GlcNAc-coated glycodendrimers, which are polyvalent glycomimetics, display strong in vitro affinity for the rat natural killer cell protein-1A (NKR-P1A), a C-type lectin-like receptor of natural killer (NK) cells in rats, humans and some strains of mice. Administration of these compounds in vivo results in a substantial increase in the antitumour activity with involvement of the natural cell immunity. To clarify the in vitro and in vivo fate of these molecules, we synthesized labelled glycodendron analogues of the previously studied glycodendrimers. Labelling with fluorescent tags enabled the localization of the glycodendrons in white blood cells, tumours and other tissues by using different imaging techniques such as fluorescence and confocal microscopy. These studies are useful for probing the mechanism of action and fate of artificial ligands and the cell receptors involved.
following a re-evaluation of controversial results of Professor K. Bezouska on NKR-P1 (rat and mouse receptors) interactions with carbohydrates, we need to correct some statements of this paper and the interpretation of some results consequent to these statements (which were based on published data by Professor K. Bezouska considered still valid at the time of preparation and publication of this paper).At present, we need to consider the following statment as erroneous:-the NKR-P1 receptor is a high affinity receptor for various oligosaccharides which were considered mimetics of putative ligands for this receptor (as previously reported in literature);-PAMAM-GlcNAc 8 glycodendrimer has high affinity and selectivity for the NKR-P1 receptor.Instead, the effects of PAMAM-GlcNAc 8 reported in this paper, modulating the tumor biology and immune response, have to be re-interpreted: as the result of not exclusive interaction of glycodendrimers with NKR-P1 receptor and NK cells but as the possible result of interactions with a wider panel of cells and recep-
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