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Coexpression of binding sites for A(B) histo‐blood group trisaccharides with galectin‐3 and Lag antigen in human Langerhans cells
Author(s) -
Smetana Karel,
Holíková Zuzana,
Klubal Radek,
Bovin Nicolai V.,
Dvořánková Barbora,
Bartůňková Jiřina,
Liu FuTong,
Gabius HansJoachim
Publication year - 1999
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 - 10.1002/jlb.66.4.644
Subject(s) - birbeck granules , biology , langerin , glycoconjugate , antigen , antibody , galectin , lectin , immunology , microbiology and biotechnology , biochemistry , langerhans cell , dendritic cell
Galectin‐3 is an immunomodulatory protein with binding capacity for various glycoconjugates including IgE. It has been shown to be produced by epidermal keratinocytes and is present on the surfaces of skin Langerhans cells (LC). Therefore, it may have a role in the pathogenesis of various skin diseases, such as atopic dermatitis. To study the expression of galectin‐3 in LC, we used, in addition to specific antibodies, a panel of synthetic, carrier‐immobilized, specific oligosaccharides of the A‐ and B‐histo‐blood group, which are recognized by this lectin. In the mean time, Birbeck granules were visualized with an anti‐Lag antibody. The double labeling experiments showed a remarkable colocalization of signals for Lag antigen (Birbeck granules) and galectin‐3, as well as the binding sites for A‐ and B‐histo‐blood group trisaccharides. The specificity of the oligosaccharide binding was demonstrated by the lack of binding by Le c , Le d (H blood group antigen), and sLe x , which are not recognized by galectin‐3. These results suggest that galectin‐3 is present in Birbeck granules, where it retains reactivity for its glycoligands. J. Leukoc. Biol. 66: 644–649; 1999.