Immunoreactivity of antibodies against transglutaminase-deamidated gliadins in adult celiac disease.

Background: The significance of the presence of anti-gliadin antibodies in patients affected by celiac disease is still unclear. It is hypothesized that gliadin deamidation, catalysed by transglutaminase, plays a role in favoring the antigen presentation.

Aim: To determine the immunoreactivity of anti-gliadin antibodies from untreated celiac patients to transglutaminase deamidated gliadins.

Celiac-related properties of chemically and enzymatically modified gluten proteins.

The effects of chemical (acid-heating treatment) and enzymatic (microbial transglutaminase, TGase) modification (deamidation) of gluten proteins on their physicochemical and celiac disease-related properties were studied. Ammonia release, sodium dodecyl sulfate-polyacrylamide gel electrophoresis, and sample solubility analyses were employed to check the extent of gluten modification. Among different treatments achieved, the acid-heating treatment performed at 90 degrees C for 3 h induced gluten deamidation, paralleling an increase of gluten solubility without relevant proteolysis.

Damaging effects of gliadin on three-dimensional cell culture model.

Aim: To evaluate the effects of gliadin on the oxidative environment in the "in vivo-like" model of a three-dimensional cell culture system.

Methods: LoVo cell line (intestinal adenocarcinoma) multicellular spheroids were treated with digested gliadin (with albumin used as a control). Spheroid volumes, cell viability and morphology, lactate dehydrogenase (LDH) release, content of reduced glutathione (GSH) and activity of GSH-related enzymes were examined.