Molekulare Physiologie und Pathobiochemie ausgewählter Magen ...

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ZIEL Molekulare Physiologie - Pathobiochemie Gliadin peptide fragment derived from gluten protein is presented by antigen-presenting cells with specific class II HLA-DQ alleles. Model of the gliadin peptide. Surface of HLA-DQ with bound gliadin peptide to red region. Hydrogen-bonding network in the HLA-DQ-gliadin complex
ZIEL Molekulare Physiologie - Pathobiochemie Gliadin is absorbed into the lamina propia and presented in conjunction with HLA-DQ2 or DQ8 cell-surface antigens by antigen-presenting cells, probably dendritic cells, to sensitized T cells expressing the α/β TT-cell cell receptor. Tissue transglutaminase deaminates gliadin peptides, generating acidic, negatively charged residues of glutamic acid from neutral glutamines (inset). Since negatively charged residues are preferred in positions 4,6, and 7 of the antigen-binding groove of HLA-DQ2, deaminated gliadin elicits a stronger T-cell response. These lymphocytes then activate other lymphocytes to generate cytokines, such as interferon-γ, interleukin-4, and tumor necrosis factor α (TNF- α), which damage the villi, resulting in enteritis. Induction of aberrant HLA class II cell-surface antigens on the enterocytes may permit these cells to present additional antigens to the sensitized lymphocytes (Westerberg et al.,2006).
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Molekulare Physiologie und Pathobiochemie ausgewählter Magen ...

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