Cathepsin-G and leukocyte elastase inactivate human tumor necrosis factor and lymphotoxin.
Cell Immunol
; 135(2): 299-313, 1991 Jul.
Article
em En
| MEDLINE
| ID: mdl-2036673
ABSTRACT
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.
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Base de dados:
MEDLINE
Assunto principal:
Elastase Pancreática
/
Catepsinas
/
Linfotoxina-alfa
/
Fator de Necrose Tumoral alfa
Idioma:
En
Ano de publicação:
1991
Tipo de documento:
Article