Matrix metalloproteinases and processing of pro-TNF-α
| Autor: | A J H Gearing, P Beckett, M Christodoulou, M Churchill, J M Clements, M Crimmin, A H Davidson, A H Drummond, W A Gallowav, R Gilbert, J L Gordon, T M Leber, M Mangan, K Miller, P Nayee, K Owen, S Patel, W Thomas, G Wells, L M Wood, K Woolley |
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| Rok vydání: | 1995 |
| Předmět: |
Gelatinases
Matrix metalloproteinase inhibitor Recombinant Fusion Proteins medicine.medical_treatment Molecular Sequence Data Immunology Cell Gene Expression Matrix metalloproteinase Pharmacology Biology Monocytes medicine Humans Immunology and Allergy Amino Acid Sequence Protein Precursors Matrilysin Tumor Necrosis Factor-alpha Metalloendopeptidases Cell Biology Cytokine medicine.anatomical_structure Collagenase Tumor necrosis factor alpha Peptides Protein Processing Post-Translational medicine.drug |
| Zdroj: | Journal of Leukocyte Biology. 57:774-777 |
| ISSN: | 1938-3673 0741-5400 |
| DOI: | 10.1002/jlb.57.5.774 |
| Popis: | Tumor necrosis factor-α (TNF-α) is released from a cell membrane-anchored precursor by proteolytic cleavage. We have shown that broad spectrum synthetic inhibitors of matrix metalloproteinases (MMPs) prevent the processing of the TNF precursor but do not inhibit the release of other cytokines. Purified MMPs, stromelysin, matrilysin, collagenase, and the gelatinases can all cleave a recombinant pro-TNF substrate to yield mature TNF. MMP inhibitors prevent the rise in blood levels of TNF after endotoxin administration in rats and are effective in animal models of inflammatory disease such as adjuvant arthritis. Drugs that inhibit MMP action and TNF release show great promise for the treatment of autoimmune inflammatory diseases. J. Leukoc. Biol. 57: 774–777; 1995. |
| Databáze: | OpenAIRE |
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