Elsevier

Life Sciences

Volume 59, Issue 23, 1 November 1996, Pages 1951-1960
Life Sciences

Hydrophobic interactions between gliadin and proteins and celiac disease

https://doi.org/10.1016/S0024-3205(96)00546-2Get rights and content

Abstract

Gliadin-protein interaction and its relationship to the pathogenesis hypotheses of celiac disease was investigated. Wheat germ agglutinin was not immunodetected in gliadin preparations. Peptic-tryptic gliadin digest was used to study the gliadin-protein interactions by crossed immunoelectrophoresis and affinity blotting. Biotinylated gliadin digest interacted with IgG and bovine serum albumin but not with several glycoproteins. Since albumin and IgG light chains are not glycosylated, this interaction is not lectin-like, neither completely immunological because of recognition of the IgG Fc fraction. Immobilized and boiled IgG was not recognized by gliadin digest as a lectin. Gliadin digest fractions from T-gel chromatography reduced the fluorescence intensity of cis-parinaric acid bound to albumin. The gliadin-protein interaction is not lectin-like or completely immunological but hydrophobic. Hydrophobicity of gliadins may contribute to the pathogenic events that result in celiac disease.

References (31)

  • M.N. Marsh

    Gastroenterol.

    (1992)
  • H.A. Gjertsen et al.

    Human Immunol.

    (1994)
  • J.P. Michalski et al.

    Am. J. Med. Sci.

    (1994)
  • P. Juto et al.

    Lancet

    (1994)
  • S. Auricchio et al.

    Gastroenterol.

    (1990)
  • M. De Vincenzi et al.

    Toxicol.

    (1995)
  • E. Köttgen et al.

    Biochem. Biophys. Res. Comm.

    (1982)
  • L. Faye et al.

    Anal. Biochem.

    (1985)
  • A. Lihme et al.

    Anal. Biochem.

    (1991)
  • A. Kato et al.

    Biochim. Biophys. Acta.

    (1980)
  • I. Bjarnason et al.

    Lancet

    (1983)
  • J. Rühlmann et al.

    Biochim. Biophys. Acta

    (1993)
  • J.A. Walker-Smith et al.

    Arch. Dis. Child.

    (1990)
  • P.D. Howdle et al.

    Gut.

    (1992)
  • A. Franco et al.

    Clin. Immunol. Immunopathol.

    (1994)
  • Cited by (8)

    • Modification of gluten by methionine binding to prepare wheat bread with reduced reactivity to serum IgA of celiac disease patients

      2010, Journal of Cereal Science
      Citation Excerpt :

      Bound methionine was calculated from the difference between free alpha-amino groups in enzyme catalyzed reactions and control reactions. Gluten proteins and modified gluten proteins were digested in vitro as previously (Calderón de la Barca et al., 1996). Peptic–tryptic digestion was sequentially carried out for 2 h at 37 °C for each enzyme (pepsin and trypsin, ratio 1:100 enzyme:substrate).

    View all citing articles on Scopus
    View full text