Pancreatic ductal adenocarcinoma is the fourth leading cause of BMS-690514 cancer death, with a 5-year survival rate of less than 5%. This extremely poor outcome is mainly due to its aggressiveness and delay in diagnosis, since approximately 85% of patients are diagnosed at advanced stages of disease, when metastasis is already present. Therefore, there is an urgent need to identify the underlying molecular mechanisms of PDAC, envisioning potential clinical applications. PDAC is characterized by an intense desmoplastic response, suggesting a role for ECM cell adhesion molecules, such as integrins, throughout the tumorigenic process. A number of reports have described the up-regulation and delocalization of several integrin subunits, including a1, a2, a3 and a6 subunits in pancreatic cancer. Furthermore, b1 BTB06584 integrins have been reported to play an essential role in promoting adhesion and invasion of pancreatic carcinoma and, in the case of a2b1 integrin, in mediating the malignant phenotype on type 1 collagen in pancreatic cancer cell lines. On the other hand, downregulation or inactivation of Ecadherin expression has also been associated with poor survival and acquisition of invasiveness, as well as dedifferentiation of PDAC. Glycosylation is one of the most important protein posttranslational modification and tumor cells frequently display an altered pattern of cell surface glycosylation in relation to their normal counterparts, which directly influences several cellular processes, including cell-cell adhesion and cell-ECM interaction. In particular, several pancreatic adenocarcinoma cells have been described to exhibit an increase in the expression of the Lewis-type sialylated epitopes sialyl-Lewis a and sialyl-Lewis x and the correspondent glycosyltransferases involved in their biosynthesis, which have been correlated with PDAC invasiveness and metastasis. Furthermore, several studies have reported that N-glycans influence the stability of AJ and E-cadherin biological functions in a variety of tumors. In addition, integrins are also carriers of N-glycans, and changes in glycan branching and sialylation of integrins have been reported to influence integrin binding to ECM and cell migration capabilities although the mechanisms underlying these actions are still unknown.