The toxic fraction of gliadin digests in coeliac disease. Isolation by chromatography on Biogel P-10

J, Jos; Charbonnier, L.; Mossé, Jacques; Olives, J. P.; Tand, M.-F. de; J, Rey

doi:10.1016/0009-8981(82)90339-4

Cited by 58 publications

(20 citation statements)

References 11 publications

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“…However, we feel that true cross-reactivity is a more likely explanation of these results in view of their similarity with those of Kag noff et al [14] and also with other studies assessing similarities between gliadins in other ways [9][10][11][12][13].…”

Section: Discussionsupporting

confidence: 85%

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Responses of Antigen-Specific Long-Term Murine T Cell Lines to Wheat Gliadin Fractions

Howdle

Hanson²,

Trejdosiewicz³

et al. 1989

Int Arch Allergy Immunol

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Recent evidence suggests that the four electrophoretically defined gliadin subfractions (α, β, γ and ω) of wheat can induce the typical pathological finding of coeliac disease. We have prepared long-term murine T cell lines to gliadin and its four major subfractions. The cell lines were tested in proliferative assays with each homologous gliadin subfraction, and to the other gliadin subfractions. There was some cross-reactivity, with unfractionated gliadin and its α-subfraction being the most antigenic, while ω-gliadin was the least. These data demonstrate that gliadin components are effective stimuli for specific T cell responses, and further suggest that the α-gliadin subfraction generates the highest specific responses. This accords with observations in man that all four gliadin subfractions exacerbate coeliac mucosa, but that the α-subfraction is the most active.

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Section: Discussionsupporting

confidence: 85%

“…Initially, it was thought that only the a-subfraction exacerbated coeliac disease [7,8]. Recent in vitro and in vivo studies, however, have shown that each of the four gliadin subfractions can induce typical pathological changes in coeliac mu cosa [9][10][11],…”

Section: Introductionmentioning

confidence: 99%

Responses of Antigen-Specific Long-Term Murine T Cell Lines to Wheat Gliadin Fractions

Howdle

Hanson²,

Trejdosiewicz³

et al. 1989

Int Arch Allergy Immunol

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show abstract

“…Bread wheat 0 a-Gliadin [69] 0 A-gliadin [73] 0 Tryptic a-gliadin digest [74] 0 Peptic-tryptic gluten digest [66,69,71,72] 0 Peptic-tryptic gliadin digest [33, 75 -78] 0 Peptic-tryptic-cotazym gliadin digest [33, 74, 78 -80] 0 Peptic-tryptic a-gliadin digest [33,41,66,75,76] 0 Peptic-tryptic b-gliadin digest [33,41,75,76] 0 Peptic-tryptic c-gliadin digest [33,41,75,76] 0 Peptic-tryptic x-gliadin digest [33,41,75,76] 0 Peptide 2R derived from a peptic-tryptic-cotazym digest of gliadin [81] 0 Peptides fractionated from a peptic-tryptic-cotazym digest including peptide fractions B 2 and B 3142 [40,41]. Peptide B 3142 is homologous to A-gliadin amino acid sequence 3 -55 [42] …”

Section: Toxic Cereal Fractionsmentioning

confidence: 99%

Bioactive antinutritional peptides derived from cereal prolamins: A Review

Silano

Vincenzi

1999

Nahrung

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Alcohol-soluble endosperm proteins (prolamins) from some cereals (e.g. wheat, barley, and rye) give origin upon proteolytic digestion to biologically-active antinutritional peptides able to adversely affect in vivo the intestinal mucosa of coeliac patients, whereas prolamins from other cereals (e.g. maize and rice) do not. These antinutritional peptides are also able to: (a) prevent in vitro recovery of atrophic coeliac mucosa; (b) to inhibit differentiation of isolated rat fetal and chick fetal intestines; and (c) to interact with undifferentiated cells either agglutinating them or affecting their proliferation and metabolism. Studies performed with A-gliadin, a highly purified bread wheat prolamin fraction, and its fragments obtained either by chemical cleavage of A-gliadin or by synthesis from aminoacids, clearly pointed out to a few small sequences very rich in glutamine and proline residues as the biologically-active agents. Several protective substances, including mannan and N,N',N"-triacetylchitotriose, have been identified as being able to prevent the effects of these peptides in vitro, but the evidence of their in vivo activity is still missing. The present paper provides a synthetic overview of the available data concerning this highly complex matter and offers a critical appraisal of present hypotheses on the action mechanism of biologically-active peptides derived from cereal prolamins.

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“…Early studies implicated only the α-gliadins in disease activity [5], whereas later studies implied that β-and γ-, but not ω-, gliadins were also active [6,7]. Other studies have implicated all gliadin fractions, with decreasing activity from α-to ω-gliadins [8][9][10][11]. As reviewed by Cole and Kagnoff [12], discrepancies can arise due to a number of factors including the methodologies of gliadin fractionation and protein purity, extrapolation of data from in vitro systems to in vivo disease and different clinical and laboratory end points used to interpret results.…”

Section: Introductionmentioning

confidence: 99%

Studies in vivo of ω-gliadins in gluten sensitivity (coeliac sprue disease)

et al. 1998

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1. Highly purified omega-gliadins from wheat were used to challenge gluten-sensitized individuals. Characteristic responses by mucosal CD3(+) and gamma delta+ lymphocytes were demonstrated. Each lymphocyte subset showed an increase within 8-12 h post-challenge, indicating a specific response by the rectal mucosa to this gliadin species.2. Available sequence data for the omega-gliadins and homologous proteins from barley and rye indicate a common repeating octapeptide motif (consensus PQQPFPQQ). The results indicate, therefore, that the octapeptide repeat, or a contained sequence such as PQQP, plays an important role in the mucosal immunopathology of gluten sensitivity.

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The toxic fraction of gliadin digests in coeliac disease. Isolation by chromatography on Biogel P-10

Cited by 58 publications

References 11 publications

Responses of Antigen-Specific Long-Term Murine T Cell Lines to Wheat Gliadin Fractions

Responses of Antigen-Specific Long-Term Murine T Cell Lines to Wheat Gliadin Fractions

Bioactive antinutritional peptides derived from cereal prolamins: A Review

Studies in vivo of ω-gliadins in gluten sensitivity (coeliac sprue disease)

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