Binding of gliadin to lymphoblastoid, myeloid and epithelial cell lines
Language English Country United States Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
8763158
DOI
10.1007/bf02814752
Knihovny.cz E-resources
- MeSH
- Adenocarcinoma pathology MeSH
- Leukemia, Basophilic, Acute pathology MeSH
- alpha-Fetoproteins pharmacology MeSH
- Cell Adhesion MeSH
- Burkitt Lymphoma pathology MeSH
- Leukemia, Myelogenous, Chronic, BCR-ABL Positive pathology MeSH
- Gliadin metabolism MeSH
- Platelet Membrane Glycoproteins * MeSH
- Embryonal Carcinoma Stem Cells MeSH
- Rats MeSH
- L Cells MeSH
- Lectins MeSH
- Humans MeSH
- Lymphocytes metabolism MeSH
- Lymphoma pathology MeSH
- Macrophages metabolism MeSH
- Mannans pharmacology MeSH
- Molecular Sequence Data MeSH
- Mice MeSH
- Tumor Cells, Cultured MeSH
- Neoplastic Stem Cells metabolism MeSH
- Maxillary Neoplasms pathology MeSH
- Colonic Neoplasms pathology MeSH
- Peptides pharmacology MeSH
- Receptors, Cell Surface metabolism MeSH
- Carbohydrates pharmacology MeSH
- Amino Acid Sequence MeSH
- Teratocarcinoma pathology MeSH
- Platelet Glycoprotein GPIb-IX Complex * MeSH
- Dose-Response Relationship, Drug MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Humans MeSH
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- alpha-Fetoproteins MeSH
- Gliadin MeSH
- glycoprotein receptor GPIb-IX MeSH Browser
- Platelet Membrane Glycoproteins * MeSH
- Lectins MeSH
- Mannans MeSH
- Peptides MeSH
- phosphomannan MeSH Browser
- Receptors, Cell Surface MeSH
- Carbohydrates MeSH
- Platelet Glycoprotein GPIb-IX Complex * MeSH
The aim of our work was to investigate the in 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 alpha-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 inhibit the agglutination of K562 cells with peptic-tryptic- but not with peptic-tryptic pancreatic digest of alpha-gliadin. The lack of 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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