title: House dust mite allergen Der p 1 effects on sinonasal epithelial tight junctions.
abstract: BACKGROUND
  Epithelial permeability is highly dependent upon the integrity of tight junctions, which are cell-cell adhesion complexes located at the apical aspect of the lateral membrane of polarized epithelial cells. We hypothesize that sinonasal epithelial exposure to Der p 1 house dust mite antigen decreases expression of tight junction proteins (TJPs), representing a potential mechanism for increased permeability and presentation of antigens across the sinonasal epithelial layer.
  
  
  METHODS
  Confluent cultured primary human sinonasal epithelial cells were exposed to recombinant Der p 1 antigen vs control, and transepithelial resistance measurements were performed over 24 hours. Antibody staining for a panel of TJPs was examined with immunofluorescence/confocal microscopy and Western blotting. Tissue for these experiments was obtained from 4 patients total.
  
  
  RESULTS
  Der p 1 exposed sinonasal cells showed a marked decrease in transepithelial resistance when compared to control cells. In addition, results of Western immunoblot and immunofluorescent labeling demonstrated decreased expression of TJPs claudin-1 and junction adhesion molecule-A (JAM-A) in Der p 1-exposed cultured sinonasal cells vs controls.
  
  
  CONCLUSIONS
  Der p 1 antigen exposure decreases sinonasal epithelium TJP expression, most notably seen in JAM-A and claudin-1 in these preliminary experiments. This decreased TJP expression likely contributes to increased epithelial permeability and represents a potential mechanism for transepithelial antigen exposure in allergic rhinitis.
authors.affiliation: Department of Otolaryngology, Emory University, Atlanta, GA 30308, USA.
authors.forename: Oswaldo A
authors.initials: OA
authors.lastname: Henriquez
authors.forename: Kyle
authors.initials: K
authors.lastname: Den Beste
authors.forename: Elizabeth K
authors.initials: EK
authors.lastname: Hoddeson
authors.forename: Charles A
authors.initials: CA
authors.lastname: Parkos
authors.forename: Asma
authors.initials: A
authors.lastname: Nusrat
authors.forename: Sarah K
authors.initials: SK
authors.lastname: Wise
mesh_terms: D039741:Antigens, Dermatophagoides / Q000378:metabolism*; D060829:Arthropod Proteins / Q000378:metabolism*; D015153:Blotting, Western; D015820:Cadherins / Q000378:metabolism; D015815:Cell Adhesion Molecules / Q000378:metabolism; D062445:Claudin-1 / Q000378:metabolism; D003546:Cysteine Endopeptidases / Q000378:metabolism*; D004847:Epithelial Cells / Q000378:metabolism*; D006801:Humans; D018613:Microscopy, Confocal; D008856:Microscopy, Fluorescence; D009296:Nasal Cavity / Q000378:metabolism*; D062793:Occludin / Q000378:metabolism; D010539:Permeability; D011956:Receptors, Cell Surface / Q000378:metabolism; D019108:Tight Junctions / Q000378:metabolism*
chemical_list: D039741:Antigens, Dermatophagoides; D060829:Arthropod Proteins; D015820:Cadherins; D015815:Cell Adhesion Molecules; D062445:Claudin-1; C407243:F11R protein, human; D062793:Occludin; D011956:Receptors, Cell Surface; D003546:Cysteine Endopeptidases; C451162:Dermatophagoides pteronyssinus antigen p 1
keywords: allergic rhinitis; claudin-1; epithelium; house dust mite; junction adhesion molecule; rhinitis; sinonasal; tight junction