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.