Vitamin D3 Versus Gliadin: A Battle to the Last Tight Junction

Excerpt

Celiac disease (CD), the most common chronic autoimmune enteropathy present in Western populations, is triggered by gluten ingestion in genetically susceptible individuals carrying the HLA DQ2 and/or DQ8 loci [1]. Gluten, a high molecular weight protein present in the endosperm of grass-related grains, including wheat, barley, and rye, is stored within seeds in order to ensure a stable nutrient supply supporting the germination and development of young plants. Gluten-containing cereals, the most important crop in the world, are used to make food products such as pasta, bread, other baked and pastry products. The viscoelastic and stabilizing properties of gluten have fostered its use as an additive in the baking industry; furthermore, it gives food greater palatability due to the creation of disulfide bonds that in combination with atmospheric oxygen and nitrogen alter the properties of the dough as a function of the sulfhydryl and disulfide content [1]. Gluten is a composite of two classes of protein, glutenins and prolamins (gliadin, secalin, and hordein), which can be further fractionated to produce peptides. Pepsin–trypsin-resistant gliadin (PT-G) is an undigested gliadin fragment that substantially contributes to the pathogenesis of CD by altering intercellular tight junctions (TJs) [2]. …