Effect of DNase on the activity of neutrophil elastase, cathepsin G and proteinase 3 in the presence of DNA

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

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Bibliographische Detailangaben
Veröffentlicht in:	FEBS letters 2000-05, Vol.473 (2), p.154-156
Hauptverfasser:	Duranton, Jérôme, Belorgey, Didier, Carrère, Jacqueline, Donato, Lionel, Moritz, Thomas, Bieth, Joseph G.
Format:	Artikel
Sprache:	eng
Schlagworte:	Binding, Competitive cat G, neutrophil cathepsin G Cathepsin G Cathepsins - drug effects Cathepsins - metabolism Cellulose Chromatography, Affinity Cystic fibrosis Cystic Fibrosis - drug therapy Cystic Fibrosis - enzymology Deoxyribonucleases - metabolism Deoxyribonucleases - pharmacology Deoxyribonucleases - therapeutic use DNA DNA - metabolism DNA - pharmacology DNase Elastase Elastin - metabolism Humans Leukocyte Elastase - drug effects Leukocyte Elastase - metabolism Lung - drug effects Lung - enzymology Lung - metabolism Myeloblastin NE, neutrophil elastase Neutrophils - enzymology Oligonucleotides - metabolism Oligonucleotides - pharmacology PR3, neutrophil proteinase 3 Proteinase 3 Serine Endopeptidases - drug effects Serine Endopeptidases - metabolism
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Beschreibung
Zusammenfassung:	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
ISSN:	0014-5793 1873-3468
DOI:	10.1016/S0014-5793(00)01512-X