Interestingly, we have further demonstrated that E-cadherin is a carrier of sialylation in the pancreatic cancer cell lines, being a target of modification by the ST3Gal III enzyme. In particular, an increase in a2,3-sialic acid and a decrease in a2,6-sialic acid was shown in the E-cadherin molecule of the ST3Gal III overexpressing cells. This specific modification of E-cadherin with terminal sialylated structures was concomitantly observed with alterations in cellular morphology together with alterations on E-cadherin cellular localization compared with control cells. In addition, these alterations could account for the observed decrease in cell-cell aggregation of the ST3Gal III transfectants together with their increased invasive potential. In PDAC clinical samples. E-cadherin expression was found in some tumor areas, with points of Ecadherin and SLex colocalization where a potential interface between both molecules could exist. In conclusion, we have demonstrated that the alteration of the membrane sialylation pattern of PDAC cells has a modulatory effect in the proper function of important membrane adhesive molecules such as a2b1 integrin and E-cadherin, influencing cell adhesion and invasion processes. In particular, increase in SLex and decrease in a2,6-sialic acid as a consequence of ST3Gal III transfection led to reduced cell-cell adhesiveness, and endowed the cells with a more invasive phenotype. Glycosylation of E-cadherin and a2b1 integrin molecules was also modified as a result of the ST3Gal III transfection, with impact in the modulation of their functions and thus underlying the observed differences in the adhesive and motile phenotype. Specifically, glycan Desloratadine changes in a2b1 integrin of ST3Gal III transfected cells were further shown to activate integrin-mediated signaling pathways through FAK phosphorylation and therefore contributing to increase cell migration. Glycosylation of proteins is a key process. Indeed, congenital disorders of glycosylation lead to severe dysfunction and disability. Maturation of glycoproteins in the Golgi apparatus requires hundreds of enzymes, known as AZD7687 Carbohydrate-Active Enzymes, and also chaperones that act through complex protein-protein interactions.