Role of tissue transglutaminase in gliadin binding to reticular extracellular matrix and relation to coeliac disease autoantibodies.

Journal article

On different tissue sections, binding of gliadin to reticular matrix components was observed which was Ca2+-dependent, inhibited by Cu2+ and Zn2+ ions, by putrescine, and by preincubation with antibodies against tissue transglutaminase (tTG) suggesting that binding of gliadin is mediated by tTG. tTG was able to bind to gliadin and fibronectin fixed to microplates. Furthermore, tTG mediated binding of gliadin to fibronectin coated to microplates. On tissue sections, treatment with sera contain...

Expand abstract

Authors: Uhlig, H; Osman, A; Tanev, I; Viehweg, J; Mothes, T

• Publication status: Published
• Journal: Autoimmunity
• Volume: 28
• Issue: 4
• Pages: 185-195
• Publication date: 1998-01-01
• DOI: 10.3109/08916939808995366
• EISSN: 1607-842X
• ISSN: 0891-6934
• Language: English
• Keywords: Animals; Rats; GTP-Binding Proteins; Reticulum; Autoantibodies; Rabbits; Extracellular Matrix; GTP Phosphohydrolases; Transglutaminases; Humans; Celiac Disease; Gliadin