Severe neutrophil-mediated lung inflammation in myeloperoxidase-deficient mice exposed to zymosan

Inflamm Res. 2012 Mar;61(3):197-205. doi: 10.1007/s00011-011-0401-y. Epub 2011 Nov 25.

Abstract

Objective and design: This study examines the role of myeloperoxidase (MPO), a major constituent of neutrophils that generates hypochlorous acid, in neutrophil recruitment into the zymosan-exposed lung of mice.

Methods: Mice were inoculated intranasally with zymosan. The accumulation of neutrophils and other inflammatory cells within the lung was analyzed by flow cytometry. Macrophage inflammatory protein 2 (MIP-2) expression in the lung was quantified, and the contribution of this chemokine to neutrophil accumulation was examined by intranasal administration of MIP-2 antibody. The cellular sources of MIP-2 were identified, and the production of this chemokine from macrophages and neutrophils was quantified in vitro.

Results: Zymosan exposure led to greater neutrophil infiltration into the lungs of MPO(-/-) mice relative to wild-type mice. This was associated with higher MIP-2 levels in the mutant mice. Neutralization of MIP-2 in vivo significantly reduced neutrophil infiltration. Neutrophils from MPO(-/-) mice produced more MIP-2, and the production was reduced when MPO was added exogenously.

Conclusions: MPO deficiency results in severe lung inflammation in mice exposed to zymosan. Relatively high MIP-2 levels likely contribute to the strong inflammatory response in these animals.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bronchoalveolar Lavage Fluid / cytology
  • Cell Count
  • Chemokine CXCL2 / immunology*
  • Macrophages / immunology
  • Mice
  • Mice, Inbred C57BL
  • Mice, Knockout
  • Neutrophils / immunology*
  • Peroxidase / deficiency
  • Peroxidase / genetics
  • Peroxidase / immunology*
  • Pneumonia / chemically induced
  • Pneumonia / immunology*
  • Pneumonia / pathology
  • Zymosan

Substances

  • Chemokine CXCL2
  • Cxcl2 protein, mouse
  • Zymosan
  • Peroxidase