Effect of DNase on the activity of neutrophil elastase, cathepsin G and proteinase 3 in the presence of DNA |
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Authors: | Duranton J Belorgey D Carrère J Donato L Moritz T Bieth J G |
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Affiliation: | Laboratoire d'Enzymologie, INSERM Unité 392, Faculté de Pharmacie, Université Louis Pasteur de Strasbourg, F-67400, Illkirch, France. |
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Abstract: | It has been shown previously that DNA binds and inhibits neutrophil elastase (NE). Here we demonstrate that DNA has a better affinity for neutrophil cathepsin G (cat G) than for NE and is a better inhibitor of cat G than of NE. DNase-generated <0.5 kb DNA fragments inhibit NE and cat G as potently as full length DNA. This rationalises our observation that administration of DNase to cystic fibrosis patients does not enhance the NE and cat G activity of their lung secretions. Neutrophil proteinase 3 is not inhibited by DNA and might thus be the most harmful proteinase in inflammatory lung diseases. |
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