epsilon-(gamma-glutamyl)-lysine and Celiac-Disease

epsilon-(gamma-glutamyl)-lysine has been researched along with Celiac-Disease* in 2 studies

Other Studies

2 other study(ies) available for epsilon-(gamma-glutamyl)-lysine and Celiac-Disease

ArticleYear
Microbial transglutaminase treatment in pasta-production does not affect the immunoreactivity of gliadin with celiac disease patients' sera.
    Journal of agricultural and food chemistry, 2014, Jul-30, Volume: 62, Issue:30

    The effect of microbial transglutaminase (MTG)-treatment of pasta-dough on the immunoreactivity with celiac disease patient's sera has been investigated. Modification by MTG has been proven by determination of the MTG reaction product ε-(γ-glutamyl)lysine (3.63 μmol/g protein), which was not detectable in non-MTG-treated pasta. Antigenicity has been analyzed by immunoblotting and ELISA using gliadin-extracts from pasta and MTG-treated pasta. Immunoblotting showed that the antibody-population (antigliadin antibodies and antideamidated gliadin antibodies) of the sera is specific for every individual patient. Immunoblotting and ELISA showed that there is no difference in immunoreactivity of gliadin extracted from pasta and MTG-pasta. Recognition pattern and intensity in Western blot as well as antibody titer has also been identical even for sera with a high antideamidated gliadin antibody titer. These results indicate no difference between pasta-gliadin and MTG-pasta-gliadin and especially no increased deamidation in pasta-gliadin by MTG-treatment.

    Topics: Adolescent; Adult; Aged; Aged, 80 and over; Antibody Formation; Celiac Disease; Child; Child, Preschool; Dipeptides; Enzyme-Linked Immunosorbent Assay; Food Handling; Gliadin; Humans; Immunoblotting; Infant; Middle Aged; Streptomyces; Transglutaminases; Triticum; Young Adult

2014
Localization of tissue transglutaminase and N (epsilon)-(gamma) -glutamyl lysine in duodenal cucosa during the development of mucosal atrophy in coeliac disease.
    Virchows Archiv : an international journal of pathology, 2005, Volume: 446, Issue:6

    Expression and transamidation activity of tissue transglutaminase (tTG) may be involved in the morphological modifications leading to the mucosal atrophy observed in coeliac disease (CD). We aimed to investigate the localization of tTG within the duodenal mucosa during the development of villous atrophy. The localization and level of expression of N epsilon-(gamma-glutamyl) lysine isopeptides which could reflect the transamidation activity of tTG were also analyzed. tTG and N epsilon-(gamma-glutamyl) lysine were localized using an immunohistochemical technique on duodenal biopsies obtained from 75 patients with CD and 51 subjects with normal mucosa (control group). The number of cases displaying tTG-expressing cells in the basement membrane and lamina propria was significantly higher in CD patients than in the control group. Moreover, the intensity of tTG staining in these areas was higher in CD. In contrast, the number of biopsies with tTG-expressing enterocytes was significantly lower in CD than in the control group. There was no difference in N epsilon-(gamma-glutamyl) lysine between the two populations. Tissue transglutaminase was differently expressed in the various areas of the mucosa according to the stage of atrophy, whereas the localization and the intensity of the labelling of N epsilon-(gamma-glutamyl) lysine isopeptides did not show any modification. The preferential localization in the basement membrane and lamina propria may reflect the involvement of tTG in the development of mucosal atrophy in CD.

    Topics: Adolescent; Adult; Atrophy; Celiac Disease; Child; Child, Preschool; Dipeptides; Duodenum; Female; Humans; Immunohistochemistry; Infant; Intestinal Mucosa; Male; Middle Aged; Transglutaminases

2005