Enzymatic digestion of gliadin: the effect of the resultant peptides in adult celiac disease

Bronstein, H D; Haeffner, L J; Kowlessar, O. Dhodanand

doi:10.1016/0009-8981(66)90080-5

Cited by 63 publications

(15 citation statements)

References 25 publications

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“…The finding that this fraction is not toxic when consumed in considerable amounts by patients with treated coeliac disease establishes that the damaging component of gluten is not an oligopeptide despite the findings of earlier workers (Krainick and Mohn, 1959;Bronstein et al, 1966), and supports the later work of Douglas and Booth (1970) and Berg, Dahlqvist, Lindberg, and Nord6n (1970).…”

Section: Discussionsupporting

confidence: 60%

Identifying toxic fractions of wheat gluten and their effect on the jejunal mucosa in coeliac disease

Dissanayake¹,

Jerrome²,

Offord³

et al. 1974

Gut

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SUMMARY The toxicity of three fractions (A, B, and C) obtained by ultrafiltration of a peptic: tryptic digest of gluten has been assessed by serial feeding experiments in patients with treated coeliac disease.The first fraction (A), which contains amino acids and oligopeptides, produced no damage to the jejunal mucosa.The other two fractions (B and C) both caused mucosal damage. Fraction B, which contains the products of digestion of smaller molecular weight, consists of polypeptides which are concentrated in the region of 8000 molecular weight. It contains no gliadin (molecular weight 50 000) or gluten.Ultrastructural evidence of damage was visible six hours after challenge with fraction B and by 10 hours histological abnormalities were also present.Ultrastructural abnormalities occurred early in the epithelial cells and preceded changes in the basement membrane and capillaries.The disaccharidases showed a pronounced depression in all three subjects by 24 hours. The rapid onset of damage after challenge, coupled with the evidence of recovery as soon as 72 hours later, is more in keeping with a direct action on the surface epithelial cells rather than an immune mechanism.

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Section: Discussionsupporting

confidence: 60%

Identifying toxic fractions of wheat gluten and their effect on the jejunal mucosa in coeliac disease

Dissanayake¹,

Jerrome²,

Offord³

et al. 1974

Gut

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“…0 Peptic-tryptic gluten digest [35] 0 Fractions B and C from peptic-tryptic gluten digest [36] 0 Peptic-tryptic gliadin digest [37] 0 Peptic-tryptic-cotazym gliadin digest [37,38] 0 Tryptic a-gliadin digest [39] 0 Gliadin peptide fractions B 2 , B 3 and B 3142 [40,41]. Peptide B 3142 is homologous to A-gliadin amino acid sequence 3 -55 [42] [59] reported that patients with tropical sprue reacted to a glutenfree diet with a decreased steatorrhea and with an improvement in the jejunal lesion.…”

Section: Bread Wheatmentioning

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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“…PT-gliadin Peptic-tryptic digested gliadin (Fluka, Buchs, Switzerland) was hydrolised according to Bronstein et al (1966) as modified by Cornell and Townley, (1973). The final digest was adjusted to pH 7-2 with HCI and centrifuged for 20 minutes at 2000 x g. The supernatant was immersed into a boiling water bath for 15 minutes to destroy trypsin activity.…”

Section: Gliadin or Gluten Preparationsmentioning

confidence: 99%

Re-evaluation of the techique of organ culture for studying gluten toxicity in coeliac disease.

Hauri¹,

Kédinger²,

Haffen³

et al. 1978

Gut

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SUMMARY In vitro cytotoxicity of four different gluten fractions was tested in organ culture for up to 48 hours using flat intestinal biopsies from children with coeliac disease. The fractions were (1) a peptic-tryptic digest of gliadin containing a moderate amount of alpha-gliadin, (2) a peptic-tryptic digest of gluten (Frazer fraction III) from a strain of wheat with a high content of alpha-gliadin, (3) alpha-gliadin, and (4) alpha-GT-18 000, a tryptic fragment of alpha-gliadin. The latter three fractions were toxic to coeliac patients in vivo. In vitro, however, none of these fractions proved to be cytotoxic. When added to the culture medium they were not capable of inhibiting the regeneration of the surface epithelium as visualised by histology and electron microscopy. The only difference between cultures with and without gluten fractions was that the former produced slightly more mucus when maintained in vitro as observed in the dissecting microscope. Furthermore, for Frazer fraction III the absence of apparent toxicity was confirmed by the behaviour of brush border enzyme activities during culture. Our results are not in accordance with those reported in the literature. We believe that the criteria used at the present time for the assessment of gluten toxicity in vitro should be extended to include the process of enterocyte desquamation.

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Enzymatic digestion of gliadin: the effect of the resultant peptides in adult celiac disease

Cited by 63 publications

References 25 publications

Identifying toxic fractions of wheat gluten and their effect on the jejunal mucosa in coeliac disease

Identifying toxic fractions of wheat gluten and their effect on the jejunal mucosa in coeliac disease

Bioactive antinutritional peptides derived from cereal prolamins: A Review

Re-evaluation of the techique of organ culture for studying gluten toxicity in coeliac disease.

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