Biography
Biography: Rosa Peracaula Miro
Abstract
Altered glycosylation is one of the hallmarks of tumor cells and it is involved in each and every aspect of tumor progression. It affects cell surface carbohydrates and cellular and secreted glycoproteins, some of which may reach the bloodstream and be used as tumor markers 1. Our group has focused on the altered glycosylation of serum proteins in prostate and pancreatic cancer as potential tumor markers. We have described glycosylation changes of Prostate Specific Antigen (PSA) glycans, related to sialylation and fucosylation, in prostate cancer compared to Benign Prostate Hyperplasia and seminal plasma from healthy controls 2-5. In pancreatic cancer, we have described glycosylation changes on human pancreatic ribonuclease (RNase 1) and acute-phase proteins. An increase in core fucosylated structures in the N-glycan chains of RNase 1 6 and an increase of sialyl-Lewis x (SLex) and fucosylation of the acute-phase proteins ceruloplasmin and alpha-1-acid glycoprotein, respectively, were described and were found in advanced pancreatic cancer patients 7-9. These tumor associated glycan changes are currently being investigated in larger cohort of patients as cancer diagnostic or prognostic tools. The expression of the glycosyltransferases responsible for the synthesis of the tumor associated carbohydrate antigens such as SLex has been found deregulated in cancer. In particular, our group has focused on the study of sialyltransferases, which have received much attention recently as they are frequently up-regulated in cancer cells. We have described using in vitro and in vivo models the involvement of the α2,3-sialyltransferases ST3Gal III, and ST3Gal IV in key steps of pancreatic tumor progression processes, and have found that they are highly expressed in most pancreatic adenocarcinoma tissues10-12.