Gliadin stimulates human monocytes to production of IL-8 and TNF-alpha through a mechanism involving NF-kappaB
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
15280021
DOI
10.1016/j.febslet.2004.06.057
PII: S0014579304008099
Knihovny.cz E-resources
- MeSH
- Cell Line MeSH
- Enzyme-Linked Immunosorbent Assay MeSH
- Gliadin pharmacology MeSH
- Interleukin-8 biosynthesis MeSH
- Kinetics MeSH
- Humans MeSH
- Monocytes drug effects immunology physiology MeSH
- NF-kappa B metabolism MeSH
- Ovalbumin pharmacology MeSH
- Peptide Fragments pharmacology MeSH
- Soybean Proteins pharmacology MeSH
- Triticum MeSH
- Amino Acid Sequence MeSH
- Tumor Necrosis Factor-alpha biosynthesis MeSH
- U937 Cells MeSH
- Check Tag
- Humans MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Gliadin MeSH
- Interleukin-8 MeSH
- NF-kappa B MeSH
- Ovalbumin MeSH
- Peptide Fragments MeSH
- Soybean Proteins MeSH
- Tumor Necrosis Factor-alpha MeSH
Wheat gliadin is the triggering agent in coeliac disease. In this study, we documented that proteolytic fragments of gliadin, in contrast to other food antigens, induced interleukin (IL)-8 and tumour necrosis factor-alpha (TNF-alpha) production and significantly increased interferon (IFN)-gamma-induced cytokine secretion in human monocytic line THP-1 cells. Stimulation with gliadin resulted in elevated phosphorylation of the IkappaBalpha molecule and increased NF-kappaB/DNA binding activity that was inhibited by sulfasalazine, l-1-tosylamido-2-phenylethyl chloromethyl ketone and pyrrolidine dithiocarbamate (PDTC). The activation pathway was shown to be independent of the CD14 molecule. Less mature U-937 monocytes responded to gliadin stimulation by low IL-8 secretion, TNF-alpha production was not detectable. We propose that gliadin-induced activation of monocytes/macrophages can participate in mechanisms leading to the impairment of intestinal mucosa in coeliac patients.
References provided by Crossref.org
Gliadin peptides activate blood monocytes from patients with celiac disease