The Experts below are selected from a list of 10377 Experts worldwide ranked by ideXlab platform
D 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, D 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, D 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.
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, D 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, D 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.
J E M Gilmour - 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, D 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, D 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.
Peter J. A. Davies - One of the best experts on this subject based on the ideXlab platform.
-
Expression of Tissue Transglutaminase in the developing chicken limb is associated both with apoptosis and endochondral ossification.
Cell Death & Differentiation, 1999Co-Authors: Vilmos A. Thomazy, Peter J. A. DaviesAbstract:The cross-linking enzyme Tissue Transglutaminase (tTG) participates in a variety of cellular functions. To assess its contribution to extracellular and intracellular processes during development we cloned the cDNA for chicken heart Tissue Transglutaminase and localized the sites of Transglutaminase expression by in situ hybridization and immunohistochemistry. Compared with the chicken red blood cell Transglutaminase cDNA, the heart cDNA encodes a Transglutaminase with an amino-terminal truncation. The truncated enzyme retains full catalytic activity and is GTP-inhibitable. Tissue Transglutaminase expression was observed in developmentally transient structures in embryonic chicken limb at day 7.5 of incubation suggesting that its expression is dynamically regulated during limb morphogenesis. The major morphogenetic events of the limb associated with Transglutaminase expression were cartilage maturation during skeletal development, interdigital apoptosis, and differentiation of skeletal muscle. Maturation of the cartilage during endochondral ossification was characterized by intra- and extracellular Transglutaminase accumulation in the zone of hypertrophic chondrocytes. Only intracellular enzyme could be detected in mesenchymal cells of the prospective joints, in apoptotic cells of the interdigital web, and in skeletal muscle myoblasts. An apparently constitutive expression of Tissue Transglutaminase was found in vascular endothelial cells corresponding to the adult expression pattern. The dynamic pattern of Transglutaminase expression during morphogenesis suggests that Tissue remodeling is a major trigger for Transglutaminase induction.
-
TNF-α modulates expression of the Tissue Transglutaminase gene in liver cells
American Journal of Physiology-gastrointestinal and Liver Physiology, 1998Co-Authors: Gerald S. Kuncio, Peter J. A. Davies, Vilmos A. Thomazy, Mariya Tsyganskaya, Laszlo Nagy, Mark A. ZernAbstract:One of several postulated roles for Tissue Transglutaminase (tTG) is the stabilization and assembly of extracellular matrix via peptide cross-linking. We previously determined that tTG activity inc...
-
Lack of induction of Tissue Transglutaminase but activation of the preexisting enzyme in c-Myc-induced apoptosis of CHO cells.
Biochemical and Biophysical Research Communications, 1997Co-Authors: Zoltán Balajthy, Laszlo Nagy, Peter J. A. Davies, Noemi Kedei, László FésüsAbstract:Abstract The intracellular activity and expression of Tissue Transglutaminase, which crosslinks proteins through ϵ(γ-glutamyl)lysine isodipeptide bond, was investigated in CHO cells and those stably transfected with either inducible c-Myc (which leads to apoptosis) or with c-myc and the apoptosis inhibitor Bcl-2. Protein-bound cross-link content was significantly higher when apoptosis was induced by c-Myc while the concomitant presence of Bcl-2 markedly reduced both apoptosis and enzymatic protein cross-linking. The expression of Tissue Transglutaminase did not change following the initiation of apoptosis by c-Myc or when it was blocked by Bcl-2. Studying transiently co-transfected elements of the mouse Tissue Transglutaminase promoter linked to a reporter enzyme revealed their overall repression in cells expressing c-Myc. This repression was partially suspended in cells also carrying Bcl-2. Our data suggest that Tissue Transglutaminase is not induced when c-Myc initiates apoptosis but the pre-existing endogenous enzyme is activated.
-
Regulation of the expression of the Tissue Transglutaminase gene by DNA methylation
Proceedings of the National Academy of Sciences of the United States of America, 1997Co-Authors: Shan Lu, Peter J. A. DaviesAbstract:We have investigated the role of DNA methylation in the regulation of the expression of the human Tissue Transglutaminase gene. Studies on the methylation of the Transglutaminase promoter in normal and neoplastic human cells demonstrated that the promoter is methylated in vivo and hypomethylation of the promoter is correlated with constitutive gene expression. Demethylation of the promoter in vivo by treatment of the cells with 5-azacytidine increased Transglutaminase expression and hypermethylation of the promoter in vitro suppressed its activity. These studies suggest that alternations in DNA methylation may be one of the mechanisms regulating the Tissue-specific expression of the Tissue Transglutaminase gene.
