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Original Article

Enzymatic detoxification of gluten by germinating wheat proteases: Implications for new treatment of celiac disease

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Pages 390-400 | Received 02 Oct 2008, Published online: 08 Jul 2009

References

  • Fasano A, Berti I, Gerarduzzi T, Not T, Colletti RB, Drago S, et al. Prevalence of celiac disease in at-risk and not-at-risk groups in the United States: a large multicenter study. Arch Intern Med. 2003; 163: 286–92
  • Bruce G, Woodley JF, Swan CH. Breakdown of gliadin peptides by intestinal brush borders from coeliac patients. Gut. 1984; 25: 919–24
  • Shan L, Molberg O, Parrot I, Hausch F, Filiz F, Gray GM, et al. Structural basis for gluten intolerance in celiac sprue. Science. 2002; 297: 2275–9
  • Garcia-Horsman JA, Venalainen JI, Lohi O, Auriola IS, Korponay-Szabo IR, Kaukinen K, et al. Deficient activity of mammalian prolyl oligopeptidase on the immunoactive peptide digestion in coeliac disease. Scand J Gastroenterol. 2007; 42: 562–71
  • de Ritis G, Auricchio S, Jones HW, Lew EJ, 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
  • Sturgess R, Day P, Ellis HJ, Lundin KE, Gjertsen HA, Kontakou M, et al. Wheat peptide challenge in coeliac disease. Lancet. 1994; 343: 758–61
  • Anderson RP, Degano P, Godkin AJ, Jewell DP, Hill AV. In vivo antigen challenge in celiac disease identifies a single transglutaminase-modified peptide as the dominant A-gliadin T-cell epitope. Nat Med. 2000; 6: 337–42
  • Maiuri L, Ciacci C, Ricciardelli I, Vacca L, Raia V, Auricchio S, et al. Association between innate response to gliadin and activation of pathogenic T cells in coeliac disease. Lancet. 2003; 362: 30–7
  • Sollid LM. Molecular basis of celiac disease. Annu Rev Immunol. 2000; 18: 53–81
  • Bethune MT, Khosla C. Parallels between pathogens and gluten peptides in celiac sprue. PLoS Pathog. 2008; 4: e34
  • Lammers KM, Lu R, Brownley J, Lu B, Gerard C, Thomas K, et al. Gliadin induces an increase in intestinal permeability and zonulin release by binding to the chemokine receptor CXCR3. Gastroenterology. 2008; 135: 194–204.e3
  • Lee A, Newman JM. Celiac diet: its impact on quality of life. J Am Diet Assoc. 2003; 103: 1533–5
  • Xia J, Bergseng E, Fleckenstein B, Siegel M, Kim CY, Khosla C, et al. Cyclic and dimeric gluten peptide analogues inhibiting DQ2-mediated antigen presentation in celiac disease. Bioorg Med Chem. 2007; 15: 6565–73
  • Chaudhary R, Ghosh S. Infliximab in refractory coeliac disease. Eur J Gastroenterol Hepatol. 2005; 17: 603–4
  • Sollid LM, Khosla C. Future therapeutic options for celiac disease. Nat Clin Pract Gastroenterol Hepatol. 2005; 2: 140–7
  • Benahmed M, Meresse B, Arnulf B, Barbe U, Mention JJ, Verkarre V, et al. Inhibition of TGF-beta signaling by IL-15: a new role for IL-15 in the loss of immune homeostasis in celiac disease. Gastroenterology. 2007; 132: 994–1008
  • Maurano F, Siciliano RA, De Giulio B, Luongo D, Mazzeo MF, Troncone R, et al. Intranasal administration of one alpha gliadin can downregulate the immune response to whole gliadin in mice. Scand J Immunol. 2001; 53: 290–5
  • RP Anderson. Development of a vaccine for celiac disease. Frontiers in celiac disease. Pediatric and adolescent medicine. 12. BaselSwitzerland: Karger; 2008.
  • Clemente MG, De Virgiliis S, Kang JS, Macatagney R, Musu MP, Di Pierro MR, et al. Early effects of gliadin on enterocyte intracellular signalling involved in intestinal barrier function. Gut. 2003; 52: 218–23
  • Paterson BM, Lammers KM, Arrieta MC, Fasano A, Meddings JB. The safety, tolerance, pharmacokinetic and pharmacodynamic effects of single doses of AT-1001 in coeliac disease subjects: a proof of concept study. Aliment Pharmacol Ther. 2007; 26: 757–66
  • Hausch F, Halttunen T, Maki M, Khosla C. Design, synthesis, and evaluation of gluten peptide analogs as selective inhibitors of human tissue transglutaminase. Chem Biol. 2003; 10: 225–31
