12
Views
2
CrossRef citations to date
0
Altmetric
Original Article

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

, &
Pages 240-246 | Received 08 May 1995, Accepted 14 Aug 1995, Published online: 08 Jul 2009

References

  • Trier JS. Celiac sprue. N Engl J Med 1991; 325: 1709–19
  • 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
  • Frazer AC, Fletcher RF, Ross CAC. Gluten induced enteropathy: the effect of partially digested gluten. Lancet 1957; 2: 252–5
  • Wieser H, Belitz HD, Ashkenazi A. Isolation of coeliac active peptide fractions from gliadin. Z Lebensm Unters Forsch 1983; 176: 85–94
  • 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
  • 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
  • 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
  • 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
  • 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
  • Bruce G, Woodley JF, Swan CHJ. Breakdown of gliadin peptides by intestinal brush borders from coeliac patients. Gut 1984; 25: 919–24
  • 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
  • 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
  • Cornell HJ, Mothes T. The activity of wheat gliadin peptides in in vitro assays for coeliac disease. Biochim Biophys Acta 1993; 1181: 169–73
  • Wieser H, Belitz HD. Coeliac active peptides from gliadin: large scale preparation and characterization. Z. Lebensm Unters Forsch 1992; 194: 229–34
  • 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
  • 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
  • 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
  • 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
  • Mercier J-C, Grosclaude F, Ribadeau-Dumas B. The primary structure of bovine α1-casein. Eur J Biochem 1971; 23: 41–51
  • 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
  • Trier JS, Browning TH. Organ culture methods in the study of gastrointestinal mucosal function and development. N Engl J Med 1970; 283: 1245–50
  • 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
  • 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
  • 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
  • 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
  • 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
  • Cornell HJ. Mucosal digestion studies of whole gliadin fractions in coeliac disease. Ann Clin Biochem 1990; 27: 44–9
  • 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
  • Tighe MR, Ciclitira PJ. The implications of recent advances in coeliac disease. Acta Paediatr 1993; 82: 805–10
  • 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
  • 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
  • Sturgess R, Day P, Ellis HJ, Lundin KEA, Gjertsen HA, Kontakou M. Wheat peptide challenge in coeliac disease. Lancet 1994; 343: 758–61
  • 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
  • Sollid LM, Thorsby E. HLA susceptibility genes in celiac disease: Genetic mapping and role in pathogenesis. Gastroenterology 1993; 105: 910–22
  • 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
  • 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
  • Hoyne GF, Callow MG, Kuo M-C, Thomas WR. Presentation of peptides and proteins by intestinal epithelial cells. Immunology 1993; 80: 204–8

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.