The Experts below are selected from a list of 19290 Experts worldwide ranked by ideXlab platform
Markku Maki - One of the best experts on this subject based on the ideXlab platform.
-
tissue Transglutaminase autoantibody enzyme linked immunosorbent assay in detecting celiac disease
Gastroenterology, 1998Co-Authors: S Sulkanen, Tuula Halttunen, Kaija Laurila, Ilma Rita Korponayszabo, Annikki Sarnesto, Pekka Collin, Kaija-leena Kolho, Erkki Savilahti, Markku MakiAbstract:BACKGROUND & AIMS: Tissue Transglutaminase has been reported to be the target for endomysial antibodies in celiac disease. We sought to establish whether immunoglobulin (Ig) A class tissue Transglutaminase autoantibodies can be considered specific for celiac disease. METHODS: Serum samples from 136 patients with untreated celiac disease (diagnosed according to the criteria of the European Society for Pediatric Gastroenterology, Hepatology and Nutrition) and 207 disease controls were studied. Enzyme-linked immunosorbent assay (ELISA) and Western blots were performed using calcium-treated and untreated tissue Transglutaminase as antigen. Reticulin, endomysial, and mouse monoclonal tissue Transglutaminase antibodies were studied by an indirect immunofluorescence method and gliadin antibodies with ELISA. RESULTS: The calcium-activated tissue Transglutaminase autoantibody ELISA was highly sensitive (129 of 136) and specific (194 of 207) in detecting celiac disease. The new autoantibody ELISA test correlated well with the endomysial antibody test. Tissue Transglutaminase autoantibody ELISA showed a clearly better predictive potential than the IgA class gliadin antibody ELISA. Immunoblots and ELISA blocking studies showed that calcium is needed for the specific antigen-antibody reaction to occur. Double immunofluorescence staining in human umbilical cord with sera from patients with celiac disease and with monoclonal tissue Transglutaminase antibodies showed complete overlap. CONCLUSIONS: Calcium-activated tissue Transglutaminase autoantibody ELISA is highly accurate in detecting untreated celiac disease. Tissue Transglutaminase seems to be the target self-antigen for endomysial antibodies.
-
tissue Transglutaminase autoantibody enzyme linked immunosorbent assay in detecting celiac disease
Gastroenterology, 1998Co-Authors: S Sulkanen, Tuula Halttunen, Kaija Laurila, Ilma Rita Korponayszabo, Annikki Sarnesto, Pekka Collin, Kaija-leena Kolho, Erkki Savilahti, Markku MakiAbstract:Abstract Background & Aims: Tissue Transglutaminase has been reported to be the target for endomysial antibodies in celiac disease. We sought to establish whether immunoglobulin (Ig) A class tissue Transglutaminase autoantibodies can be considered specific for celiac disease. Methods: Serum samples from 136 patients with untreated celiac disease (diagnosed according to the criteria of the European Society for Pediatric Gastroenterology, Hepatology and Nutrition) and 207 disease controls were studied. Enzyme-linked immunosorbent assay (ELISA) and Western blots were performed using calcium-treated and untreated tissue Transglutaminase as antigen. Reticulin, endomysial, and mouse monoclonal tissue Transglutaminase antibodies were studied by an indirect immunofluorescence method and gliadin antibodies with ELISA. Results: The calcium-activated tissue Transglutaminase autoantibody ELISA was highly sensitive (129 of 136) and specific (194 of 207) in detecting celiac disease. The new autoantibody ELISA test correlated well with the endomysial antibody test. Tissue Transglutaminase autoantibody ELISA showed a clearly better predictive potential than the IgA class gliadin antibody ELISA. Immunoblots and ELISA blocking studies showed that calcium is needed for the specific antigen-antibody reaction to occur. Double immunofluorescence staining in human umbilical cord with sera from patients with celiac disease and with monoclonal tissue Transglutaminase antibodies showed complete overlap. Conclusions: Calcium-activated tissue Transglutaminase autoantibody ELISA is highly accurate in detecting untreated celiac disease. Tissue Transglutaminase seems to be the target self-antigen for endomysial antibodies. GASTROENTEROLOGY 1998;115:1322-1328