-
Isolation and Characterization of the Human Tissue Transglutaminase Gene Promoter
Journal of Biological Chemistry, 1995Co-Authors: Shan Lu, Margaret Saydak, Vittorio Gentile, Joseph P. Stein, Peter J. A. DaviesAbstract:Abstract Tissue Transglutaminase belongs to a family of calcium-dependent enzymes, the Transglutaminases that catalyze the covalent cross-linking of specific proteins by the formation of (-glutamyl)lysine isopeptide bonds. The goal of this study has been the isolation and characterization of the human Tissue Transglutaminase gene promoter. Genomic DNA clones, spanning the 5′ region of the gene, were isolated and the structure of the 5′-end of the human Tissue Transglutaminase gene was determined. 1.74 kilobases of flanking DNA were sequenced and were found to contain a TATA box element (TATAA), a CAAT box element (GGACAAT), a series of potential transcription factor-binding sites (AP1, SP1, interleukin-6 response element), and a glucocorticoid response elements. Transient transfection experiments showed that this DNA fragment included a functional promoter, which is constitutively active in multiple cell types.
Alessandro Ventura - One of the best experts on this subject based on the ideXlab platform.
-
role of human Tissue Transglutaminase igg and anti gliadin igg antibodies in the diagnosis of coeliac disease in patients with selective immunoglobulin a deficiency
Digestive and Liver Disease, 2004Co-Authors: A Lenhardt, Vincenzo Villanacci, Alessandro Plebani, F Marchetti, T Gerarduzzi, A Meini, Stefano Martelossi, Alessandro VenturaAbstract:Abstract Background. Selective IgA deficiency is associated with coeliac disease, and studies have shown an increased prevalence of coeliac disease in these patients ranging from 0.71 to 30.7%, depending on the test used for screening. Aims. To determine the sensitivity of IgG anti-gliadin-antibodies and of IgG human-Tissue-Transglutaminase for diagnosing coeliac disease and assessing its prevalence in subjects with IgA deficiency. Subjects. We tested serum samples from 126 IgA-deficient children (66 female, median age: 10.8 years). Methods. All samples were analysed to measure IgG anti-gliadin-antibodies and IgG anti-human-Tissue-Transglutaminase. Patients testing positive to either test underwent intestinal biopsy. Subjects testing positive for IgG anti-human-Tissue-Transglutaminase underwent genetic testing for the human leucocyte antigen heterodimer. Results. Twenty-seven of 126 subjects tested positive for IgG anti-gliadin-antibodies (five of whom tested positive also for IgG anti-human-Tissue-Transglutaminase) and 18 (including the aforementioned five) for IgG anti-human-Tissue-Transglutaminase. Intestinal biopsy was performed in 37 of the 40 patients who tested positive (three subjects refused). Eleven had positive intestinal biopsies all of whom tested positive for IgG anti-human-Tissue-Transglutaminase, but only five of these tested positive also for IgG anti-gliadin-antibodies. All 22 patients testing positive for anti-gliadin-antibody alone had normal intestinal mucosa. All the patients who tested positive for IgG anti-human-Tissue-Transglutaminase and underwent genetic screening (15/18) had the coeliac-related human leucocyte antigen. Overall, coeliac disease was diagnosed in 11 of the 126 subjects with IgA deficiency (8.7%). Conclusions. The prevalence of coeliac disease in subjects with total IgA deficiency was 8.7%. Assay of IgG anti-human-Tissue-Transglutaminase can be recommended for screening coeliac disease in IgA-deficient subjects.
-
human recombinant Tissue Transglutaminase elisa an innovative diagnostic assay for celiac disease
The American Journal of Gastroenterology, 2000Co-Authors: Daniele Sblattero, Irene Berti, C Trevisiol, Roberto Marzari, Alberto Tommasini, Andrew Bradbury, Alessio Fasano, Alessandro VenturaAbstract:OBJECTIVE: Tissue Transglutaminase is the autoantigen recognized by the sera of celiac patients. An enzyme-linked immunosorbent assay (ELISA) based on guinea-pig Tissue Transglutaminase was recently used to measure serum Tissue Transglutaminase antibodies for the diagnosis of celiac disease. We determine the sensitivity and specificity of an ELISA test based on the use of human recombinant Transglutaminase, compared with the guinea pig Transglutaminase ELISA and IgA antiendomysium antibodies. METHODS: Serum samples were tested from 65 patients with intestinal biopsy proven celiac disease, from 10 patients with Crohn's disease, and from 150 healthy blood donors. RESULTS: Human Transglutaminase ELISA identified 64 of 65 celiac patients, whereas the guinea pig Transglutaminase ELISA and IgA antiendomysium antibodies identified 58 of 65 and 60 of 65 subjects, respectively. The three tests showed comparable specificity. CONCLUSIONS: These results proved that the human Tissue Transglutaminase-based ELISA represents a cost-effective strategy for identifying both symptomatic and atypical forms of celiac disease and could mean that intestinal biopsy need no longer be the gold standard for diagnosing this clinical condition. Furthermore, early identification and treatment of patients with celiac disease in an outpatient setting could have significant implications for reducing long-term morbidity and can produce major savings in future health care costs.