BINDING OF GLIADIN TO LYMPHOBLASTOID, MYELOID AND EPITHELIAL-CELL LINES

The aim of our work was to investigate the in vitro reactivity of glia din peptides of natural and synthetic origin with various cell lines. We have found that all tested cell lines of human, mouse and rat origi n were agglutinated by enzymically digested gliadin (peptic-tryptic- a nd peptic-tryptic pancreatic digest of alpha-gliadin) in a concentrati on dependent manner. In order to test the specificity of binding, inhi bition studies were performed using a panel of sugars as well as natur al and synthetic peptides derived from gliadin. We have found that amo ng twelve tested sugars only fetuin and phosphomannan were able to inh ibit the agglutination of K562 cells with peptic-tryptic- but not with peptic-tryptic pancreatic digest of alpha-gliadin. The lack of inhibi tion by gliadin peptides and most of the saccharides suggests that agg lutinating activity of gliadin is the result of a nonspecific binding of gliadin to the cell membrane.