-
tissue Transglutaminase autoantibody enzyme linked immunosorbent assay in detecting celiac disease
Gastroenterology, 1998Co-Authors: S Sulkanen, Tuula Halttunen, Kaija Laurila, Ilma Rita Korponayszabo, Annikki Sarnesto, Pekka Collin, Kaija-leena Kolho, Erkki Savilahti, Markku MakiAbstract:BACKGROUND & AIMS: Tissue Transglutaminase has been reported to be the target for endomysial antibodies in celiac disease. We sought to establish whether immunoglobulin (Ig) A class tissue Transglutaminase autoantibodies can be considered specific for celiac disease. METHODS: Serum samples from 136 patients with untreated celiac disease (diagnosed according to the criteria of the European Society for Pediatric Gastroenterology, Hepatology and Nutrition) and 207 disease controls were studied. Enzyme-linked immunosorbent assay (ELISA) and Western blots were performed using calcium-treated and untreated tissue Transglutaminase as antigen. Reticulin, endomysial, and mouse monoclonal tissue Transglutaminase antibodies were studied by an indirect immunofluorescence method and gliadin antibodies with ELISA. RESULTS: The calcium-activated tissue Transglutaminase autoantibody ELISA was highly sensitive (129 of 136) and specific (194 of 207) in detecting celiac disease. The new autoantibody ELISA test correlated well with the endomysial antibody test. Tissue Transglutaminase autoantibody ELISA showed a clearly better predictive potential than the IgA class gliadin antibody ELISA. Immunoblots and ELISA blocking studies showed that calcium is needed for the specific antigen-antibody reaction to occur. Double immunofluorescence staining in human umbilical cord with sera from patients with celiac disease and with monoclonal tissue Transglutaminase antibodies showed complete overlap. CONCLUSIONS: Calcium-activated tissue Transglutaminase autoantibody ELISA is highly accurate in detecting untreated celiac disease. Tissue Transglutaminase seems to be the target self-antigen for endomysial antibodies.
Ilma Rita Korponayszabo - One of the best experts on this subject based on the ideXlab platform.
-
tissue Transglutaminase autoantibody enzyme linked immunosorbent assay in detecting celiac disease
Gastroenterology, 1998Co-Authors: S Sulkanen, Tuula Halttunen, Kaija Laurila, Ilma Rita Korponayszabo, Annikki Sarnesto, Pekka Collin, Kaija-leena Kolho, Erkki Savilahti, Markku MakiAbstract:BACKGROUND & AIMS: Tissue Transglutaminase has been reported to be the target for endomysial antibodies in celiac disease. We sought to establish whether immunoglobulin (Ig) A class tissue Transglutaminase autoantibodies can be considered specific for celiac disease. METHODS: Serum samples from 136 patients with untreated celiac disease (diagnosed according to the criteria of the European Society for Pediatric Gastroenterology, Hepatology and Nutrition) and 207 disease controls were studied. Enzyme-linked immunosorbent assay (ELISA) and Western blots were performed using calcium-treated and untreated tissue Transglutaminase as antigen. Reticulin, endomysial, and mouse monoclonal tissue Transglutaminase antibodies were studied by an indirect immunofluorescence method and gliadin antibodies with ELISA. RESULTS: The calcium-activated tissue Transglutaminase autoantibody ELISA was highly sensitive (129 of 136) and specific (194 of 207) in detecting celiac disease. The new autoantibody ELISA test correlated well with the endomysial antibody test. Tissue Transglutaminase autoantibody ELISA showed a clearly better predictive potential than the IgA class gliadin antibody ELISA. Immunoblots and ELISA blocking studies showed that calcium is needed for the specific antigen-antibody reaction to occur. Double immunofluorescence staining in human umbilical cord with sera from patients with celiac disease and with monoclonal tissue Transglutaminase antibodies showed complete overlap. CONCLUSIONS: Calcium-activated tissue Transglutaminase autoantibody ELISA is highly accurate in detecting untreated celiac disease. Tissue Transglutaminase seems to be the target self-antigen for endomysial antibodies.
