Summary
Cell surface lectins have been characterized on monocytes, macrophages and tumor cells by using fluoresceinylated neoglycoproteins. Neoglycoproteins are obtained by substitution of bovine serum albumin with phenyldiazo-or phenylisothiocyanate- glycosides and contain about 20 sugar units. Endogenous lectins of these cells mediate binding and uptake of specific neoglycoproteins as shown by a quantitative assay based on flow cytofluorometry. Membrane lectins of monocytes, macrophages, Lewis lung carcinoma cells (3LL) and leukemic cells (L1210) bind and internalize preferentially neoglycoproteins containing 6-P-α-Man, α-Man and 6-P-α-Man, α-Glc and α-L-Fuc residues respectively. Neoglycoproteins may also be used to target toxic drugs. Membrane lectins are involved in cell adhesion as shown by in vitro and in vivo experiments with 3LL cells: the binding of 3LL cells to lung cells is mediated by the a-Glc-specific lectin of 3LL cells and by the α -L-Fuc specific lectin of lung cells. Monocytes and macrophages can be rendered tumoricidal by using neoglycoproteins carrying muramyldipeptide. This activator-neoglycoprotein conjugate allows to kill tumor cells in vitro and in vivo and to eradicate metastases in 3LL tumor-bearing mice upon tumor resection. In conclusion, membrane lectins on tumor cells and on myeloid cells could be used in the future, to target drugs leading to new antitumor therapies.
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Monsigny, M., Roche, A.C., Midoux, P., Kieda, C., Mayer, R. (1988). Endogenous Lectins of Myeloid and Tumor Cells: Characterization and Biological Implications. In: Gabius, HJ., Nagel, G.A. (eds) Lectins and Glycoconjugates in Oncology. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-73662-9_3
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