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| It is unclear why only specific indiviudals produce this pathogenic and T-cell specific activation. Biochemically, HLA binding of gliadin peptides should be the same in celiac and non-celiac patients. These implications suggest an underlying genetic component (Maiuri, 2003). | | It is unclear why only specific indiviudals produce this pathogenic and T-cell specific activation. Biochemically, HLA binding of gliadin peptides should be the same in celiac and non-celiac patients. These implications suggest an underlying genetic component (Maiuri, 2003). |
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| == Disease == | | == Immune Response == |
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| === HLA-DQ2 === | | === HLA-DQ2 and HLA-DQ8 === |
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| === HLA-DQ8 === | | === Interactions === |
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| Background
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| When gliadin of the gluten complex makes contact with the intestinal lumen, specifically the transglutaminase tissue, the complex HLA-DQ8 is formed<ref>CECILIO, Lucila Arantes, & BONATTO, Mauro W.. (2015). THE PREVALENCE OF HLA DQ2 AND DQ8 IN PATIENTS WITH CELIAC DISEASE, IN FAMILY AND IN GENERAL POPULATION. ABCD. Arquivos Brasileiros de Cirurgia Digestiva (São Paulo), 28(3), 183-185. https://dx.doi.org/10.1590/S0102-67202015000300009</ref>. This complex is comprised of three chains, two being MHC class II antigens of alpha helical and beta sheet nature with the third being the gluten peptide. The MHC class II molecule HLA-DQ8 is one of the two human leukocyte antigens associated the genetic risk of developing celiac disease and serves as a MHC class II molecule in the immune system of the body. The molecular basis of how HLA-DQ8 causes celiac disease differs from that of HLA-DQ2, however the underlying mechanisms of how it causes celiac disease are not well understood.
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| Interactions | | Interactions |