Cellular and humoral responses in coeliac disease. 1. Wheat protein fractions

Penttila, I A; Devery, Jannine M.; Gibson, C.E.; LaBrooy, Justin T.; Skerritt, John H.

doi:10.1016/0009-8981(91)90221-w

Cited by 10 publications

(11 citation statements)

References 15 publications

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“…This has been confirmed by Skerritt et al [5,25], who showed that only a small proportion (between 1 to 10%) of the proteins in the starch fraction (containing 0.25 to 0.3% protein) were residual gluten or gliadin proteins. This was further confirmed by Pentilla et al [52], who demonstrated that "true" starch granule-associated proteins do not display gluten-like activity on blood lymphocytes of celiac (gluten-intolerant) patients. the SGAPs) have minor immunological homologies to certain wheat gluten and gliadin proteins, the majority show distinct immunological differences from gluten or gliadin proteins.…”

Section: The Influence Of Starch Extraction and Purificationmentioning

confidence: 59%

Starch Granule-Associated Proteins and Polypeptides: A Review

2001

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This paper reviews current information regarding the (non-gluten) proteins which are naturally located in and on starch granules, and which are termed starch granule associated proteins (SGAPs). At least ten major SGAPs can be extracted from most starches and have molecular weights in the range of approximately 5 to 149 kDa. A substantial number of these proteins are located at the starch granule surface, where their presence in association with that of other minor granule components (such as lipids), appears to significantly influence the overall properties of both starch granules and starchy products. The different extraction conditions which can be exploited to selectively remove SGAPs are detailed. Although some SGAPs may serve as supplementary storage proteins, the majority of SGAPs are believed to be starch biosynthetic enzymes, a proportion of which remain trapped within the growing granule structure. The identity and quantities of the biosynthetic enzymes varies with botanical source, genetic variety and even with time. Current knowledge regarding the identities, compositions, locations, properties and functions of several of the more common SGAPs (e.g. the ~15 kDa friabilin/puroindoline proteins, the ~30 kDa protein, and the ~60 kDa starch granule-bound starch synthase (SGBSS) protein) are reviewed in detail.

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Section: The Influence Of Starch Extraction and Purificationmentioning

confidence: 59%

Starch Granule-Associated Proteins and Polypeptides: A Review

2001

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“…Some previous studies have focused on the investigation of immune reactivity and toxic behaviour of non-gluten proteins of wheat related to celiac disease25262728. Recently, Huebener and colleagues have analysed the possible involvement of non-gluten proteins as target antigens in celiac disease related humoral response29.…”

Section: Discussionmentioning

confidence: 99%

“…Farinins, alpha-amylase inhibitors and serine–protease inhibitors are proteins with a conserved cysteine skeleton highly similar to that of prolamins and without the presence of long Q and P rich repetitive regions30. Additionally, 35% of celiac disease patient’s sera showed reactivity against protein spots identified as seed globulins using the protein extract of ‘Butte86′ wheat28. Increased celiac serum antibody reaction was also measured against cereal globulin extracts by Troncone et al 27.…”

Section: Discussionmentioning

confidence: 99%

Characterization of globulin storage proteins of a low prolamin cereal species in relation to celiac disease

Gell

Kovács

Veres

et al. 2017

Sci Rep

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Brachypodium distachyon, a small annual grass with seed storage globulins as primary protein reserves was used in our study to analyse the toxic nature of non-prolamin seed storage proteins related to celiac disease. The main storage proteins of B. distachyon are the 7S globulin type proteins and the 11S, 12S seed storage globulins similar to oat and rice. Immunoblot analyses using serum samples from celiac disease patients were carried out followed by the identification of immune-responsive proteins using mass spectrometry. Serum samples from celiac patients on a gluten-free diet, from patients with Crohn’s disease and healthy subjects, were used as controls. The identified proteins with intense serum-IgA reactivity belong to the 7S and 11–12S seed globulin family. Structure prediction and epitope predictions analyses confirmed the presence of celiac disease-related linear B cell epitope homologs and the presence of peptide regions with strong HLA-DQ8 and DQ2 binding capabilities. These results highlight that both MHC-II presentation and B cell response may be developed not only to prolamins but also to seed storage globulins. This is the first study of the non-prolamin type seed storage proteins of Brachypodium from the aspect of the celiac disease.

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“…The indirect I. Ml F and MPCA assays were per formed as described previously (2. 3], except peripheral blood mononuclear cells which were enriched for T lymphocytes [18] were used in the indirect LMIF assay. A comparison between the responses of coeliac patients and control subjects was performed using the Student t test.…”

Section: Patients and Assays For Cell-mediated Immunitymentioning

confidence: 99%

Identification of Reactive Synthetic Gliadin Peptides Specific for Coeliac Disease

Devery

Bender

Penttila

et al. 1991

Int Arch Allergy Immunol

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Gluten intolerance (coeliac disease) is characterised by the development of a small intestinal lesion following exposure to the gliadin fraction after consumption of wheat and related cereals. Cellular immune mechanisms are thought to be responsible for gliadin toxicity, but the toxic sequence/s within gliadin have not been clearly established. A panel of synthetic gliadin peptides was tested using peripheral blood mononuclear cells from coeliac patients and two assays for cell-mediated immunity. Using the indirect leucocyte migration inhibition factor and the macrophage procoagulant activity assays, gliadin peptides which were located in the aminoterminal or the proline-rich domain of the alpha/beta gliadin molecule were coeliac-active. Peptides predicted by T cell algorithms or on the basis of homology to adenovirus Ad12 Elb protein and which were located in the proline-poor gliadin domains were inactive. Protein sequence studies which indicate significant homology in the proline-poor gliadin domains with a number of non-coeliac-toxic seed proteins also supported the hypothesis that the proline-rich domains may be more important in the pathogenesis of coeliac disease.

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Cellular and humoral responses in coeliac disease. 1. Wheat protein fractions

Cited by 10 publications

References 15 publications

Starch Granule-Associated Proteins and Polypeptides: A Review

Starch Granule-Associated Proteins and Polypeptides: A Review

Characterization of globulin storage proteins of a low prolamin cereal species in relation to celiac disease

Identification of Reactive Synthetic Gliadin Peptides Specific for Coeliac Disease

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