N-glycosylation profile of Activated Leukocyte Cell Adhesion Molecule (ALCAM/CD166) dictates its selective binding to Galectin-8

CAGNONI, ALEJANDRO J; FERNANDEZ, MARISA M; FERRAGUT, FATIMA; MALCHIODI, EMILIO L.; RABINOVICH, GABRIEL A.; ELOLA, MARIA TERESA; MARIÑO, KARINA VALERIA

Villa General Belgrano, Cordoba

Simposio; Segundo Simposio Argentino de Glicobiologia GlycoAr 2016; 2016

IBYME/ CIQUIBIC/ Fundacion Leloir

Activated leukocyte cell adhesion molecule (ALCAM/CD166) is a member of the immunoglobulin superfamily, primary involved in cell-cell adhesion, and it has been proposed as a potential novel cancer indicator and therapeutic target. ALCAM can interact with galectin-8 (Gal-8), a tandem-repeat type galectin. Surface plasmon resonance (SPR) studies revealed differential Gal-8 binding affinity towards endogenous ALCAM isolated from MDA-MB-231 breast cancer cells (ALCAMend) and human recombinant ALCAM expressed in HEK-293 cells (ALCAMrec). We compared the N-glycosylation profile for ALCAMend and ALCAMrec in order to identify structural differences influencing Gal-8 selective interactions.