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The Heartbreak of Wheat-Related Disorders
Published in Stephen T. Sinatra, Mark C. Houston, Nutritional and Integrative Strategies in Cardiovascular Medicine, 2022
In the gluten family of protein fragments from poorly digested wheat, gliadin can be broken down into various amino acid lengths or peptides. Gliadorphin is a 7-amino acid-long peptide, Tyr-Pro-Gln-Pro-Gln-Pro-Phe, which forms from incompletely digested gliadin. When digestive enzymes are insufficient to break down gliadorphin into 2–3 amino acids length, and a compromised intestinal wall allows for the leakage of the entire 7-amino acid-long fragment into the blood, gliadorphin can pass through to the brain via circumventricular organs and activate opioid receptors resulting in disrupted brain function. In the brain, gliadorphin and other gluteomorphins can directly interfere with neuronal messaging by binding to the opioid receptors, thus inhibiting the natural binding of neurotransmitters to their receptors.97–99 In addition, lymphocytes carry the same receptors on their own surfaces; therefore, gluteomorphins can indirectly interfere with opioid receptors through lymphocyte secretion of cytokines and cause the delivery of aberrant messages to the brain.100 If antibodies are produced to gluteomorphins (a biomarker commonly identified in serology), these antibodies act as natural opioids on the lymphocytes and the nerve cells causing neuroimmune abnormalities.101
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.
The skin
Published in C. Simon Herrington, Muir's Textbook of Pathology, 2020
Dermatitis herpetiformis has a strong genetic component and is associated with HLA-DQ2 and DQ8. Gluten, a protein present in wheat, rye, and barley is digested by intestinal enzymes to gliadin which is transported into the lamina propria. Here the enzyme tissue transglutaminase (TTG) catalyses the removal of an amine group (deamination), increasing antigenicity. The genes HLA-DQ2 and DQ8 encode molecules on antigen presenting cells that bind gliadin and activate CD4+ T-cells.
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.
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].
Evaluation of Ocular Parameters in Adult Patients with Celiac Disease
Published in Current Eye Research, 2021
Leyla Hazar, Gülistan Oyur, Kadri Atay
Celiac disease (CD) is a chronic inflammatory disease caused by gluten. Although it predominantly affects the gastrointestinal tract, it can present multiorgan manifestations. In this autoimmune disease, the key genetic elements, human leukocyte antigen (HLA)-DQ2 and HLA-DQ8, are well defined.1 Although celiac disease occurs mainly in childhood, it is a common disease that can occur at any age, and its prevalence is 0.5 to 1.0% in the white population.2 Diagnosis is based on the combination of mucosal changes detected by duodenal biopsy and positive serological tests for anti-tissue transglutaminase 2 IgA (anti-tTG IgA) antibodies, anti-endomysium antibodies (EmA), and deamidated gliadin peptide antibodies.3 The disease typically presents with crypt hyperplasia and villous atrophy in pathological evaluation.4