  • Siegel M, Khosla C. Transglutaminase 2 inhibitors and their therapeutic role in disease states. Pharmacol Ther. 2007; 115: 232–45
  • Matysiak-Budnik T, Candalh C, Cellier C, Dugave C, Namane A, Vidal-Martinez T, et al. Limited efficiency of prolyl-endopeptidase in the detoxification of gliadin peptides in celiac disease. Gastroenterology. 2005; 129: 786–96
  • Pyle GG, Paaso B, Anderson BE, Allen DD, Marti T, Li Q, et al. Effect of pretreatment of food gluten with prolyl endopeptidase on gluten-induced malabsorption in celiac sprue. Clin Gastroenterol Hepatol. 2005; 3: 687–94
  • Shan L, Marti T, Sollid LM, Gray GM, Khosla C. Comparative biochemical analysis of three bacterial prolyl endopeptidases: implications for coeliac sprue. Biochem J. 2004; 383: 311–8
  • Gass J, Ehren J, Strohmeier G, Isaacs I, Khosla C. Fermentation, purification, formulation, and pharmacological evaluation of a prolyl endopeptidase from Myxococcus xanthus: implications for celiac sprue therapy. Biotechnol Bioeng. 2005; 92: 674–84
  • Stepniak D, Spaenij-Dekking L, Mitea C, Moester M, de Ru A, Baak-Pablo R, et al. Highly efficient gluten degradation with a newly identified prolyl endoprotease: implications for celiac disease. Am J Physiol Gastrointest Liver Physiol. 2006; 291: G621–9
  • Mitea C, Havenaar R, Drijfhout JW, Edens L, Dekking L, Koning F. Efficient degradation of gluten by a prolyl endoprotease in a gastrointestinal model: implications for coeliac disease. Gut. 2008; 57: 25–32
  • Gass J, Bethune MT, Siegel M, Spencer A, Khosla C. Combination enzyme therapy for gastric digestion of dietary gluten in patients with celiac sprue. Gastroenterology. 2007; 133: 472–80
  • Simpson DJ. Proteolytic degradation of cereal prolamins—the problem with proline. Plant Science. 2001; 161: 825–38
  • Lindfors K, Blomqvist T, Juuti-Uusitalo K, Stenman S, Venalainen J, Maki M, et al. Live probiotic Bifidobacterium lactis bacteria inhibit the toxic effects induced by wheat gliadin in epithelial cell culture. Clin Exp Immunol. 2008; 152: 552–8
  • Barone MV, Gimigliano A, Castoria G, Paolella G, Maurano F, Paparo F, et al. Growth factor-like activity of gliadin, an alimentary protein: implications for coeliac disease. Gut. 2007; 56: 480–8
  • Molberg O, McAdam SN, Korner R, Quarsten H, Kristiansen C, Madsen L, et al. Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease. Nat Med. 1998; 4: 713–7
  • Qiao SW, Bergseng E, Molberg O, Jung G, Fleckenstein B, Sollid LM. Refining the rules of gliadin T cell epitope binding to the disease-associated DQ2 molecule in celiac disease: importance of proline spacing and glutamine deamidation. J Immunol. 2005; 175: 254–61
  • Stenman SM, Lindfors K, Korponay-Szabo IR, Lohi O, Saavalainen P, Partanen J, et al. Secretion of celiac disease autoantibodies after in vitro gliadin challenge is dependent on small-bowel mucosal transglutaminase 2-specific IgA deposits. BMC Immunol. 2008; 9: 6
  • Li N, DeMarco VG, West CM, Neu J. Glutamine supports recovery from loss of transepithelial resistance and increase of permeability induced by media change in Caco-2 cells. J Nutr Biochem. 2003; 14: 401–8
  • Cerf-Bensussan N, Matysiak-Budnik T, Cellier C, Heyman M. Oral proteases: a new approach to managing coeliac disease. Gut. 2007; 56: 157–60
  • Laitila A, Kotaviita E, Peltola P, Home S, Wilhelmson A. Indigenous microbial community of barley greatly influences grain germination and malt quality. J Inst Brew. 2007; 113: 9–20
  • Hartmann G, Koehler P, Wieser H. Rapid degradation of gliadin peptides toxic for celiac disease patients by proteases from germinating cereals. J Cereal Sci. 2006; 44: 368–71
  • Siegel M, Bethune MT, Gass J, Ehren J, Xia J, Johannsen A, et al. Rational design of combination enzyme therapy for celiac sprue. Chem Biol. 2006; 13: 649–58

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