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Binding of the Galanthus nivalis Agglutinin to Thymocytes Reveals Alterations in Surface Glycosylation during T‐Cell Development
Author(s) -
Šinkora J.,
Kolínská J.,
Řeháková Z.,
Černý J.,
Doubravská L.
Publication year - 2002
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1046/j.1365-3083.2002.01047.x
Subject(s) - thymocyte , biology , peanut agglutinin , glycoprotein , microbiology and biotechnology , cd8 , monoclonal antibody , staining , flow cytometry , glycosylation , agglutinin , lectin , biochemistry , antibody , immunology , antigen , genetics
Surface binding of the Galanthus nivalis agglutinin (GNA) to thymocyte subsets has been studied in pigs and rodents by multicolour flow cytometry. In all the species examined, analogous staining profiles have been recorded. Counter‐staining with anti‐CD3ε, anti‐CD4 and anti‐CD8 monoclonal antibodies (MoAb) revealed that a significant increase of the GNA targets on the cell surface occurred during early thymocyte differentiation and reached its maximum at the level of the CD3 lo CD4 + CD8 + small cortical thymocyte. This was followed by a decrease in the GNA binding capacity upon terminal maturation to the single positive thymocytes. PAGE analysis has revealed a dominant GNA‐binding glycoprotein (molar mass approx. 90 kDa) present on thymocyte plasma membranes and absent on the surface of splenic lymphocytes, although both the whole cell lysates from both organs contained GNA ligands of the same size. Our findings are in agreement with previous data showing that immature thymocytes differ from their mature counterparts and peripheral T lymphocytes in the surface glycosylation pattern, and support the hypothesis that lectin–glycoprotein interaction plays a significant role in the cell‐to‐cell crosstalk in the thymic cortex.