Immunosuppressive networks mediated by galectins in cancer

MARIANA SALATINO

Beijin, China.

Congreso; 17th Reunión Anual de la IUIS 2019; 2019

IUIS

Enormous effort has been made to delineate the ?glycosylation signature? of the tumor microenvironment, which in general is altered, as compared with healthy tissues. Tumor-associated glycosylation is the result of the expression and activity of glycosyltransferases, glycosidases, and enzyme chaperons, not only in tumor cells, but also in tumor-associated stromal, endothelial, and immune cells. The multiple combinatorial possibilities of glycan structures expressed by neoplastic versus normal tissue provide vast potential for information displayed and open many therapeutic opportunities. The responsibility of deciphering the biological information encoded by glycome is partially assigned, to a highly conserved family of endogenous glycan-binding proteins or lectins, named galectins; whose expression and function are dysregulated in cancerous tissues. Galectins, a particularly Galectin-1, modulate biological processes as immune response, inflammation or tumor progression by interacting with glycosylated proteins in the cell surface or in the ECM, clustering receptors and activating signaling pathways. We have shown that tumor-derived Galectin-1 is a crucial modulator of cell migration and invasion, angiogenesis, and tumor?immune escape. In this talk, I will highlight recent findings on how galectin?glycan lattices control the dialogue between tumor and immune cells and how these interactions could be exploited for therapeutic purposes in cancer. Thus, targeting galectin-glycan interactions may halt tumor progression by simultaneously augmenting antitumor immunity and suppressing aberrant angiogenesis.