-
tissue Transglutaminase autoantibody enzyme linked immunosorbent assay in detecting celiac disease
Gastroenterology, 1998Co-Authors: S Sulkanen, Tuula Halttunen, Kaija Laurila, Ilma Rita Korponayszabo, Annikki Sarnesto, Pekka Collin, Kaija-leena Kolho, Erkki Savilahti, Markku MakiAbstract:Abstract Background & Aims: Tissue Transglutaminase has been reported to be the target for endomysial antibodies in celiac disease. We sought to establish whether immunoglobulin (Ig) A class tissue Transglutaminase autoantibodies can be considered specific for celiac disease. Methods: Serum samples from 136 patients with untreated celiac disease (diagnosed according to the criteria of the European Society for Pediatric Gastroenterology, Hepatology and Nutrition) and 207 disease controls were studied. Enzyme-linked immunosorbent assay (ELISA) and Western blots were performed using calcium-treated and untreated tissue Transglutaminase as antigen. Reticulin, endomysial, and mouse monoclonal tissue Transglutaminase antibodies were studied by an indirect immunofluorescence method and gliadin antibodies with ELISA. Results: The calcium-activated tissue Transglutaminase autoantibody ELISA was highly sensitive (129 of 136) and specific (194 of 207) in detecting celiac disease. The new autoantibody ELISA test correlated well with the endomysial antibody test. Tissue Transglutaminase autoantibody ELISA showed a clearly better predictive potential than the IgA class gliadin antibody ELISA. Immunoblots and ELISA blocking studies showed that calcium is needed for the specific antigen-antibody reaction to occur. Double immunofluorescence staining in human umbilical cord with sera from patients with celiac disease and with monoclonal tissue Transglutaminase antibodies showed complete overlap. Conclusions: Calcium-activated tissue Transglutaminase autoantibody ELISA is highly accurate in detecting untreated celiac disease. Tissue Transglutaminase seems to be the target self-antigen for endomysial antibodies. GASTROENTEROLOGY 1998;115:1322-1328
-
tissue Transglutaminase autoantibody enzyme linked immunosorbent assay in detecting celiac disease
Gastroenterology, 1998Co-Authors: S Sulkanen, Tuula Halttunen, Kaija Laurila, Ilma Rita Korponayszabo, Annikki Sarnesto, Pekka Collin, Kaija-leena Kolho, Erkki Savilahti, Markku MakiAbstract:BACKGROUND & AIMS: Tissue Transglutaminase has been reported to be the target for endomysial antibodies in celiac disease. We sought to establish whether immunoglobulin (Ig) A class tissue Transglutaminase autoantibodies can be considered specific for celiac disease. METHODS: Serum samples from 136 patients with untreated celiac disease (diagnosed according to the criteria of the European Society for Pediatric Gastroenterology, Hepatology and Nutrition) and 207 disease controls were studied. Enzyme-linked immunosorbent assay (ELISA) and Western blots were performed using calcium-treated and untreated tissue Transglutaminase as antigen. Reticulin, endomysial, and mouse monoclonal tissue Transglutaminase antibodies were studied by an indirect immunofluorescence method and gliadin antibodies with ELISA. RESULTS: The calcium-activated tissue Transglutaminase autoantibody ELISA was highly sensitive (129 of 136) and specific (194 of 207) in detecting celiac disease. The new autoantibody ELISA test correlated well with the endomysial antibody test. Tissue Transglutaminase autoantibody ELISA showed a clearly better predictive potential than the IgA class gliadin antibody ELISA. Immunoblots and ELISA blocking studies showed that calcium is needed for the specific antigen-antibody reaction to occur. Double immunofluorescence staining in human umbilical cord with sera from patients with celiac disease and with monoclonal tissue Transglutaminase antibodies showed complete overlap. CONCLUSIONS: Calcium-activated tissue Transglutaminase autoantibody ELISA is highly accurate in detecting untreated celiac disease. Tissue Transglutaminase seems to be the target self-antigen for endomysial antibodies.
David J Unsworth - One of the best experts on this subject based on the ideXlab platform.
