In vitro Hydrolysis of Gliadin and Casein Peptides: Secondary Defect in Coeliac Disease Shown by Organ Culture

References

• Trier JS. Celiac sprue. N Engl J Med 1991; 325: 1709–19
   PubMed Web of Science ®Google Scholar
• Marsh MN. Gluten, major histocompatibility complex, and the small intestine. A molecular and immunobiologic approach to the spectrum of gluten sensitivity (‘celiac sprue’). Gastroenterology 1992; 102: 330–54
   PubMed Web of Science ®Google Scholar
• Frazer AC, Fletcher RF, Ross CAC. Gluten induced enteropathy: the effect of partially digested gluten. Lancet 1957; 2: 252–5
   Google Scholar
• Wieser H, Belitz HD, Ashkenazi A. Isolation of coeliac active peptide fractions from gliadin. Z Lebensm Unters Forsch 1983; 176: 85–94
   PubMedGoogle Scholar
• Falchuk ZM, Gebhard RL, Sessoms C. An in vitro model of gluten-sensitive enteropathy: effect of gliadin on intestinal epithelial cells of patients with gluten-sensitive enteropathy in organ culture. J Clin Invest 1974; 53: 487–500
   PubMed Web of Science ®Google Scholar
• Jos J, Lenoir G, De Ritis G. In vitro pathogenetic studies of coeliac disease. Effects of protein digests on coeliac intestinal biopsy specimen maintained in organ culture. Scand J Gastroenterol 1975; 10: 121–8
   PubMed Web of Science ®Google Scholar
• Fluge Ø, Sletten K, Fluge G, Aksnes L, Elsayed S. In vitro toxicity of purified gluten peptides tested by organ culture. J Pediatr Gastroenterol Nutr 1994; 18: 186–92
   PubMedGoogle Scholar
• Stallmach A. In-vitro Wirkungen von Gliadinfraktionen in der intestinalen Organkultur. Untersuchungen zur Enterotoxizität und Immunogenität von Gliadinpartialhydrolysaten in der. Pathogenese der Zöliakie [thesis]. Hamburg 1985
   Google Scholar
• Douglas AP, Booth CC. Digestion of gluten peptides by normal human jejunal mucosa and by mucosa from patients with adult coeliac disease. Clin Sci 1970; 38: 11–25
   PubMedGoogle Scholar
• Bruce G, Woodley JF, Swan CHJ. Breakdown of gliadin peptides by intestinal brush borders from coeliac patients. Gut 1984; 25: 919–24
   PubMedGoogle Scholar
• Cornell HJ. Amino acid composition of peptides remaining after in vitro digestion of a gliadin subfraction with duodenal mucosa from patients with coeliac disease. Clin Chim Acta 1988; 176: 279–90
   PubMed Web of Science ®Google Scholar
• Cornell HJ, Auricchio RS, De Ritis G, De Vincenzi M, Maiuri L, Raia V. Intestinal mucosa of celiacs in remission is unable to abolish toxicity of gliadin peptides on in vitro developing fetal rat intestine and cultured atrophic celiac mucosa. Pediatr Res 1988; 24: 233–7
   PubMed Web of Science ®Google Scholar
• Cornell HJ, Mothes T. The activity of wheat gliadin peptides in in vitro assays for coeliac disease. Biochim Biophys Acta 1993; 1181: 169–73
   PubMedGoogle Scholar
• Wieser H, Belitz HD. Coeliac active peptides from gliadin: large scale preparation and characterization. Z. Lebensm Unters Forsch 1992; 194: 229–34
   PubMedGoogle Scholar
• Walker-Smith JA, Guandalini S, Schmitz J, Shmerling BH, Visakorpi JK. Revised criteria for diagnosis of coeliac disease. Arch Dis Child 1990; 65: 909–11
   PubMed Web of Science ®Google Scholar
• Savilahti E, Heyman M, MacDonald T, Navarro J, Stern M, Strobel S. Diagnostic criteria for food allergy with predominantly intestinal symptoms. J Pediatr Gastroenterol Nutr 1992; 14: 108–12
   PubMedGoogle Scholar
• Wieser H, Mödl A, Seilmeier W, Belitz HD. High-performance liquid chromatography of gliadins from different wheat varieties: amino acid composition and N-terminal amino acid sequence of components. Z Lebensm Unters Forsch 1987; 185: 371–8
   Google Scholar
• Kasarda DD. Toxic cereal grains in coeliac disease. Gastrointestinal immunology and gluten-sensitive disease, C Feighery, C O'Farrelly. Oak Tree Press, Dublin 1994; 203–20
   Google Scholar
