DISTINCTIVE GLYCOSYLATION SIGNATURE AND GALECTIN-1 EXPRESSION IN DIFFERENT HUMAN BREAST CANCER LINES AND TISSUES

DALOTTO-MORENO T; MARIÑO KV; SALATINO M; PERROTA RM; CAGNONI A; RABINOVICH GA; MOSES F; CROCI DO

Congreso; Reunion Anual de la SAIC-SAI-SAFE; 2016

Galectins can influence antitumor immune response, cell survival, angiogenesis and tumor metastasis by interacting with cells surface glycans. It was shown that transformed cells experience changes in glycosylation which are sensed by lectins and can be used as disease biomarkers. With the main goal of studying galectin-glycan interactions that may shape distinct breast cancer phenotypes, 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 six biotinylated lectins (Galectin-1 (Gal-1), LEL, SNA, PNA, PHA-L and MAA) and analyzed their binding to the cell surface by flow cytometry. We found that highly aggressive lines, as the triple negative MDA-MB-231 and the HER2 enriched Trastuzumab (TZ)-resistant JIMT-1, showed higher binding of Gal1 (p