Wheat-dependent exercise-induced anaphylaxis in mice is caused by gliadin and glutenin treatments

Kozai, Hana; Yano, Hiromi; Matsuda, Tsukasa; Kato, Yasuko

doi:10.1016/j.imlet.2005.07.007

Cited by 30 publications

(33 citation statements)

References 27 publications

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“…Studies in humans [43] and mice [44] have shown that exercise facilitates allergen absorption from the gastrointestinal tract. Palosuo et al [45] hypothesized that transglutaminase (intestinal enzyme) could play a role in increasing ω5-gliadin allergenicity during exercise.…”

Section: Discussionmentioning

confidence: 99%

Evaluation of an in vitro Mast Cell Degranulation Test in the Context of Food Allergy to Wheat

Bodinier

Brossard

Triballeau

et al. 2008

Int Arch Allergy Immunol

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Background: Antigenic profiles obtained by ELISA with IgE from patients with wheat food allergy (WFA) established that major allergens are albumins/globulins (AG) for children suffering from atopic eczema/dermatitis syndrome (AEDS), ω5-gliadins for adults suffering from wheat-dependent exercise-induced anaphylaxis (WDEIA), anaphylaxis or urticaria and low-molecular-weight (LMW) glutenin subunits for patients with anaphylaxis. We aimed to characterize a new mast cell transfectant for its ability to degranulate with wheat proteins and patient sera and compare these results to those obtained by ELISA. Methods: Thirty sera from patients with WFA were tested: 14 with AEDS (group 1) and 16 with WDEIA, anaphylaxis or urticaria (group 2). An IgE Fc receptor (FcΕRI) humanized rat RBL-2H3 line was established by transfection with cDNAs encoding α-, β- and γ-subunits for the human IgE receptor. Results: A humanized RBL clone was selected for its capacity to express mRNA α-, β- and γ-subunits of FcΕRI, to bind allergen-specific human IgE and to degranulate. In group 1, sera induced enhanced degranulation with AG extract, but rarely reacted with gliadins and glutenins. In group 2, half of the sera showed degranulation with LMW glutenins whereas the AG fraction and lipid transfer proteins were rarely positive. ω5-Gliadins did not appear as a major allergen in degranulation assays, although functional allergen-specific IgE was measurable in appreciable amounts. Conclusion: Our data demonstrate that in wheat food allergen evaluation, correlation exists between mast cell degranulation and IgE measurements, depending on the type of allergen. Therefore, the biological activity of some allergen types may also be affected by other parameters.

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Section: Discussionmentioning

confidence: 99%

Evaluation of an in vitro Mast Cell Degranulation Test in the Context of Food Allergy to Wheat

Bodinier

Brossard

Triballeau

et al. 2008

Int Arch Allergy Immunol

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“…In addition, alcohol-soluble gliadins were not included in the crude antigen extracts. Gliadins are a major cause of WDEIA and glutenins also are implicated in WDEIA, although to a lesser extent (Kozai et al 2006). However, in the present study, we used the salt-soluble proteins to sensitize mice and found induction of allergy responses.…”

Section: Resultsmentioning

confidence: 88%

“…Non-gluten proteins are typically salt-soluble and the major components are albumin and globulin, which range in size from 15 to 100 kDa (Kozai et al 2006). Gluten proteins include gliadins and glutenins and are salt-insoluble proteins.…”

Section: Resultsmentioning

confidence: 99%

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Differential induction of allergy responses by low molecular weight wheat proteins from six wheat cultivars

Cho

Lee

Hwang

et al. 2017

JABC

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Although wheat is a common staple food in the world, some people suffer from a variety of wheat allergies. For example, wheat-dependent exercise-induced anaphylaxis is induced in the gastrointestinal tract by wheat proteins. Relatively high molecular weight proteins that are salt-insoluble induce many wheat allergies. In the present study, we investigated the induction of an allergy response using crude wheat proteins, which are relatively low molecular weight, salt-soluble proteins. The crude antigen used in this study was extracted using phosphate buffered saline. When the antigen extracts from various wheat cultivars were orally administered, differentiable degrees of allergy responses were observed as measured by serum IgE and histamine secretion compared to the control. Serum IgE levels increased following administration of three of the wheat extracts. This evidence suggests that a combination of salt-soluble wheat proteins could be antigens for the induction of various allergy responses.

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“…Matsuo et al [25] reported that IgE antibodies from 80% of patients with WDEIA reacted strongly to ω-5 gliadin, and IgE antibodies from the remaining patients reacted to high-molecular-mass glutenin subunits. Although we already reported that whole-gliadin-sensitized mice had a greater elevation in serum IgE, a remarkably shorter running time and a higher level of intestinal erosion when compared with control animals [26], it remains unclear whether ω-5 gliadin alone causes anaphylaxis symptoms, such as a decrease in body temperature and physical activity, after oral administration of ω-5 gliadin in sensitized animals or humans. In addition, very recently we observed that ω-5 gliadin also caused WDEIA in a similar manner to the whole gliadin fraction [27].…”

Section: Introductionmentioning

confidence: 99%

Exercise-Independent Wheat-Induced Anaphylaxis Caused by ω-5 Gliadin in Mice

Tanaka

Nagano²,

Yano³

et al. 2011

Int Arch Allergy Immunol

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Background: ω-5 Gliadin is known as a major allergen in wheat-dependent exercise-induced anaphylaxis. The characteristics that make ω-5 gliadin an allergen remain unclear. Methods: Mice were sensitized by means of intraperitoneal injection of gliadin fractions together with the adjuvant alum. Anaphylactic responses were assessed by measuring body temperature and voluntary physical activity. Specific IgE levels in mouse serum were evaluated by ELISA. After oral administration of proteins to mice, concentrations of administered proteins in their portal blood were also analyzed by competitive inhibition ELISA. Results: Oral administration of ω-5 gliadin evoked significant decreases in body temperature and physical activity of sensitized mice, whereas the gliadin fraction did not induce these effects at the same dose. These responses were exercise independent. ELISA analysis revealed that IgE antibodies from sensitized mice react to ω-5 gliadin with great efficacy. After oral administration of either the gliadin fraction or ω-5 gliadin, blood levels of ω-5 gliadin were much higher than those of the gliadin fraction. Conclusions: ω-5 Gliadin caused anaphylaxis in sensitized mice, whereas the gliadin fraction did not at the same dose. The anaphylactic response was exercise independent. It is likely that IgE of sensitized mice reacts strongly to ω-5 gliadin and that ω-5 gliadin is better absorbed from the gastrointestinal tract than other components of the gliadin fraction. These results indicated that ω-5 gliadin has prominent characteristics as an allergen and that exercise might be an indirect factor in anaphylaxis induction.

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Wheat-dependent exercise-induced anaphylaxis in mice is caused by gliadin and glutenin treatments

Cited by 30 publications

References 27 publications

Evaluation of an in vitro Mast Cell Degranulation Test in the Context of Food Allergy to Wheat

Evaluation of an in vitro Mast Cell Degranulation Test in the Context of Food Allergy to Wheat

Differential induction of allergy responses by low molecular weight wheat proteins from six wheat cultivars

Exercise-Independent Wheat-Induced Anaphylaxis Caused by ω-5 Gliadin in Mice

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