• Mercier J-C, Grosclaude F, Ribadeau-Dumas B. The primary structure of bovine α1-casein. Eur J Biochem 1971; 23: 41–51
   PubMedGoogle Scholar
• Stallmach A, Belitz HD, Gellermann B, Schäfer H, Wieser H, Stern M. Effects of gliadin peptides B1-B4 in celiac disease. I. Organ culture studies. J Pediatr Gastroenterol Nutr 1987; 6: 335–40
   PubMedGoogle Scholar
• Trier JS, Browning TH. Organ culture methods in the study of gastrointestinal mucosal function and development. N Engl J Med 1970; 283: 1245–50
   PubMed Web of Science ®Google Scholar
• Bramble MG, Watson AJ, Record CD. The effect of the topical steroid clobetasone butyrate on coeliac mucosa maintained in organ culture. Digestion 1981; 21: 316–24
   PubMedGoogle Scholar
• Howdle PD, Corazza GR, Bullen AW, Losowsky MS. Gluten sensitivity of small intestinal mucosa in vitro: Quantitative assessment of histologic change. Gastroenterology 1981; 80: 442–50
   PubMed Web of Science ®Google Scholar
• Fluge G, Aksnes L. Morphological and morphometric assessment of human duodenal biopsies maintained in organ culture. In vitro influence of coeliac disease. Scand J Gastroenterol 1981; 16: 555–7
   PubMed Web of Science ®Google Scholar
• Howdle PD, Corazza GR, Bullen AV, Losowsky MS. Gluten sensitivity of small intestinal mucosa in vitro: quantitative assessment of histologic change. Gastroenterology 1981; 80: 442–50
   PubMed Web of Science ®Google Scholar
• De Ritis G, Auricchio RS, Jones HW, Lew EJ-L, Bernardin JE, Kasarda DD. In vitro (organ culture) studies of the toxicity of specific A-gliadin peptides in celiac disease. Gastroenterology 1988; 94: 41–9
   PubMed Web of Science ®Google Scholar
• Cornell HJ. Mucosal digestion studies of whole gliadin fractions in coeliac disease. Ann Clin Biochem 1990; 27: 44–9
   PubMed Web of Science ®Google Scholar
• Cornell HJ, Wieser H, Belitz HD. Characterization of the gliadin derived peptides which are biologically active in coeliac disease. Clin Chim Acta 1992; 213: 37–50
   PubMedGoogle Scholar
• Tighe MR, Ciclitira PJ. The implications of recent advances in coeliac disease. Acta Paediatr 1993; 82: 805–10
   PubMedGoogle Scholar
• Mantzaris G, Jewell DP. In vivo toxicity of a synthetic dodecapeptide from A gliadin in patients with coeliac disease. Scand J Gastroenterol 1991; 26: 392–8
   PubMed Web of Science ®Google Scholar
• Ellis HJ, Doyle EA, Sturgess R, Ciclitira P. Coeliac disease: characterization of monoclonal antibodies raised against a synthetic peptide corresponding to amino acid residues 206–217 of A-gliadin. Gut 1992; 33: 1504–7
   PubMedGoogle Scholar
• Sturgess R, Day P, Ellis HJ, Lundin KEA, Gjertsen HA, Kontakou M. Wheat peptide challenge in coeliac disease. Lancet 1994; 343: 758–61
   PubMed Web of Science ®Google Scholar
• Rühlmann J, Sinha P, Hansen G, Tauber R, Köttgen E. Studies on the aetiology of coeliac disease: No evidence for lectin-like components in wheat gluten. Biochem Biophys Acta 1993; 1181: 249–56
   PubMedGoogle Scholar
• Sollid LM, Thorsby E. HLA susceptibility genes in celiac disease: Genetic mapping and role in pathogenesis. Gastroenterology 1993; 105: 910–22
   PubMed Web of Science ®Google Scholar
• Lundin KEA, Scott H, Hansen T, Paulsen G, Halstensen TS, Fausa O. Gliadin-specific, HLA-DQ (α1*0501,β1*0201) restricted T cells isolated from the small intestinal mucosa of celiac disease patients. J Exp Med 1993; 178: 187–96
   PubMed Web of Science ®Google Scholar
• Gjertsen HA, Lundin KEA, Sollid LM, Eriksen JA, Thorsby E. T cells recognize a peptide derived from α-gliadin presented by the celiac disease-associated HLA-DQ (α1*0501 β1*0201) heterodimer. Hum Immunol 1994; 39: 243–52
   PubMed Web of Science ®Google Scholar
• Hoyne GF, Callow MG, Kuo M-C, Thomas WR. Presentation of peptides and proteins by intestinal epithelial cells. Immunology 1993; 80: 204–8
   PubMedGoogle Scholar