Adhesion of human breast carcinoma to extracellular matrix proteins is modulated by galectin-3.

Abstract

In this report, we have analyzed the adhesive interactions of a breast carcinoma cell line, BT-549, and its galectin-3-transfected subclone 11-9-1-4 with laminin, collagen IV and fibronectin. We determined that 11-9-1-4 cells adhered much more rapidly (within 1 h of plating) to laminin- and collagen IV-coated wells than the galectin-3 null expressing BT-549 cells. However, after 24 h, both cell lines fully adhered to laminin and collagen IV. Both cell lines also achieved maximum adhesion to fibronectin within 30 min. Not only did 11-9-1-4 express galectin-3 in the usual punctate pattern on its cell surface, it demonstrated a higher surface expression of alpha 6 beta 1 integrin compared to BT-549. The 11-9-1-4 cells were able to invade through matrigel-coated polycarbonate filters at approximately 3 times the rate of BT-549 parental cells. Our data suggest that galectin-3 is essential for adhesion to laminin and collagen IV but not fibronectin by breast carcinoma cells. In addition, galectin-3 expression may modulate the surface expression of some of the integrins specific for laminin and collagen IV adhesion and invasion of basement membrane by breast carcinoma cells.