, 823-840 (1995).
13. 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).
14. Cerretti, D. P. et al. Molecular cloning of the interleukin-1β converting enzyme. Science 256, 97-100 (1992).
15. Woessner, J. F. Jr Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB J. 5, 2145-2154 (1991).
16. Barr, P. J. Mammalian subtilisins: the long-sought dibasic processing endoproteases. Cell 66, 1-3 (1991)
17. Teeter, M. M., Roe, S. M. & Heo, N. H. Atomic resolution (0.83 A) crystal structure of the hydrophobic protein crambin at 130K. J. Mol. Biol. 230, 292-311 (1993).
18. Wolfsberg, T. G. et al. The precursor region of a protein active in sperm-egg fusion contains a metalloprotease and a disintegrin domain: structural, functional, and evolutionary implications. Proc. Natl Acad. Sci. USA 90, 10783-10787 (1993).
19. Yoshida, S., Setoguchi, M., Higuchi, Y., Akizuki, S. & Yamamoto, S. Molecular cloning of cDNA encoding MS2 antigen, a novel cell surface antigen strongly expressed in murine monocytic lineage. Int. Immunol. 2, 585-591 (1990).
20. Krätzschmar, J., Lum, L. & Blobel, C. P. Metargidin, a membrane-anchored metalloprotease-disintegrin protein with an RGD integrin binding sequence. J. Biol. Chem. 271, 4593-4596 (1996).
21. Yagami-Hiromasa, T. et al. A metalloprotease-disintegrin participating in myoblast fusion. Nature 377, 652-656 (1995).
22. Weskamp, G., Krätzschmar, J., Reid, M. S. & Blobel, C. P. MDC9, a widely expressed cellular disintegrin containing cytoplasmic SH3 ligand domains. J. Cell. Biol. 132, 717-726 (1996).
23. McMahan, C. J. et al. A novel IL-1 receptor, cloned from B cells by mammalian expression, is expressed in many cell types. EMBO J. 10, 2821-2832 (1991).
24. Peschon, J. J. et al. Early lymphocyte expansion is severely impaired in interleukin 7 receptor-deficient mice. J. Exp. Med. 180, 1955-1960 (1994).
25. Mortensen, R. M., Conner, D. A., Chao, S., Geisterfer-Lowrance, A. A. & Seidman, J. G. Production of homozygous mutant ES cells with a single targeting construct. Mol. Cell. Biol. 12, 2391-2395 (1992).
26. Dexter, T. M., Allen, T. D. & Lajtha, L. G. Conditions controlling the proliferation of haemopoietic stem cells in vitro. J. Cell. Physiol. 91, 335-344 (1976).
27. Snell, W. J. & White, J. M. The molecules of mammalian fertilization. Cell 85, 629-637 (1996).
28. Libby, P., Alroy, J. & Pereira, M. E. A neuraminidase from Trypanosoma cruzi removes sialic acid from the surface of mammalian myocardial and endothelial cells. J. Clin. Invest. 77, 127-135 (1986).
29. Warner, S. J. & Libby, P. Human vascular smooth muscle cells. Target for and source of tumor necrosis factor. J. Immunol. 142, 100-109 (1989).
30. Meier, T., Arni, S., Malarakannan, S., Poincelet, M. & Hoessli, D. Immunodetection of biotinylated lymphocyte-surface proteins by enhanced chemiluminescence: a non radioactive method for cell-surface protein analysis. Anal. Biochem. 204, 220-226 (1992).