Abstract
The aim of our work was to investigate thein vitro reactivity of gliadin peptides of natural and synthetic origin with various cell lines. We have found that all tested cell lines of human, mouse and rat origin were agglutinated by enzymically digested gliadin (peptic-tryptic-and peptic-tryptic pancreatic digest of α-gliadin) in a concentration dependent manner. In order to test the specificity of binding, inhibition studies were performed using a panel of sugars as well as natural and synthetic peptides derived from gliadin. We have found that among twelve tested sugars only fetuin and phosphomannan were able to inhibition by gliadin peptides and most of the saccharides suggests that agglutinating activity of gliadin is the result of a nonspecific binding of gliadin to the cell membrane.
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Abbreviations
- FFIII:
-
Frazer's fraction III
- PTP:
-
peptic-tryptic-pancreatic digest of α-gliadin
- PBS:
-
phosphate buffered saline
- BSA:
-
bovine serum albumin
- ConA:
-
concanavalin A
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Dedicated to Professor J. Šterzl on the occasion of his 70th birthday
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Castany, M.A.F., Kocna, P. & Tlaskalová-Hogenová, H. Binding of gliadin to lymphoblastoid, myeloid and epithelial cell lines. Folia Microbiol 40, 431–435 (1995). https://doi.org/10.1007/BF02814752
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DOI: https://doi.org/10.1007/BF02814752