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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

Cathepsin-G and leukocyte elastase inactivate human tumor necrosis factor and lymphotoxin.

The addition of either cathepsin-G or leukocyte elastase to endotoxin- stimulated human peripheral blood monocytes decreased the immunoreactive tumor necrosis factor (TNF) detected in culture supernatants in a concentration-dependent manner. Both enzymes also induced a loss of supernatant cytolytic activity as determined on the WEHI-164 target cell line. Incubation of recombinant human TNF and lymphotoxin (LT) with either cathepsin-G or leukocyte elastase resulted in a loss of cytokine bioactivity. Examination of enzyme-treated recombinant cytokines by gel electrophoresis revealed that cathepsin-G cleaved LT into a 12.6-kDa fragment and leukocyte elastase fragmented LT into a 14.1-kDa product. On Western blots cathepsin-G and leukocyte elastase degraded TNF into 11- and 7.6-kDa fragments, respectively. Incubating leukocyte elastase with plasma elastase inhibitor alpha-1-antitrypsin prevented the loss of recombinant TNF bioactivity and blocked the degradation of this cytokine. This study suggests that two of the most abundant neutrophil proteases, cathepsin-G and leukocyte elastase, may be important regulators of TNF and LT bioactivity.[1]


  1. Cathepsin-G and leukocyte elastase inactivate human tumor necrosis factor and lymphotoxin. Scuderi, P., Nez, P.A., Duerr, M.L., Wong, B.J., Valdez, C.M. Cell. Immunol. (1991) [Pubmed]
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