Cross linking to tissue transglutaminase and collagen favours gliadin toxicity in coeliac disease.

Background And Aims: Intestinal inflammation in coeliac disease is driven by the gluten fraction of wheat proteins. Deamidation or cross linking of gluten peptides by tissue transglutaminase (tTG), the coeliac disease autoantigen, creates potent T cell stimulatory peptides. Therefore, our aim was to identify the reaction patterns of gluten peptides, intestinal extracellular matrix proteins, and tTG.

Enhanced peptide-binding capacities of small intestinal brush border membranes in celiac disease.

In pathogenesis of celiac disease, the significance of prolamin peptide interactions with enterocytes is controversial. Changes in cellular metabolism induced by gliadin peptides, as well as uptake and presentation by enterocytes, are discussed. We analyzed peptide binding to enterocytic membranes as a potential key event.

Comparative investigations of partial amino acid sequences of prolamins and glutelins from cereals. VIII. Amino acid sequences of glutelin peptides.

The peptide fractions isolated from chymotryptic hydrolysates of wheat, rye and barley glutelins were separated by high-performance liquid chromatography on octadecyl silica gel. The peptides obtained were analysed for their amino acid composition and some also for their amino acid sequence. Characteristic sequences of peptides from wheat glutelin can be grouped into three types.

High-performance liquid chromatography of reduced glutenin: amino acid composition of fractions and components.

Reduced glutenin is separated by gel permeation high-performance liquid chromatography into three major and five minor fractions, which significantly differ in their amino acid compositions. By reversed-phase high performance liquid chromatography, about 20 glutenin components are obtained. These can be classified into three groups according to their amino acid compositions: a hydrophilic group with relatively high values of Glx and Phe, a more hydrophobic group with a high content of Gly, and a strongly hydrophobic group with higher values of Val and Leu.

[Comparative study of partial amino acid sequences of prolamins and glutelins from various cereals. VII. Amino acid sequences of prolamin peptides].

The peptide fractions isolated from chymotryptic hydrolysates of wheat, rye and barley prolamines [this journal (1984) 178:173] were separated into pure peptides by high-performance liquid chromatography on octadecyl silica gel. The peptides which were most abundant were analyzed for amino acid composition and in part for amino acid sequence. Besides peptides which are typical for only one of the cereals investigated, peptides of similar composition were found in all three prolamines.