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(Journal of Leukocyte Biology. 2002;71:625-631.)
© 2002 by Society for Leukocyte Biology

Activation of macrophages by gliadin fragments: isolation and characterization of active peptide

Ludmila Tucková*, Jana Novotná*, Petr Novák*, Zuzana Flegelová{dagger}, Tomás Kveton*, Lenka Jelínková*, Zdenek Zídek{ddagger}, Petr Man* and Helena Tlaskalová-Hogenová*

* Institutes of Microbiology and
{ddagger} Pharmacology, Academy of Sciences of the Czech Republic, Prague; and
{dagger} Research Institute of Biopharmacy and Veterinary Drugs, Jílové, Czech Republic

Correspondence: Ludmila Tucková, Ph.D., Institute of Microbiology, Department of Immunology, Academy of Sciences of the Czech Republic, Vídenská 1083, 142 20 Prague 4, Czech Republic. E-mail: tuckova{at}biomed.cas.cz

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-{alpha} 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-{alpha}, IL-10, and RANTES secretion and increase in IFN-{gamma}-primed NO production by mouse macrophages. In contrast, C-terminally shortened peptides had a lower ability to stimulate macrophages than the native form.

Key Words: iNOS • celiac disease • IFN-{gamma} • TNF-{alpha}




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