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Celiac disease
Published in Phillip D. Smith, Richard S. Blumberg, Thomas T. MacDonald, Principles of Mucosal Immunology, 2020
Celiac disease is a chronic, T-cell–mediated, inflammatory disorder of the small intestine resulting from an inappropriate immune response to gluten. Gluten is a complex of proteins present in wheat, barley, and rye. Wheat gluten proteins consist of α-, γ-, and ω-gliadins as well as high and low molecular weight glutenin subcomponents. Both gliadin and glutenin proteins can induce the disease, which is treated with a lifelong gluten exclusion diet. The mucosal pathology associated with celiac disease is localized to the proximal small intestine and is characterized by villus atrophy and prominent infiltration of leukocytes into the epithelium and lamina propria. The mucosal absorptive surface is reduced as a consequence of villus atrophy, leading to malabsorption that may result in anemia and steatorrhea. Additional symptoms, including fatigue, infertility, neurologic manifestations, and enamel defects, may not indicate an intestinal disease, and some patients have few or even no symptoms. The eclectic nature of the symptoms is a challenge to clinicians, and consequently, many patients are not diagnosed or experience long delays before diagnosis.
Relation of Antigliadin Antibodies to Gluten-Sensitive Enteropathy
Published in Tadeusz P. Chorzelski, Ernst H. Beutner, Vijay Kumar, Tadeusz K. Zalewski, Serologic Diagnosis of Celiac Disease, 2020
Wim Th. J. M. Hekkens, Marja van Twist - de Graaf
We therefore speculate that the immunogenic sites on a prolamin molecule are more or less buried in the tertiary and quaternary structure. Depending on the exposure of the potentially immunogenic site, the immunocompetent cell can recognize the structure and produce antibodies against it. These antibodies, being of a much smaller size than the immunocompetent cell, can more easily penetrate at least part of the prolamin structure and react with epitopes that were not exposed on the surface of the protein. There are some controversies about the cross-reactivity of antiprolamin sera with glutenin. Since glutenin as such is insoluble, a reaction is difficult to demonstrate. Degradation by cleavage of -SS- bonds by reduction gives a partly soluble product, and some cross-reactivity is obtained. If the structural relationship between gliadin and glutenin allows for common epitopes, then it cannot be excluded that glutenin is also toxic to celiac patients. This latter point is one of the poorly studied areas in celiac disease.
Food allergens
Published in Richard F. Lockey, Dennis K. Ledford, Allergens and Allergen Immunotherapy, 2020
Wheat and other cereal grains are common food allergens, particularly in children. The proteins of wheat include the water-soluble albumins, the saline-soluble globulins, the aqueous ethanol-soluble prolamines (i.e., gliadins), and the glutelins. Subjects with wheat allergy have specific IgE to wheat fractions of 47 kDa and 20 kDa, proteins not recognized by specific-IgE from subjects with grass allergy [47]. Wheat α-amylase inhibitor (15 kDa) is also a major wheat allergen. This protein does not bind IgE from wheat-tolerant control subjects, including those with grass allergy. Battais et al. [48] identified major wheat allergens by IgE-binding studies. IgE from subjects with wheat-dependent exercise-induced anaphylaxis and urticaria react with sequential epitopes (QQX1PX2QQ) in the repetitive domain of gliadins, whereas IgE from atopic dermatitis subjects recognizes conformational epitopes [49].
Recent developments in Phos-tag electrophoresis for the analysis of phosphoproteins in proteomics
Published in Expert Review of Proteomics, 2022
Kinoshita et al. [18] separated the non-phosphorylated E. coli protein ClpX and human histone H2A using Phos-tag SDS-PAGE. They found that the protein mobilities were significantly different from those obtained when using SDS-PAGE. They suggested that this was caused by the interaction of the Phos-tag molecule with the negatively charged carboxyl group of the proteins’ glutamate residues. Recently, wheat seed proteins were separated by Phos-tag diagonal electrophoresis (Hirano, H. unpublished data). The storage proteins glutenin and gliadin are the major proteins present in wheat seeds. In Phos-tag diagonal electrophoresis, both the proteins migrate away from the diagonal line to the cathode side. Thus, even if glutenin and gliadin separated by SDS-PAGE are stained with ProQ diamond, which can detect phosphoproteins, they are not detected as phosphoproteins. Additionally, phosphorylated glutenin and gliadin were not detected when shotgun analysis was used to detect the presence of phosphoproteins. Both glutenin and gliadin are known to be glutamate-rich proteins. It is thought that the presence of glutamate residues is the reason why both these proteins migrate away from the diagonal line to the cathode side on performing Phos-tag diagonal electrophoresis.
The effect of chronic exposure to flour dust on pulmonary functions
Published in International Journal of Occupational Safety and Ergonomics, 2021
Ahmadreza Zamani, Narges Khanjani, Majid Bagheri Hosseinabadi, Malihe Ranjbar Homghavandi, Roholah Miri
Flour dust is widely recognized as one of the most important causes of pulmonary dysfunction [1]. The content of wheat flour significantly contributes to its harmful effects. Wheat flour is a complex, allergenic dust, which contains various types of antigenic and allergic compounds [2]. The major proteins found in wheat flour include salt-soluble globulins, water-soluble albumins, glutens and gliadins, which are effectively involved in the development of pulmonary function disorders. Gliadins and glutelins, which make up about 80% of wheat flour proteins [3,4], play an effective role in allergic diseases. Also, albumins and globulins are the major contributing proteins in hypersensitivity reactions to flour dust [5,6]. In addition to proteins, the contaminants associated with flour, like parasites, insects and fungi, and its metabolites (aflatoxin), silica, bacterial endotoxins and various chemical additives such as insecticides and herbicides can exacerbate the adverse pulmonary effects [7,8]. A wide range of employees and workers in various food industries, including traditional and industrial bakeries, producing biscuits, cakes, pasta and pizza, and grain mill workers are occupationally exposed to flour dust [9]. In 2011, the threshold limit value for flour dust was recommended to be 0.5 mg/m3 by the American Conference of Governmental Industrial Hygienists (ACGIH) [10], which has also been accepted by the Iranian Center for Environmental and Occupational Health. This was the exposure level in the respiratory region for flour mill industry workers.
An updated overview on celiac disease: from immuno-pathogenesis and immuno-genetics to therapeutic implications
Published in Expert Review of Clinical Immunology, 2021
Paolo D’Avino, Gloria Serena, Victoria Kenyon, Alessio Fasano
One feature that makes CD a unique autoimmune disease is the known causative agent, gluten. Gluten is the major protein of wheat grains and it is composed by hundreds of distinct proteins such as gliadin and glutenin. It is found in common grains like wheat, rye and barley and it is formed by numerous proteins containing antigenic epitopes for patients with CD [17]. The wheat kernel contains 8%-15% of protein, out of 90% is gluten and the 10% remaining is albumin. Other grains such as rye and barley contain similar proteins (secalin and hordein). Furthermore, there are other hybrid species of cereals which contain gluten such as triticale (which comes from the cross between wheat and rye), or other derivatives of wheat, such as kamut (Triticum turgidum) and spelt (Triticum spelta), which contain gluten as well [18].