Role of Tissue Transglutaminase in Gliadin Binding to Reticular Extracellular Matrix and Relation to Coeliac Disease Autoantibodies

References

• Mäki M. The humoral immune system in coeliac disease. Baillere's Clin. Gastroenterol. 1995; 9: 231–249
   PubMed Web of Science ®Google Scholar
• Seah P. P., Fry L., Hoffbrand A. V., Holborow E. J. Tissue antibodies in dermatitis herpetiformis and adult coeliac disease. Lancet 1971; ii: 834–836
   Google Scholar
• Chorzelski T., Beutner E. H., Sulej J., Tchorzewska H., Jablonska S., Kumar V., Kapuscinska A. IgA antiendomysium antibody. A new immunologic marker of dermatitis heretiformis and coeliac disease. Br. J. Dermatol. 1984; 111: 395–402
   PubMed Web of Science ®Google Scholar
• Mäki M., Hällström O., Martinen A. Reaction of human non-collagenous polypeptides with coeliac disease autoantibodies. Lancet 1991; 338: 724–725
   PubMed Web of Science ®Google Scholar
• Martinen A., Mäki M. Purification of fibroblast-derived celiac disease autoantigen molecules. Pediatr. Res. 1993; 34: 420–423
   PubMed Web of Science ®Google Scholar
• Börner H., Ostnan A. A., Meergans T., Weiske T., Mothes T. Isolation of antigens recognized by coeliac disease autoantibodies and their use in enzyme immunoassay of endomysium and reticulin antibody-positive human sera. Clin. Exp. Immunol. 1996; 106: 344–350
   PubMed Web of Science ®Google Scholar
• Dietench W., Ehnis T., Bauer M., Donner P., Volta U., Riecken E. O., Schuppan D. Identification of tissue transglutaminase as the autoantigen of coeliac disease. Nature Med. 1997; 3: 797–801
   PubMed Web of Science ®Google Scholar
• Unsworth D. J., Johnson G. D., Haffenden G., Fry L., Holborow E. J. Binding of wheat gliadin in vitro to reticulin in normal and dermatitis herpetiformis skin. J. Invest. Dermatol. 1981; 76: 88–93
   PubMed Web of Science ®Google Scholar
• Unsworth D. J., Walker-Smith J. A., McCarthy D., Holborow E. J. Studies on the significance of the R1 antireticulin antibody associated with gluten sensitivity. Int. Arch. Allergy Apll. Immunol. 1985; 76: 47–51
   Web of Science ®Google Scholar
• Beutner E. H., Chorzelski T. P., Kumar V., Leonhard J., Krasny S. Sensitivity and specificity of IgA-class antiendomysial antibodies for dermatitis herpetiformis and findings relevant to their pathogenic significance. J. American Academy Dennatol. 1986; 15: 464–473
   PubMed Web of Science ®Google Scholar
• Unsworth D. J., Leonard J. N., Hobday C. M., Griffiths C. E. M., Powles A. V., Haffenden G., Fry L. Gliadins bind to reticulin in a lectin-like manner. Arch. Dermatol. Res. 1987; 279: 232–235
   PubMed Web of Science ®Google Scholar
• Beutner E. H., Chorzelski T. P., Kumar V., Valeski J. E., Rossi T. Role of autoimmunity in gluten sensitive enteropathy. Serologic Diagnosis of Celiac Disease, T. P. Chorzelski, E. H. Beutner, V. Kumar, T. K. Zalewski. CRC Press, Boca Raton, FL 1990; 143–164
   Google Scholar
• Walker-Smith J. A., Guandalini S., Schmitz J., Shmerling D. H., Visakorpi J. K. Revised criteria for diagnosis of coeliac disease. Arch. Dis. Child. 1990; 65: 909–911
   PubMed Web of Science ®Google Scholar
• Ostnan A. A. Thesis, University of Leipzig. 1992
   Google Scholar
• Laurie G. W., Ciclitira P. J., Ellis H. J., Pogany G. Immunological and partial sequence identity of mouse BM180 with wheat alpha-gliadin. Biochem. Biophys. Res. Commun. 1995; 217: 10–15
   PubMed Web of Science ®Google Scholar
• Karská K., Tuckova L., Steiner L., Tlaskalová-Hogenová H., Micholak M. Calreticulin-the potential autoanligen in celiac disease. Biochim. Biophys. Rex. Commun. 1995; 209: 597–605
   PubMed Web of Science ®Google Scholar
• Farré Castany M. A., Kocna P., Tlaskalová-Hogenová H. Binding of gliadin to lymphoblastoid, myeloid and epithelial cell lines. Folia Microbiol. 1995; 40: 431–435
   PubMed Web of Science ®Google Scholar
