title: Tissue transglutaminase is the target in both rodent and primate tissues for celiac disease-specific autoantibodies.
abstract: BACKGROUND
  Endomysial antibodies have recently been shown to react with tissue transglutaminase. This study was undertaken to investigate whether the tissue distribution of transglutaminase is also compatible with reticulin, jejunal, and fibroblast autoantibody binding patterns.
  
  
  METHODS
  Sera from patients with and without celiac disease, monoclonal tissue transglutaminase antibodies, and sera from mice parenterally immunized against commercially available tissue transglutaminase, transglutaminase complexed with gliadin, or gliadin were used in indirect immunofluorescence and double-staining studies using both rodent and primate tissues as substrates. Also, antibody competition, affinity chromatography, and potassium thiocyanate extraction studies were undertaken.
  
  
  RESULTS
  Tissue transglutaminase antibody binding patterns were identical with the extracellular binding patterns seen with celiac patient sera. Human umbilical cord-derived fibroblasts exhibited both cytoplasmic and extracellular matrix staining. Double staining with patients' sera and tissue transglutaminase antibodies showed complete overlapping. Tissue transglutaminase effectively absorbed reticulin-endomysial antibodies from celiac sera, and patients' sera blocked the staining of the monoclonal tissue transglutaminase antibodies. Potassium thiocyanate extraction abolished the staining patterns, but they were elicited again after readdition of tissue transglutaminase.
  
  
  CONCLUSIONS
  Reticulin, endomysial, and jejunal antibodies detect transglutaminase in both rodent and primate tissues, indicating that these tissue autoantibodies are identical.
authors.affiliation: Institute of Medical Technology, Department of Pediatrics, University of Tampere, Finland.
authors.forename: I R
authors.initials: IR
authors.lastname: Korponay-Szabó
authors.forename: S
authors.initials: S
authors.lastname: Sulkanen
authors.forename: T
authors.initials: T
authors.lastname: Halttunen
authors.forename: F
authors.initials: F
authors.lastname: Maurano
authors.forename: M
authors.initials: M
authors.lastname: Rossi
authors.forename: G
authors.initials: G
authors.lastname: Mazzarella
authors.forename: K
authors.initials: K
authors.lastname: Laurila
authors.forename: R
authors.initials: R
authors.lastname: Troncone
authors.forename: M
authors.initials: M
authors.lastname: Mäki
mesh_terms: D000818:Animals; D000918:Antibody Specificity; D001323:Autoantibodies / Q000097:blood* / Q000276:immunology; D002446:Celiac Disease / Q000175:diagnosis* / Q000276:immunology; D002846:Chromatography, Affinity; D005347:Fibroblasts / Q000276:immunology*; D019084:Fluorescent Antibody Technique, Indirect; D000882:Haplorhini; D006801:Humans; D007070:Immunoglobulin A / Q000097:blood / Q000276:immunology; D007074:Immunoglobulin G / Q000097:blood / Q000276:immunology; D051379:Mice; D008807:Mice, Inbred BALB C; D051381:Rats; D013194:Staining and Labeling; D011503:Transglutaminases / Q000276:immunology*
chemical_list: D001323:Autoantibodies; D007070:Immunoglobulin A; D007074:Immunoglobulin G; D011503:Transglutaminases