-
anti tissue Transglutaminase anti endomysium and anti r1 reticulin autoantibodies the antibody trinity of coeliac disease
Clinical and Experimental Immunology, 1999Co-Authors: Richard J. Lock, J E M Gilmour, David J UnsworthAbstract:Anti-tissue Transglutaminase has been recently described as the predominant autoantigen in coeliac disease. We purified serum anti-tissue Transglutaminase antibodies from three patients with coeliac disease by column chromatography and eluted tissue section-bound R1-anti-reticulin antibodies from sections of rat tissue for two of these. Lastly, we generated seven mouse MoAbs to guinea pig tissue Transglutaminase. Each preparation was examined for anti-tissue Transglutaminase, anti-endomysium, anti-R1 reticulin and anti-gliadin antibodies. Column-purified patient antibodies and 2/7 mouse MoAbs gave characteristic anti-endomysium/anti-R1 reticulin reactivity on rat, monkey and human tissue. All positive sera gave indistinguishable patterns of immunofluorescence on rat liver, kidney and stomach, monkey oesophagus, and human umbilical cord. Anti-R1-reticulin eluted from sections showed anti-tissue Transglutaminase reactivity in 2/2 cases, but 0/2 showed anti-gliadin reactivity. In both, tissue section-eluted anti-R1 reticulin gave endomysial staining on monkey oesophagus. None of the mouse monoclonals, or any of the purified patient's anti-tissue Transglutaminase or anti-R1-reticulin antibody showed any reactivity with gliadin. These data confirm tissue Transglutaminase as the predominant autoantigen in coeliac disease and suggest that both anti-endomysium and anti-R1 reticulin reactivities seen in coeliac disease arise due to an immune response to tissue Transglutaminase. Rigorous immunoabsorption was sufficient to abrogate reactivity in the tissue Transglutaminase ELISA, but failed to completely absorb anti-endomysium and anti-reticulin activity. The possibility remains that some of the anti-endomysium and anti-reticulin activity was directed against antigens other than tissue Transglutaminase.
-
anti tissue Transglutaminase anti endomysium and anti r1 reticulin autoantibodies the antibody trinity of coeliac disease
Clinical and Experimental Immunology, 1999Co-Authors: Richard J. Lock, J E M Gilmour, David J UnsworthAbstract:Anti-tissue Transglutaminase has been recently described as the predominant autoantigen in coeliac disease. We purified serum anti-tissue Transglutaminase antibodies from three patients with coeliac disease by column chromatography and eluted tissue section-bound R1-anti-reticulin antibodies from sections of rat tissue for two of these. Lastly, we generated seven mouse MoAbs to guinea pig tissue Transglutaminase. Each preparation was examined for anti-tissue Transglutaminase, anti-endomysium, anti-R1 reticulin and anti-gliadin antibodies. Column-purified patient antibodies and 2/7 mouse MoAbs gave characteristic anti-endomysium/anti-R1 reticulin reactivity on rat, monkey and human tissue. All positive sera gave indistinguishable patterns of immunofluorescence on rat liver, kidney and stomach, monkey oesophagus, and human umbilical cord. Anti-R1-reticulin eluted from sections showed anti-tissue Transglutaminase reactivity in 2/2 cases, but 0/2 showed anti-gliadin reactivity. In both, tissue section-eluted anti-R1 reticulin gave endomysial staining on monkey oesophagus. None of the mouse monoclonals, or any of the purified patient's anti-tissue Transglutaminase or anti-R1-reticulin antibody showed any reactivity with gliadin. These data confirm tissue Transglutaminase as the predominant autoantigen in coeliac disease and suggest that both anti-endomysium and anti-R1 reticulin reactivities seen in coeliac disease arise due to an immune response to tissue Transglutaminase. Rigorous immunoabsorption was sufficient to abrogate reactivity in the tissue Transglutaminase ELISA, but failed to completely absorb anti-endomysium and anti-reticulin activity. The possibility remains that some of the anti-endomysium and anti-reticulin activity was directed against antigens other than tissue Transglutaminase.
S Sulkanen - One of the best experts on this subject based on the ideXlab platform.
-
tissue Transglutaminase autoantibody enzyme linked immunosorbent assay in detecting celiac disease
Gastroenterology, 1998Co-Authors: S Sulkanen, Tuula Halttunen, Kaija Laurila, Ilma Rita Korponayszabo, Annikki Sarnesto, Pekka Collin, Kaija-leena Kolho, Erkki Savilahti, Markku MakiAbstract:BACKGROUND & AIMS: Tissue Transglutaminase has been reported to be the target for endomysial antibodies in celiac disease. We sought to establish whether immunoglobulin (Ig) A class tissue Transglutaminase autoantibodies can be considered specific for celiac disease. METHODS: Serum samples from 136 patients with untreated celiac disease (diagnosed according to the criteria of the European Society for Pediatric Gastroenterology, Hepatology and Nutrition) and 207 disease controls were studied. Enzyme-linked immunosorbent assay (ELISA) and Western blots were performed using calcium-treated and untreated tissue Transglutaminase as antigen. Reticulin, endomysial, and mouse monoclonal tissue Transglutaminase antibodies were studied by an indirect immunofluorescence method and gliadin antibodies with ELISA. RESULTS: The calcium-activated tissue Transglutaminase autoantibody ELISA was highly sensitive (129 of 136) and specific (194 of 207) in detecting celiac disease. The new autoantibody ELISA test correlated well with the endomysial antibody test. Tissue Transglutaminase autoantibody ELISA showed a clearly better predictive potential than the IgA class gliadin antibody ELISA. Immunoblots and ELISA blocking studies showed that calcium is needed for the specific antigen-antibody reaction to occur. Double immunofluorescence staining in human umbilical cord with sera from patients with celiac disease and with monoclonal tissue Transglutaminase antibodies showed complete overlap. CONCLUSIONS: Calcium-activated tissue Transglutaminase autoantibody ELISA is highly accurate in detecting untreated celiac disease. Tissue Transglutaminase seems to be the target self-antigen for endomysial antibodies.
