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To study lectin-mediated phagocytosis of apoptotic bodies by THP-1 cells, an inhibitory phagocytosis assay was performed. Presence of cognate β-galactoside-related epitopes within a polysaccharide chain or its branch will not automatically establish binding properties, and structural constellations lacking galactosides, like rhamnan, were found to be active. All the blood group related antigens A, H, Lewis a, Lewis x, Lewis b, and Lewis y, had their expression strongly diminished on apoptotic cells. Hydrophobic-interaction chromatography on the Butyl-WPG promotes the better resolution of nonactive contaminants from the active lectin. Using a cell-based assay and probing galectin reactivity with a panel of fluorescent neoglycoconjugates glycoprobes , its glycan-binding profile was determined.

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Having introduced and validated a cell assay, the comprehensive profiling of ligand binding to cell-surface-presented galectins is made possible. The carbohydrate specificity of the lectins was assayed by hemagglutination inhibition using mono- and oligosaccharides. Two step affinity chromatography provides high purification factor ofthe yield of SL1 and SL2 being 6. Some general and specific properties of these new materials and models as well as examples of their applications are discussed.




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In flow cytometry assays, the fluorescein probes demonstrated a specific binding to the lectin-transfected cells that was inhibited by unlabeled carbohydrate ligands. A similarly built digoxigenin-labeled probe was significantly better. Glycoparticles prepared by immobilization of glycoconjugates on magnetic beads are convenient for isolation of a particular cell population, expressing carbohydrate-binding molecules. Chicken galectins CG-1A and -2 as well as human galectins HGal-1 and -8 promote virus binding in dose dependent manner, but they do not influence the internalization stage. Under the condition of the cell assay, selectivity among oligosaccharides for the lectins was higher, and extraordinary affinity of galectin-1 to 3'-O-sulfated probes in a solid-phase assay was lost in the cell assay. Localization of lectins is visualized by labeling of cells with fluorescein-tagged glycoprobes, Glyc-PAA-fluo, in combination with fluorescent microscopy techniques.


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We have recently shown that the carbohydrate-binding pattern of galectins in cells differs from that determined in artificial non-cellular test-systems. The glycan-binding profile was shown to be influenced by glycocalix of the cell, where the galectin is anchored. In addition, the role of siglecs in engulfment of apoptotic bodies by tumor-associated macrophages was studied.


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Two step affinity chromatography provides high purification factor ofthe yield of SL1 and SL2 being 6. The probes for cell studies should correspond to enormously strict requirements in respect of nonspecific interaction with cell components and matrix. Gal beta GAlNAc beta as a trigger of anti-tumor macrophage activity.



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