title: Large intestinal mast cell count and proteinase expression is associated with larval burden in cyathostomin-infected horses.
abstract: BACKGROUND
  Cyathostomins are the principal pathogenic nematode of equidae worldwide. In other species mast cell (MC) proteinases, in particular chymases, appear to have protective roles. Knowledge of the equine intestinal immune response to cyathostomins is limited.
  
  
  OBJECTIVE
  To investigate MC numbers and proteinase expression in equine cyathostomin-infected large intestine.
  
  
  OBJECTIVE
  MC populations in the large intestine are positively associated with cyathostomin burden and predominantly express chymase.
  
  
  METHODS
  The caecal cyathostomin burden of naturally infected horses (n = 25) was determined by luminal counts and pepsin digest (mural count). MC were identified and enumerated in caecal tissue using toluidine blue (TB). Immunofluorescent labelling with polyclonal rabbit antibodies was used to demonstrate expression of equine tryptase and the chymase equine mast cell proteinase-1 (eqMCP-1) in Carnoy's fixed caecal sections.
  
  
  RESULTS
  Significant positive linear relationships were found between TB-stained mucosal and submucosal MC counts and total cyathostomin burden (P<0.001, r² >36%), and both luminal (P<0.010, r² >25%) and mural (P<0.001, r² >36%) larval counts. Similar relationships were found with mucosal and submucosal chymase and tryptase-labelled MC counts (total: P<0.004, r² >29%; luminal: P<0.004, r² >30%; and mural: P<0.030, r² >19%). With all three MC labels, mean MC counts were higher in the submucosa compared to the mucosa (P<0.001). All caecal MC appeared to express chymase, with a small number of MC expressing both tryptase and chymase.
  
  
  CONCLUSIONS
  Large intestinal MC counts are significantly associated with cyathostomin burden, with a predominance of chymase-positive MC. The burden is significantly associated with expression of MC proteinases, supporting their likely involvement in the intestinal immune response to cyathostomin infection. Further work to investigate the kinetics of proteinase expression, the possibility of differential proteinase expression and the role of these MC proteinases is warranted.
authors.affiliation: Veterinary Teaching Hospital, College of Sciences, Massey University, New Zealand. k.pickles@ed.ac.uk
authors.forename: K J
authors.initials: KJ
authors.lastname: Pickles
authors.forename: J A
authors.initials: JA
authors.lastname: Mair
authors.forename: N
authors.initials: N
authors.lastname: Lopez-Villalobos
authors.forename: D J
authors.initials: DJ
authors.lastname: Shaw
authors.forename: I
authors.initials: I
authors.lastname: Scott
authors.forename: W
authors.initials: W
authors.lastname: Pomroy
mesh_terms: D000818:Animals; D002432:Cecum / Q000166:cytology* / Q000473:pathology; D005260:Female; D015971:Gene Expression Regulation, Enzymologic / Q000502:physiology; D006734:Horse Diseases / Q000469:parasitology*; D006736:Horses; D007814:Larva; D008297:Male; D008407:Mast Cells / Q000166:cytology*; D009349:Nematode Infections / Q000473:pathology / Q000662:veterinary*; D010447:Peptide Hydrolases / Q000235:genetics / Q000378:metabolism*
chemical_list: D010447:Peptide Hydrolases