DNA binds neutrophil elastase and mucus proteinase inhibitor and impairs their functional activity

• Published in: FEBS letters Vol. 361; no. 2; pp. 265 - 268
• Main Authors: Belorgey, Didier, Bieth, Joseph G.
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 20.03.1995
• Subjects: Cellulose - analogs & derivatives; Chromatography, Affinity; Cystic fibrosis; DNA; DNA - metabolism; Elastase; Enzyme kinetics; Humans; Kinetics; Leukocyte Elastase; MeOSuc-Ala2-Pro-Val-pNA; methoxysuccinyl-Ala2-Pro-Val-p-nitroanilide; MPI; Mucus proteinase inhibitor; mucus proteinase inhibitor = secretory leucoprotease inhibitor (SLPI); neutrophil elastase; Pancreatic Elastase - antagonists & inhibitors; Pancreatic Elastase - metabolism; Proteinase Inhibitory Proteins, Secretory; Proteins - metabolism; RBB-elastin; remazol Brilliant-blue elastin; Sepharose; Serine Proteinase Inhibitors - metabolism; Substrate Specificity; Suc-Ala3-pNA; succinyl-Ala3-p-nitroanilide; Time Factors; Mucus proteinase inhibitor; RBB-elastin; Suc-Ala 3- pNA; DNA; MeOSuc-Ala 2-Pro-Val- pNA; NE; MPI; Cystic fibrosis; Elastase; Enzyme kinetics
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(95)00173-7

DNA binds neutrophil elastase and mucus proteinase inhibitor as evidenced by affinity chromatography on elastase-Sepharose, inhibitor-Sepharose and DNA-cellulose. DNA is a potent hyperbolic inhibitor of elastase. The polynucleotide-enzyme complex is partially active on synthetic substrates and on elastin. DNA strongly increases k diss and K i for the inhibition of elastase by mucus proteinase inhibitor ▪ The above effects are all salt-dependent. At physiological ionic strength, DNA is a potent inhibitor of the elastolytic activity of elastase and increases k diss and K i for the elastase-mucus proteinase inhibitor interaction 160-fold and 100-fold, respectively.