• Pittschieler K., Ladinser B., Petell J. K. Reactivity of gliadin and lectins with celiac intestinal mucosa. Pediatr. Res. 1994; 36(5)635–641
   PubMed Web of Science ®Google Scholar
• Bendix U., Lentz S., Rothschild M., Lehmann L., Osman A. A., Mothes T. Effect of 7-interferon on binding of gliadin and other food peptides to the human intestinal cell line HT-29. Clin. Chim. Acta 1997; 261: 69–80
   PubMed Web of Science ®Google Scholar
• Amore A., Emancipator S. N., Roccatello D., Gianoglio B., Peruzzi L., Porcellini M. G., Piccoli G., Coppo R. Functional consequences of the binding of gliadin to cultured mesangial cells: bridging immunoglobin A to cells and modulation of eicosanoid synthesis and altered cytocine production. Am. J. Kidney Dis. 1994; 23: 290–301
   PubMed Web of Science ®Google Scholar
• Gallagher R. B., Feighery C., Weir D. G., Kelly C. P., Whelan C. A. Studies on the interaction between a-gliadin and HLA and T cell receptor molecules in coeliac disease. Clin. Exp. Immunol. 1988; 74: 413–418
   PubMed Web of Science ®Google Scholar
• Verkasalo M. A. Adherence of Gliadin fractions to lymphocytes in coeliac disease. Lancet 1982; 1: 1384–1386
   PubMed Web of Science ®Google Scholar
• Weiser M. M., Douglas A. P. An alternative mechanism for gluten toxicity in coeliac disease. Lancet 1976; 1: 567–569
   PubMed Web of Science ®Google Scholar
• Köttgen E., Volk B., Kluge F., Gerok W. Gluten, a lektin with oligomanosyl specificity and the causative agent of gluten-sensitive enteropathy. Biochem. Biophvs. Res. Comm. 1982; 1119: 168–173
   Google Scholar
• Osman A. A., Braunersreuther I., Mothes T. Investigation of glaidin binding to different selected proteins using a biotin-streptavidin system. Z. Lebensm Unters Forsch 1994; 198: 249–252
   PubMedGoogle Scholar
• Bruce S. E., Bjarnason I., Peters T. J. Human jejunal transglutaminase: demonstration of activity, enzyme kinetics and substrate specificity with special relation to gliadin and coeliac disease. Clin. Sci. 1985; 68: 573–579
   PubMed Web of Science ®Google Scholar
• Folk J. E., Cole P. W. Transglutaminase: mechanistic features of the active site as determined by kinetic and inhibitor studies. Biochim. Biophvs. Acta 1966; 122: 244–264
   PubMed Web of Science ®Google Scholar
• Folk J. E., Cole P. W., Mulloy J. P. Mechanism of action of guinea pig liver transglutaminase: The metaldependent hydrolysis of p-nitrophenyl acetate; further observations on the role of metal in enzyme activation. J. Biol. Chem. 1967; 242: 2615–2621
   PubMed Web of Science ®Google Scholar
• Rubin W., Fauci A. S., Sleisenger M. H., Jeffries G. H. Immunofluorescent studies in adult celiac disease. J. Clin. Invest. 1965; 44: 475–485
   PubMed Web of Science ®Google Scholar
• Unsworth D. J., Holborow E. J. Does the reticulin binding property of cereal proteins demonstrable in vitro have pathogenetic significance for celiac disease?. Gut 1985; 26: 1204–1209
   PubMed Web of Science ®Google Scholar
• Aeschlimann D., Paulsson M. Transglutaminases: Protein cross-linking enzymes and body fluids. Thrombosis Haemostasis 1994; 71: 402–415
   PubMed Web of Science ®Google Scholar
• Unsworth D. J., Scott D. L., Almond T. J., Beard H. K., Holborow E. J., Walton K. W. Failure of Rl type antireticulin antibody to react with fibronectin, collagen type III or the non-collagenous reticulin component (NCRC). Clin. Exp. Immunol. 1984; 57: 609–613
   PubMed Web of Science ®Google Scholar
• Jeong J. M., Murthy S. N., Radek J. T., Lorand L. The fibronectin-binding domain of transglutaminase. J. Biol. Chem. 1995; 270(10)5654–5658
   PubMed Web of Science ®Google Scholar
• Fatenejad S., Craft J. Intrastructural help in diversification of humoral autoimmune responses. Clin. Exp. Immunol. 1996; 106: 1–4
   PubMed Web of Science ®Google Scholar
• Vanderlugt C. J., Miller S. D. Epitope spreading. Curr. Opinion. Immunol 1996; 8: 831–836
   PubMed Web of Science ®Google Scholar