Monitoring of in vitro deamidation of gliadin peptic fragment by mass spectrometry may reflect one of the molecular mechanisms taking place in celiac disease development
Language English Country Great Britain, England Media print
Document type Journal Article, Research Support, Non-U.S. Gov't
PubMed
12112756
DOI
10.1002/jms.305
Knihovny.cz E-resources
- MeSH
- Macrophage Activation drug effects MeSH
- Celiac Disease metabolism MeSH
- Gliadin analysis pharmacology MeSH
- Glutamine metabolism MeSH
- Spectrometry, Mass, Electrospray Ionization * MeSH
- Interleukin-10 metabolism MeSH
- Glutamic Acid metabolism MeSH
- Humans MeSH
- Molecular Sequence Data MeSH
- Guinea Pigs MeSH
- Oligopeptides analysis pharmacology MeSH
- Nitric Oxide metabolism MeSH
- Peptide Fragments analysis pharmacology MeSH
- Protein Processing, Post-Translational MeSH
- Protein Glutamine gamma Glutamyltransferase 2 MeSH
- GTP-Binding Proteins metabolism MeSH
- Amino Acid Sequence MeSH
- Sequence Analysis, Protein MeSH
- Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization * MeSH
- Tumor Necrosis Factor-alpha metabolism MeSH
- Transglutaminases metabolism MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Guinea Pigs MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Names of Substances
- Gliadin MeSH
- Glutamine MeSH
- Interleukin-10 MeSH
- Glutamic Acid MeSH
- Oligopeptides MeSH
- Nitric Oxide MeSH
- Peptide Fragments MeSH
- Protein Glutamine gamma Glutamyltransferase 2 MeSH
- GTP-Binding Proteins MeSH
- Tumor Necrosis Factor-alpha MeSH
- Transglutaminases MeSH
- VSFQQPQQQYPSSQ MeSH Browser
Celiac disease, a chronic disorder of the small intestine, is caused by dietary gluten and is characterized by villous atrophy and local inflammation associated with infiltration of B and T lymphocytes and/or macrophages into the intestinal wall. In genetically predisposed individuals, the infiltrating cells are activated by gluten, gliadin and their proteolytic fragments and produce chemokines, cytokines and reactive radicals. The sequence of one of the macrophage-stimulatory gliadin peptic fragment was determined by mass spectrometry (MS) as VSFQQPQQQYPSSQ. The role of tissue transglutaminase (tTG) in innate immunity stimulation was studied by mass spectrometric monitoring of sequence changes in this active peptide. Two sites of glutamine deamidation in this peptide were localized by high-resolution scanning in MS/MS mode in an ion trap. A single deamidation in the parent peptide led to the complete loss of its stimulatory effect on macrophages.
References provided by Crossref.org
Gliadin peptides activate blood monocytes from patients with celiac disease
