Phenotypic characteristics of nasal mast cells in a mouse model of allergic rhinitis

ORL J Otorhinolaryngol Relat Spec. 2014;76(6):303-13. doi: 10.1159/000369142. Epub 2014 Dec 17.

Abstract

Background: Mast cells (MCs) in the nasal respiratory mucosa (NRM) play a triggering role in the pathogenesis of allergic rhinitis (AR). Recent research evidence in mouse models of AR suggests an underlying MC-related allergic response in mouse nasal olfactory mucosa (NOM).

Objective: We sought to investigate the phenotypic characteristics of nasal MCs in a mouse model of AR.

Methods: By MC-specific staining and immunohistochemistry, we analyzed the subset, protease and IgE-binding phenotypes of nasal MCs in ovalbumin (OVA)-sensitized unchallenged and challenged mice.

Results: In OVA-sensitized challenged mice, increased serum OVA-specific IgE levels (p < 0.001) and eosinophil infiltration confirmed AR induction. In addition to constitutive connective tissue MCs, mucosal MCs were induced in NRM and NOM of OVA-sensitized challenged mice. Connective tissue MCs and mucosal MCs in mouse NRM and NOM were positive for mouse MC protease-1, -4, -5, -6, -7 and carboxypeptidase-A3. In line with MCs in NRM, there were increased numbers (p = 0.019) and proportions (p = 0.027) of MCs with surface-bound IgE in NOM of OVA-sensitized challenged mice.

Conclusion: In the setting of AR, MCs in mouse NOM exhibit the same subset, protease and IgE-binding phenotypes as MCs in mouse NRM.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carboxypeptidases / metabolism
  • Disease Models, Animal
  • Endopeptidases / metabolism
  • Enzyme-Linked Immunosorbent Assay
  • Eosinophils / immunology
  • Female
  • Immunoenzyme Techniques
  • Immunoglobulin E / blood
  • Mast Cells / immunology*
  • Mast Cells / metabolism
  • Mice
  • Mice, Inbred BALB C
  • Nasal Mucosa / cytology*
  • Phenotype
  • Rhinitis, Allergic / immunology*
  • Rhinitis, Allergic / metabolism

Substances

  • Immunoglobulin E
  • Carboxypeptidases
  • Endopeptidases