Gene interactions and pathways from curated databases and text-mining
J Leukoc Biol 1995, PMID: 7759957

Matrix metalloproteinases and processing of pro-TNF-alpha.

Gearing, A J; Beckett, P; Christodoulou, M; Churchill, M; Clements, J M; Crimmin, M; Davidson, A H; Drummond, A H; Galloway, W A; Gilbert, R

Tumor necrosis factor-alpha (TNF-alpha) 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.

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Text Mining Data

TNF → MMP: " 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 "

Manually curated Databases

No curated data.