Glycosylation profile of diferent breast cancer cell lines and human breast carcinoma tissues

MOSES F; SALATINO M ; DALOTTO-MORENO T; RABINOVICH GA; PERROTA RM; MARIÑO KV

Villa Gral Belgrano

Congreso; 2nd Argentinean Symposium of Glycobiology GLICOAR 2016; 2016

Altered glycosylation have been associated with cancer progression, serving as important biomarkers of malignancy and providing novel opportunities for therapeutic intervention. With the main goal of studying the glycosylation profile of breast cancer; we first selected five human cell lines that model different types of human breast cancer. To identify specific glycan structures, we used a panel of seven biotinylated lectins (Gal-1, ECL, LEL, SNA, PNA, HPA and MAA) and analyzed their binding to the tumor cell surface by flow cytometry. We found that highly aggressive lines as the triple negative MDA-MB-231 and the HER2+ Trastuzumab resistant cell line JIMT-1 showed higher binding of Gal1, ECL and MAA and low SNA indicating abundant terminal LacNAc and an enriched α2-3 versus α2-6 sialylation. MDA-MB-231 also stained positively with LEL and PNA, reflecting poly-LacNAc extension and asialo-core 1-O-glycans. In contrast, SKBR3, BT474 and T47D cells lines bound lower Gal-1, ECL and LEL which indicates less poly-LacNAc abundancy. We then evaluate lectin binding to paraffin embedded human breast cancer sections by lectin-histochemistry. Interestingly, we observed a mutually opposed binding pattern of Gal1 and SNA in stroma and epithelial cells. We can conclude that each cancer cell line and tissue have a particular ?glycosylation signature?; whether this firm is associated with cancer progression or response to targeted therapies remains to be elucidated.