Gluten, a lectin with oligomannosyl specificity and the causative agent of gluten-sensitive enteropathy

Köttgen, E.; Volk, Benedikt; Kluge, Friedrich; Gerok, W.

doi:10.1016/0006-291x(82)91580-7

Cited by 59 publications

(21 citation statements)

References 10 publications

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“…Gly coproteins from the mature villus zone showed only a very slight ability to bind glu ten, whereas binding was higher in the inter mediate zone between villous and crypt cells, and became maximal in the immature cryp tic cells [15]. Other investigators, however, were not able to demonstrate specific or pre ferred binding of gliadin to coeliac mucosal epithelium [17,18].…”

Section: Discussionmentioning

confidence: 90%

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Influence of Gliadin on Fetal Chick Intestine in Tissue Culture

Mothes¹,

Mühle

Müller

et al. 1985

Neonatology

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The purpose of this study was to develop a model system for detecting biological effects of gliadin which may be related to coeliac disease. The technique applied was tissue culture of chicken duodenum at several stages of fetal development. A normally occuring increase in disaccharidase activities in cultured tissue explants was diminished by the presence of peptic-tryptic digested gliadin or of a tryptic fragment of α-gliadin (α-GT 18,000). The effect of peptic-tryptic digested gliadin was only demonstrable in the early phase of fetal development (days 10–14), and disappeared at day 16. The release of enzymes into the culture medium was decreased by gliadin at the 12th day of fetal development. The results suggest that gliadin inhibits the differentiation processes of the fetal intestine.

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Section: Discussionmentioning

confidence: 90%

“…Previously a hypothesis was published [1] that gluten or a fraction thereof would bind to altered, exposed incomplete cell-sur face-membrane glycoproteins of less differen tiated enterocytes and might act in the man ner of toxic lectins. Recently, lectin-like prop erties of gliadin were described [4,15,16].…”

Section: Discussionmentioning

confidence: 99%

Influence of Gliadin on Fetal Chick Intestine in Tissue Culture

Mothes¹,

Mühle

Müller

et al. 1985

Neonatology

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“…The precise mechanisms responsible for these changes are still controversial (4); however, most investigators believe that local immunologic reactions are involved and that gluten initiates the process in an unknown way (5). The basis for gliadin involvement stems from reports that gliadin, a complex heterogeneous protein in gluten of wheat, barley, rye, and possibly oats, binds to smallintestinal surface elements (6). A similar hypothesis for lectin-like involvement of gluten in CD was suggested by Weiser and Douglas (7), who indicated that gluten might of patients with CD had already been described in 1965 (8).…”

mentioning

confidence: 86%

“…Immune reactions to gliadin are likely to play a role in the pathogenesis of the disease, inasmuch as both humoral and cellmediated responses have been demonstrated in the peripheral blood and in the gut of patients with CD. The precise role of gliadin as a lectin remains controversial; several investigators have conflicting reports on the binding properties of F F 111, a peptic-tryptic digest fraction of gliadin, to specific sugar moieties and their effect in culture on tissue epithelium (6,(11)(12)(13)(14)(15).…”

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confidence: 99%

Reactivity of Gliadin and Lectins with Celiac Intestinal Mucosa1

Pittschieler¹,

Ladinser²,

Petell³

1994

Pediatr Res

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The binding patterns of gliadin and selected lectins to jejunal biopsy specimens obtained from children with total villous atrophy during active celiac disease (CD; 19 patients) and in remission (16 patients) were examined by light microscopy. Three categories of carbohydratespecific lectins were chosen for the study: those recognizing mannose/glucose residues, those recognizing N-acetylglucosamine/glucose (glcNAc/glc) residues, and those recognizing N-acetylgalactosamine/galactose (galNAc/gal) residues. The galNAc/gal lectins, with the exception of phaseolus vulgaris agglutinin variants, presented a typical staining of the luminal surface of the jejunal mucosa obtained from CD patients. However, these lectins displayed no reactivity to jejunal sections of CD patients in remission or control biopsies that included healthy children (25 children) and patients suffering from cow milk protein allergy (10 children). The glcNAc/glc lectin showed a strong preferential recognition of CD jejunal tissue but also bound with less intensity to specimens from patients with cow milk allergies and healthy children. Unlike other galNAc/ gal lectins, phaseolus vulgaris agglutinin variants were indistinguishable in their binding patterns to the mucosa of control groups and CD patients in remission and failed to react to CD biopsies. The mannose/glc lectins were not distinctive in their binding patterns. In all cases, lectin binding was specifically inhibited by the lectins' competitive saccharides. Atypical of lectin binding patterns, gliadin reactivity was restricted to intracellular areas of enterocytes and was unique to active CD mucosa. The pathogenesis of childhood and adult CD is still not well understood (1, 2). CD in childhood is characterized by villous atrophy and an increase in both the number of damaged enterocytes and the cell turnover (3). The precise mechanisms responsible for these changes are still

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“…The nondisease specificity of the AGA may also be due to certain intestinal viral infections with antigenic de terminants cross-reactive with gliadin that these pa tients may be exposed to [14]. It may also be that these individuals, especially normals, may have subclinical gluten-sensitive enteropathies [5,6], Recently, Auricchio et al [1] and Kottgen et al [22] have shown that gliadin has a lectin-like property and binds high mannose-type glycoproteins and the com plex formation is inhibited by mannan. Thus, there is a possibility that gliadin absorbed from the intestine binds to the reticulin thus rendering it immunogenic, which may result in tissue damage, especially in indi viduals with genetic predisposition to such an autoim mune response.…”

Section: Discussionmentioning

confidence: 99%

Detection of Antigliadin Antibodies in Bullous Diseases and Their Recognition of Similar Antigenic Polypeptides

Kumar¹,

Jain²,

Beutner³

et al. 1987

Int Arch Allergy Immunol

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The presence of antigliadin antibodies (AGA) in dermatitis herpetiformis (DH) has been associated with gluten-sensitive enteropathy. Because of the discrepancies in the specificity of AGA, we examined the sera of patients with DH, pemphigus and pemphigoid for AGA both by enzyme immunoassay and by immunofluorescence. Approximately 80–90% of sera of patients with DH had AGA. AGA were not disease-specific, they also occurred in about 40–80% of patients with pemphigus and pemphigoid depending on the method employed. In addition, AGA were also present in normal subjects. The incidence of AGA increased with age. AGA from patients with various bullous diseases recognized the same polypeptides thus suggesting that the presence of AGA cannot be regarded as a serological marker of DH.

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Gluten, a lectin with oligomannosyl specificity and the causative agent of gluten-sensitive enteropathy

Cited by 59 publications

References 10 publications

Influence of Gliadin on Fetal Chick Intestine in Tissue Culture

Influence of Gliadin on Fetal Chick Intestine in Tissue Culture

Reactivity of Gliadin and Lectins with Celiac Intestinal Mucosa1

Detection of Antigliadin Antibodies in Bullous Diseases and Their Recognition of Similar Antigenic Polypeptides

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