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PMID: 10812064 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

FEBS letters ·Vol. 473 ·No. 2 ·2000-05-12 ·Pages 154-6

Duranton J, Belorgey D, Carrère J, Donato L, Moritz T, Bieth JG

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.

MeSH Terms
Binding, Competitive Cathepsin G Cathepsins/drug effects,metabolism Cellulose Chromatography, Affinity Cystic Fibrosis/drug therapy,enzymology DNA/metabolism,pharmacology Deoxyribonucleases/metabolism,pharmacology,therapeutic use Elastin/metabolism Humans Leukocyte Elastase/drug effects,metabolism Lung/drug effects,enzymology,metabolism Myeloblastin Neutrophils/enzymology Oligonucleotides/metabolism,pharmacology Serine Endopeptidases/drug effects,metabolism
Chemicals
Oligonucleotides Cellulose DNA Elastin Deoxyribonucleases Cathepsins Serine Endopeptidases CTSG protein, human Cathepsin G Leukocyte Elastase Myeloblastin
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Duranton J
Laboratoire d'Enzymologie, INSERM Unité 392, Faculté de Pharmacie, Université Louis Pasteur de Strasbourg, F-67400, Illkirch, France.
Belorgey D
Carrère J
Donato L
Moritz T
Bieth J G
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
Published
2000-05-12
Pages
154-6
Language
English
Region
England
NLM ID
0155157
Subset
IM
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