Recombinant human neutral endopeptidase ameliorates pancreatic elastase-induced lung injury

Surgery. 2002 Aug;132(2):193-9. doi: 10.1067/msy.2002.125309.

Abstract

Background: Genetic deletion of neutral endopeptidase (NEP), a cell-surface metalloprotease that degrades proinflammatory peptides, exacerbates lung injury induced by pancreatic elastase in a model of pancreatitis-associated lung injury. We tested 3 hypotheses: (1) genetic deletion of NEP prolongs lung recovery after elastase injections; (2) elastase-mediated lung injury is associated with down-regulation of NEP; and (3) pretreatment of NEP (-/-) and (+/+) animals with recombinant human NEP (rhNEP) reduces pulmonary damage in this model.

Methods: NEP (+/+) or (-/-) mice were injected with pancreatic elastase (0.085 U/g/dose intraperitoneally) or saline carrier at t = 0 hours and t = 1 hour. Some mice were pretreated with rhNEP (3 mg/kg intraperitoneally). Serum elastase, lung histologic score, myeloperoxidase, and NEP activities were measured at 4, 8, or 12 hours.

Results: NEP (-/-) mice had worse pulmonary inflammation at 4 and 8 hours versus (+/+) mice. Lung NEP activity was similar in elastase-treated and control (+/+) animals. Pretreatment with rhNEP reduced myeloperoxidase and improved histology at 4 hours in NEP (-/-) and (+/+) mice.

Conclusions: Pancreatic elastase induces lung injury that is worse and prolonged in NEP (-/-) mice. Pretreatment with rhNEP ameliorates this injury. Thus, upregulation of NEP is a potential therapeutic approach for pancreatitis-associated lung injury.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Disease Models, Animal
  • Female
  • Humans
  • Male
  • Mice
  • Mice, Inbred C57BL
  • Mice, Mutant Strains
  • Neprilysin / metabolism
  • Neprilysin / pharmacology*
  • Neutrophils / enzymology
  • Pancreatic Elastase / metabolism
  • Pancreatic Elastase / pharmacology*
  • Pancreatitis / complications
  • Pancreatitis / metabolism
  • Peroxidase / metabolism
  • Pneumonia / chemically induced
  • Pneumonia / enzymology*
  • Pneumonia / etiology
  • Recombinant Proteins / metabolism
  • Recombinant Proteins / pharmacology
  • Respiratory Mucosa / enzymology

Substances

  • Recombinant Proteins
  • Peroxidase
  • Pancreatic Elastase
  • Neprilysin