-
tissue Transglutaminase autoantibody enzyme linked immunosorbent assay in detecting celiac disease
Gastroenterology, 1998Co-Authors: S Sulkanen, Tuula Halttunen, Kaija Laurila, Ilma Rita Korponayszabo, Annikki Sarnesto, Pekka Collin, Kaija-leena Kolho, Erkki Savilahti, Markku MakiAbstract:Abstract Background & Aims: Tissue Transglutaminase has been reported to be the target for endomysial antibodies in celiac disease. We sought to establish whether immunoglobulin (Ig) A class tissue Transglutaminase autoantibodies can be considered specific for celiac disease. Methods: Serum samples from 136 patients with untreated celiac disease (diagnosed according to the criteria of the European Society for Pediatric Gastroenterology, Hepatology and Nutrition) and 207 disease controls were studied. Enzyme-linked immunosorbent assay (ELISA) and Western blots were performed using calcium-treated and untreated tissue Transglutaminase as antigen. Reticulin, endomysial, and mouse monoclonal tissue Transglutaminase antibodies were studied by an indirect immunofluorescence method and gliadin antibodies with ELISA. Results: The calcium-activated tissue Transglutaminase autoantibody ELISA was highly sensitive (129 of 136) and specific (194 of 207) in detecting celiac disease. The new autoantibody ELISA test correlated well with the endomysial antibody test. Tissue Transglutaminase autoantibody ELISA showed a clearly better predictive potential than the IgA class gliadin antibody ELISA. Immunoblots and ELISA blocking studies showed that calcium is needed for the specific antigen-antibody reaction to occur. Double immunofluorescence staining in human umbilical cord with sera from patients with celiac disease and with monoclonal tissue Transglutaminase antibodies showed complete overlap. Conclusions: Calcium-activated tissue Transglutaminase autoantibody ELISA is highly accurate in detecting untreated celiac disease. Tissue Transglutaminase seems to be the target self-antigen for endomysial antibodies. GASTROENTEROLOGY 1998;115:1322-1328
-
tissue Transglutaminase autoantibody enzyme linked immunosorbent assay in detecting celiac disease
Gastroenterology, 1998Co-Authors: S Sulkanen, Tuula Halttunen, Kaija Laurila, Ilma Rita Korponayszabo, Annikki Sarnesto, Pekka Collin, Kaija-leena Kolho, Erkki Savilahti, Markku MakiAbstract:BACKGROUND & AIMS: Tissue Transglutaminase has been reported to be the target for endomysial antibodies in celiac disease. We sought to establish whether immunoglobulin (Ig) A class tissue Transglutaminase autoantibodies can be considered specific for celiac disease. METHODS: Serum samples from 136 patients with untreated celiac disease (diagnosed according to the criteria of the European Society for Pediatric Gastroenterology, Hepatology and Nutrition) and 207 disease controls were studied. Enzyme-linked immunosorbent assay (ELISA) and Western blots were performed using calcium-treated and untreated tissue Transglutaminase as antigen. Reticulin, endomysial, and mouse monoclonal tissue Transglutaminase antibodies were studied by an indirect immunofluorescence method and gliadin antibodies with ELISA. RESULTS: The calcium-activated tissue Transglutaminase autoantibody ELISA was highly sensitive (129 of 136) and specific (194 of 207) in detecting celiac disease. The new autoantibody ELISA test correlated well with the endomysial antibody test. Tissue Transglutaminase autoantibody ELISA showed a clearly better predictive potential than the IgA class gliadin antibody ELISA. Immunoblots and ELISA blocking studies showed that calcium is needed for the specific antigen-antibody reaction to occur. Double immunofluorescence staining in human umbilical cord with sera from patients with celiac disease and with monoclonal tissue Transglutaminase antibodies showed complete overlap. CONCLUSIONS: Calcium-activated tissue Transglutaminase autoantibody ELISA is highly accurate in detecting untreated celiac disease. Tissue Transglutaminase seems to be the target self-antigen for endomysial antibodies.
