Аnti-gliadin IgA

Celiac disease (gluten-sensitive enteropathy) is an autoimmune disease and is accompanied by inflammation and atrophy of the villi of the small intestine mucosa.

Gliadin is an alcohol-soluble fraction of gluten, which in turn is a component of the glutenopectin (protein part) of cereals. Gluten provides the elasticity of flour dough and due to this property is widely used for the preparation of not only bakery products, but also in the production of many other food products.

Another reason for the development of celiac disease is the immaturity of tight contacts between small intestine mucosal cells in children, as it leads to the penetration of alpha-gliadin fragments into the submucosa. The increased activity of one of the connective tissue enzymes (intestinal tissue transglutaminase) in the intestine wall leads to the deamination of alpha-gliadin molecules, resulting in the formation of gliadin fragments resistant to proteolysis. These linear antigens have been well characterized and named, deamidated gliadin peptides (DGP). Tissue transaminase and gliadin fragments (DPG) become immunogenic and cause an antibody immune response.

Individuals with primary insufficiency of serum IgA synthesis (primary selective immunodeficiency) are predisposed to the development of celiac disease, however, their serological markers of the IgA class turn out to be false-negative. At low serum IgA concentrations (less than 0.2 g/l), the examination should include at least one test to detect specific IgG class autoantibodies.

Antibodies to deamidated gliadin peptides of the IgG class should be used to diagnose celiac disease in individuals with selective deficiency of IgA synthesis in conjunction with the detection of antibodies to IgG class tissue transglutaminase.

Antibody titers to gliadin and other serologic markers of celiac disease fall below the detection threshold six months after switching to a gluten-free diet. Antibody monitoring can be used to assess dietary compliance.