title: Repair of the injury to respiratory epithelial cells characteristic of asthma is stimulated by Allomyrina dichotoma agglutinin specific serum glycoproteins.
abstract: BACKGROUND
  The airway epithelium acts as a protective barrier, separating the external environment from the underlying tissue. Daily challenges result in damage to the epithelium that, in normal individuals, is quickly and effectively repaired. In respiratory diseases, such as asthma, this repair is compromised. Following injury to the epithelium, plasma leaks into the airway lumen acting as a protective protein cap. Carbohydrates are mediators of epithelial repair, however, the associated regulatory proteins remain unknown.
  
  
  OBJECTIVE
  To identify mediators of epithelial repair based on their carbohydrate moieties using an in vitro wound repair culture model of human airway epithelial cells (1HAEo(-)).
  
  
  METHODS
  Using the lectin Allomyrina dichotoma agglutinin (AlloA) as a tool, ligands essential in the repair of damaged epithelium were characterized. AlloA was subsequently used to purify and identify a glycoprotein associated with epithelial repair.
  
  
  RESULTS
  The addition of AlloA to the media of mechanically wounded monolayers inhibited repair. Fetuin, a highly glycosylated serum protein, was identified as a glycoprotein bound by AlloA. The addition of fetuin to serum starved monolayers stimulated wound closure.
  
  
  CONCLUSIONS
  These results indicate that following mechanical injury to the epithelium, serum glycoproteins, not only provide a protective barrier, but also are involved in the initiation of wound closure.
authors.affiliation: James Hogg iCAPTURE Centre for Cardiovascular and Pulmonary Research, University of British Columbia, Department of Medicine, University of British Columbia, Vancouver BC, Canada.
authors.forename: B J
authors.initials: BJ
authors.lastname: Patchell
authors.forename: D R
authors.initials: DR
authors.lastname: Dorscheid
mesh_terms: D000818:Animals; D001249:Asthma / Q000473:pathology / Q000503:physiopathology*; D001798:Blood Proteins / Q000378:metabolism; D002478:Cells, Cultured; D011232:Chemical Precipitation; D004305:Dose-Response Relationship, Drug; D004847:Epithelial Cells / Q000187:drug effects / Q000378:metabolism / Q000502:physiology*; D006023:Glycoproteins / Q000302:isolation & purification / Q000378:metabolism; D006801:Humans; D037102:Lectins / Q000378:metabolism / Q000494:pharmacology*; D008954:Models, Biological; D037121:Plant Lectins / Q000378:metabolism / Q000494:pharmacology; D012137:Respiratory System / Q000187:drug effects / Q000473:pathology*; D014945:Wound Healing / Q000502:physiology; D000509:alpha-Fetoproteins / Q000494:pharmacology; D000093422:Glycated Serum Proteins
chemical_list: C045794:Allomyrina lectin; D001798:Blood Proteins; D006023:Glycoproteins; C045475:Griffonia simplicifolia lectins; D037102:Lectins; D037121:Plant Lectins; D000509:alpha-Fetoproteins; D000093422:Glycated Serum Proteins