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Activation of macrophages by gliadin fragments: isolation and characterization of active peptide
Author(s) -
Tučková Ludmila,
Novotná Jana,
Novák Petr,
Flegelová Zuzana,
Květoň Tomáš,
Jelínková Lenka,
Zídek Zdeněk,
Man Petr,
TlaskalováHogenová Helena
Publication year - 2002
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1189/jlb.71.4.625
Subject(s) - gliadin , peptide , biology , secretion , immune system , innate immune system , gluten , peptide sequence , microbiology and biotechnology , biochemistry , immunology , gene
Celiac disease, induced by dietary gluten, is characterized by mucosal atrophy and local inflammation associated with cell infiltration and activation. Unlike other food proteins, gluten and its proteolytic fragments, besides inducing a specific immune response, were shown to activate components of innate immunity and cause, e.g., direct stimulation of TNF‐α and IL‐10 and a significant rise in NO production by peritoneal macrophages. The identity of the active fragments was established by separating the peptic digest of gliadin by RP‐HPLC chromatography. The purest fraction with the highest activity was analyzed by mass spectrometry, and the gliadin peptide sequence was identified as VSFQQPQQQYPSSQ. This peptide (T) and its N‐ and C‐terminally shortened forms (A, B, C and D, E, F) were synthesized. Peptide B (FQQPQQQYPSSQ) elicited the highest TNF‐α, IL‐10, and RANTES secretion and increase in IFN‐γ‐primed NO production by mouse macrophages. In contrast, C‐terminally shortened peptides had a lower ability to stimulate macrophages than the native form.