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

FEBS Lett. 1995 Mar 20;361(2-3):265-8. doi: 10.1016/0014-5793(95)00173-7.

Abstract

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 kdiss and Ki for the inhibition of elastase by mucus proteinase inhibitor [formula: see text] The above effects are all salt-dependent. At physiological ionic strength, DNA is a potent inhibitor of the elastolytic activity of elastase and increases kdiss and Ki for the elastase-mucus proteinase inhibitor interaction 160-fold and 100-fold, respectively.

MeSH terms

  • Cellulose / analogs & derivatives
  • Chromatography, Affinity
  • DNA / metabolism*
  • Humans
  • Kinetics
  • Leukocyte Elastase
  • Pancreatic Elastase / antagonists & inhibitors
  • Pancreatic Elastase / metabolism*
  • Proteinase Inhibitory Proteins, Secretory
  • Proteins / metabolism*
  • Sepharose
  • Serine Proteinase Inhibitors / metabolism*
  • Substrate Specificity
  • Time Factors

Substances

  • DNA-cellulose
  • Proteinase Inhibitory Proteins, Secretory
  • Proteins
  • Serine Proteinase Inhibitors
  • Cellulose
  • DNA
  • Sepharose
  • Pancreatic Elastase
  • Leukocyte Elastase