Duodenal Intraepithelial Lymphocytes of Children with Cow Milk Allergy Preferentially Bind the Glycan-Binding Protein Galectin-3

A breakdown in intestinal homeostasis results in inflammatory bowel diseases including coeliac disease and allergy. Galectins, evolutionarily conserved β-galactoside-binding proteins, can modulate immune-epithelial cell interactions by influencing immune cell fate and cytokine secretion. In this stu...

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Bibliographic Details
Published in:International journal of immunopathology and pharmacology 2009, Vol.22 (1), p.207-217
Main Authors: Mercer, N., Guzman, L., Rua, E. Cueto, Drut, R., Ahmed, H., Vasta, G.R., Toscano, M.A., Rabinovich, G.A., Docena, G.H.
Format: Article
Language:English
Subjects:
Binding Sites
Child, Preschool
Duodenum - chemistry
Duodenum - immunology
Female
Galectin 1 - analysis
Galectin 1 - metabolism
Galectin 3 - analysis
Galectin 3 - metabolism
Humans
Infant
Lymphocytes - metabolism
Male
Milk Hypersensitivity - etiology
Milk Hypersensitivity - immunology
Peanut Agglutinin - metabolism
Plant Lectins - metabolism
Ribosome Inactivating Proteins - metabolism
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Summary:A breakdown in intestinal homeostasis results in inflammatory bowel diseases including coeliac disease and allergy. Galectins, evolutionarily conserved β-galactoside-binding proteins, can modulate immune-epithelial cell interactions by influencing immune cell fate and cytokine secretion. In this study we investigated the ‘glycosylation signature’ as well as the regulated expression of galectin-1 and −3 in human duodenal samples of allergic and non-allergic children. Whereas galectin-1 was predominantly localized in the epithelial compartment (epithelial cells and intraepithelial lymphocytes) and the underlying lamina propria (T cells, macrophages and plasma cells), galectin-3 was mainly expressed by crypt epithelial cells and macrophages in the lamina propria. Remarkably, expression of these galectins was not significantly altered in allergic versus non-allergic patients. Investigation of the glycophenotype of the duodenal inflammatory microenvironment revealed substantial α2–6-linked sialic acid bound to galactose in lamina propria plasma cells, macrophages and intraepithelial lymphocytes and significant levels of asialo core 1 O-glycans in CD68+ macrophages and enterocytes. Galectin-1 preferentially bound to neutrophils, plasma cells and enterocytes, while galectin-3 binding sites were mainly distributed on macrophages and intraepithelial lymphocytes. Notably, galectin-3, but not galectin-1 binding, was substantially increased in intraepithelial gut lymphocytes of allergic patients compared to non-allergic subjects, suggesting a potential role of galectin-3-glycan interactions in shaping epithelial-immune cell connections during allergic inflammatory processes.
ISSN:0394-6320
2058-7384
DOI:10.1177/039463200902200123