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

被引：28

作者：

Duranton, J

Belorgey, D

Carrère, J

Donato, L

Moritz, T

Bieth, JG ^{[2
]}

机构：

[1] Hop Renee Sabran, F-83406 Giens, France

[2] Univ Strasbourg 1, Fac Pharm, INSERM,U392, Enzymol Lab, F-67400 Illkirch, France

[3] Hop Univ Hautepierre, Serv Peidat 2, F-67200 Strasbourg, France

来源：

FEBS LETTERS | 2000年 / 473卷 / 02期

关键词：

elastase; cathepsin G; proteinase; 3; DNA; DNase; cystic fibrosis;

D O I：

10.1016/S0014-5793(00)01512-X

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 tl;at 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. (C) 2000 Federation of European Biochemical Societies.

引用

页码：154 / 156

页数：3

共 21 条

[1]

BAGGIOLINI M, 1978, AGENTS ACTIONS, V8, P1

[2]

BARRETT AJ, 2004, HDB PROTEOLYTIC ENZY

[3] DNA BINDS NEUTROPHIL ELASTASE AND MUCUS PROTEINASE-INHIBITOR AND IMPAIRS THEIR FUNCTIONAL-ACTIVITY [J].