They also play the largest positive role in increasing loaf volume, while showing the lowest weakening effects on dough strength [4] and [5]. Functional analysis in vitro [10] of such contributions to wheat flours by the α-gliadin protein subunit ACX71610 (encoded by GQ891685 and carrying an extra cysteine residue in the C-terminal unique domain II) has been confirmed. But recent advances in the study of the pathogenesis of celiac disease (CD), a T-cell-mediated

chronic inflammatory disease with an incidence as high as 1% in many populations and caused by a permanent intolerance of dietary gluten, have also revealed that the α-gliadins are the major initiators of CD [11], [12], [13] and [14]. Based on the available literature, a variety of gluten peptides with proven in vivo Onalespib manufacturer or in vitro activity have been identified in gliadins as well as glutenins; however, their relative importance differs [15]. Only five peptides, one (glia-γ1: QQPQQSFPQQQ) occurring in γ-gliadins and four (glia-α9: PFPQPQLPY, glia-α2: PQPQLPYPQPQLPY, glia-α20:

PFRPQQPYPQ, and glia-α: QGSFQPSQQ) in α-gliadins, are dominant, and are generally referred to as the immunodominant peptides. They have been shown to be recognized find more by T-cells from almost all CD patients, both children and adults, whereas T-cell responses to other gluten proteins are much less frequent and generally appear in young CD patients. Furthermore, they elicit a stronger T-cell response and their immune activity

is designated as +++ compared to the + of the other epitopes [16], [17], [18], [19], [20] and [21]. Comparative analysis [13] of the deduced amino acid sequences of the full-ORF α-gliadin genes derived from several diploid wheat species representing the ancestral A (Triticum monococcum), D (Aegilops tauschii) and potentially ancestral B (Aegilops speltoides) genome of hexaploid bread wheat indicates Vasopressin Receptor significant differences in the average lengths of the two glutamine repeats, as well as the occurrence of the four major T-cell peptides in α-gliadins, according to their genomic origin. The α-gliadins derived from the A genome almost invariably contain only glia-α9 and glia-α20 and carry a larger average number (27.7 ± 1.7) of glutamine residues in the glutamine repeat I than do the B (20.0 ± 3.4) and D (20.7 ± 1.1) genomes. The α-gliadins originating in the B genome usually lack such immunogenic peptides or contain only glia-α and carry a larger average number (18.8 ± 1.9) of glutamine residues in the second glutamine repeat than do the A (10.2 ± 0.6) and D (9.7 ± 1.4) genomes.