Wheat α-amylase inhibitor: A second route of allergic sensitization☆☆☆★★★

Jm, James; Jp, Sixbey; Rm, Helm; Ga, Bannon; Burks, A.W.

doi:10.1016/s0091-6749(97)70103-9

Cited by 124 publications

(74 citation statements)

References 29 publications

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“…and high m.w. glutenin subunits (LMW-GSs and HMW-GSs, respectively) (9, 10), a-amylase inhibitor subunits (11)(12)(13)(14)(15), and lipid transfer protein (10,16), the panel of wheat allergens is still incomplete (17).…”

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confidence: 99%

Molecular and Immunological Characterization of Tri a 36, a Low Molecular Weight Glutenin, as a Novel Major Wheat Food Allergen

Baar

Pahr

Constantin

et al. 2012

The Journal of Immunology

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Wheat is an essential element in our nutrition but one of the most important food allergen sources. Wheat allergic patients often suffer from severe gastrointestinal and systemic allergic reactions after wheat ingestion. In this study, we report the molecular and immunological characterization of a new major wheat food allergen, Tri a 36. The cDNA coding for a C-terminal fragment of Tri a 36 was isolated by screening a wheat seed cDNA expression library with serum IgE from wheat food-allergic patients. Tri a 36 is a 369-aa protein with a hydrophobic 25-aa N-terminal leader peptide. According to sequence comparison it belongs to the low m.w. glutenin subunits, which can be found in a variety of cereals. The mature allergen contains an N-terminal domain, a repetitive domain that is rich in glutamine and proline residues, and three C-terminal domains with eight cysteine residues contributing to intra- and intermolecular disulfide bonds. Recombinant Tri a 36 was expressed in Escherichia coli and purified as soluble protein. It reacted with IgE Abs of ∼80% of wheat food-allergic patients, showed IgE cross-reactivity with related allergens in rye, barley, oat, spelt, and rice, and induced specific and dose-dependent basophil activation. Even after extensive in vitro gastric and duodenal digestion, Tri a 36 released distinct IgE-reactive fragments and was highly resistant against boiling. Thus, recombinant Tri a 36 is a major wheat food allergen that can be used for the molecular diagnosis of, and for the development of specific immunotherapy strategies against, wheat food allergy.

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confidence: 99%

Molecular and Immunological Characterization of Tri a 36, a Low Molecular Weight Glutenin, as a Novel Major Wheat Food Allergen

Baar

Pahr

Constantin

et al. 2012

The Journal of Immunology

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“…These proteins for many years were recognized only as undesirable, anti-nutritional substances: they decrease the availability of nutritional components (6)(7)(8)(9)(10)(11) and moreover are listed among protein fractions causing food allergies ( 12,13 ) . However, in recent years, more and more studies have demonstrated that these proteins can be utilized as components of therapeutic and health-related products under some conditions ( 8 , 14, 15 ).…”

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confidence: 99%

Digestive Enzyme Inhibitors from Grains as Potential Components of Nutraceuticals

Piasecka‐Kwiatkowska

Warchalewski

Zielińska‐Dawidziak

et al. 2012

J Nutr Sci Vitaminol

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Summary Inhibitor activity against digestive enzymes, such as ␣ -amylase from human saliva and porcine pancreas and trypsin from bovine pancreas, of three cereal grains species were studied as potential components of nutraceuticals strengthening diabetes and obesity treatment. Significant differences were demonstrated: the highest antitryptic activity was found in the grain of the rye varieties studied, whereas the grain of the wheat varieties had significantly higher ability to inhibit ␣ -amylases from human saliva and porcine pancreas. Additionally, seeds of Puma, one of the studied wheat varieties, demonstrated especially low antitryptic activity. Such a beneficial arrangement of inhibitors, i.e. high level of inhibitors of ␣ -amylase from human saliva and porcine pancreas and simultaneously low level of trypsin inhibitors from bovine pancreas, indicate the possibility of the application of seeds with such properties to the preparation of nutraceuticals for people with obesity or suffering from diabetes.

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“…This resistance may be very important for both sensitisation of the immune system after penetration of the intestinal mucosa and for elicitation of gastrointestinal symptoms of food allergy (Astwood et al 1996;Mouécoucou et al 2004). Hypersensitivity reactions after wheat ingestion have been reported by several authors (James et al 1997;Mittag et al 2004). Ingestion of foods containing wheat and other related cereals can induce gastrointestinal (GI) symptoms by either immunological or non-immunological mechanisms (Simonato et al, 2001).…”

Section: Resultsmentioning

confidence: 99%

Influence of glycation and pepsin hydrolysis on immunoreactivity of albumin/globulin fraction of herbicide resistant wheat line

Nagy¹,

Marciniak-Darmochwał²,

Krawczuk³

et al. 2009

Czech J. Food Sci.

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Nagy A., Marciniak-Darmochwał K., Krawczuk S., Mierzejewska D., Kostyra H., Gelencsér É.(2009): Influence of glycation and pepsin hydrolysis on immunoreactivity of albumin/globulin fraction of herbicide resistant wheat line. Czech J. Food Sci., 27: 320-329.The aim of this study was to investigate the influence of non-enzymatic glycosylation on the immunogenic properties of soluble wheat proteins. Albumin/globulin fractions of herbicide resistant wheat line were non-enzymatically glycosylated using glucose for seven days at 37°C. The changes in their structures and immunoreactivity were then determined. The protein fractions were also hydrolysed with pepsin to determine the resistance to digestion. Albumin/globulin fractions before and after non-enzymatic glycosylation were analysed using o-phthaldialdehyde method and sodium dodecyl sulphate-polyacrylamide gel electrophoresis. The immunoreactivity of the protein fractions was determined using enzyme-linked immunosorbent assay methods, as well as affinity chromatography. The soluble wheat proteins showed smaller amounts of available α-amino groups after non-enzymatic glycosylation, and were stronger immunogens after glycation, but their antigenicity was not been affected significantly. However, pepsin hydrolysis of wheat proteins decreased their immunoreactivity.

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Wheat α-amylase inhibitor: A second route of allergic sensitization☆☆☆★★★

Cited by 124 publications

References 29 publications

Molecular and Immunological Characterization of Tri a 36, a Low Molecular Weight Glutenin, as a Novel Major Wheat Food Allergen

Molecular and Immunological Characterization of Tri a 36, a Low Molecular Weight Glutenin, as a Novel Major Wheat Food Allergen

Digestive Enzyme Inhibitors from Grains as Potential Components of Nutraceuticals

Influence of glycation and pepsin hydrolysis on immunoreactivity of albumin/globulin fraction of herbicide resistant wheat line

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