Richard J. Lock - One of the best experts on this subject based on the ideXlab platform.
-
anti tissue Transglutaminase anti endomysium and anti r1 reticulin autoantibodies the antibody trinity of coeliac disease
Clinical and Experimental Immunology, 1999Co-Authors: Richard J. Lock, J E M Gilmour, David J UnsworthAbstract:Anti-tissue Transglutaminase has been recently described as the predominant autoantigen in coeliac disease. We purified serum anti-tissue Transglutaminase antibodies from three patients with coeliac disease by column chromatography and eluted tissue section-bound R1-anti-reticulin antibodies from sections of rat tissue for two of these. Lastly, we generated seven mouse MoAbs to guinea pig tissue Transglutaminase. Each preparation was examined for anti-tissue Transglutaminase, anti-endomysium, anti-R1 reticulin and anti-gliadin antibodies. Column-purified patient antibodies and 2/7 mouse MoAbs gave characteristic anti-endomysium/anti-R1 reticulin reactivity on rat, monkey and human tissue. All positive sera gave indistinguishable patterns of immunofluorescence on rat liver, kidney and stomach, monkey oesophagus, and human umbilical cord. Anti-R1-reticulin eluted from sections showed anti-tissue Transglutaminase reactivity in 2/2 cases, but 0/2 showed anti-gliadin reactivity. In both, tissue section-eluted anti-R1 reticulin gave endomysial staining on monkey oesophagus. None of the mouse monoclonals, or any of the purified patient's anti-tissue Transglutaminase or anti-R1-reticulin antibody showed any reactivity with gliadin. These data confirm tissue Transglutaminase as the predominant autoantigen in coeliac disease and suggest that both anti-endomysium and anti-R1 reticulin reactivities seen in coeliac disease arise due to an immune response to tissue Transglutaminase. Rigorous immunoabsorption was sufficient to abrogate reactivity in the tissue Transglutaminase ELISA, but failed to completely absorb anti-endomysium and anti-reticulin activity. The possibility remains that some of the anti-endomysium and anti-reticulin activity was directed against antigens other than tissue Transglutaminase.
-
anti tissue Transglutaminase anti endomysium and anti r1 reticulin autoantibodies the antibody trinity of coeliac disease
Clinical and Experimental Immunology, 1999Co-Authors: Richard J. Lock, J E M Gilmour, David J UnsworthAbstract:Anti-tissue Transglutaminase has been recently described as the predominant autoantigen in coeliac disease. We purified serum anti-tissue Transglutaminase antibodies from three patients with coeliac disease by column chromatography and eluted tissue section-bound R1-anti-reticulin antibodies from sections of rat tissue for two of these. Lastly, we generated seven mouse MoAbs to guinea pig tissue Transglutaminase. Each preparation was examined for anti-tissue Transglutaminase, anti-endomysium, anti-R1 reticulin and anti-gliadin antibodies. Column-purified patient antibodies and 2/7 mouse MoAbs gave characteristic anti-endomysium/anti-R1 reticulin reactivity on rat, monkey and human tissue. All positive sera gave indistinguishable patterns of immunofluorescence on rat liver, kidney and stomach, monkey oesophagus, and human umbilical cord. Anti-R1-reticulin eluted from sections showed anti-tissue Transglutaminase reactivity in 2/2 cases, but 0/2 showed anti-gliadin reactivity. In both, tissue section-eluted anti-R1 reticulin gave endomysial staining on monkey oesophagus. None of the mouse monoclonals, or any of the purified patient's anti-tissue Transglutaminase or anti-R1-reticulin antibody showed any reactivity with gliadin. These data confirm tissue Transglutaminase as the predominant autoantigen in coeliac disease and suggest that both anti-endomysium and anti-R1 reticulin reactivities seen in coeliac disease arise due to an immune response to tissue Transglutaminase. Rigorous immunoabsorption was sufficient to abrogate reactivity in the tissue Transglutaminase ELISA, but failed to completely absorb anti-endomysium and anti-reticulin activity. The possibility remains that some of the anti-endomysium and anti-reticulin activity was directed against antigens other than tissue Transglutaminase.
