Galectin-3 regulates the adhesive interaction between breast carcinoma cells and elastin.

Galectin-3 is a beta-galactoside binding lectin whose precise physiological role is not yet defined. In the present studies, we questioned whether galectin-3 plays a role in the adhesion of breast carcinoma cells to elastin. The impetus for this analysis was the initial observation that the cellular receptor for elastin, the 67 kDa elastin/laminin protein may have galectin-like properties (Mecham et al. [1989] J. Biol. Chem. 264:16652-16657). We therefore analyzed the adhesion of breast carcinoma cells to microtiter wells coated with elastin under conditions which eliminate integrin participation in adhesion. The adhesion assay was done in the absence and presence of purified recombinant galectin-3. We hereby demonstrate that high concentrations of galectin-3 ligate breast carcinoma cells to microtiter wells coated with elastin. Galectin-3 also demonstrated a specific binding interaction with purified elastin in a dose and lactose dependent manner. Furthermore we demonstrated by immunoprecipitation that endogenous galectin-3 in breast carcinoma cells is associated with tropoelastin. Lastly, the breast carcinoma cells which expressed galectin-3 on their surface, demonstrated enhanced cellular proliferation on elastin compared to galectin-3 null expressing cells. These studies suggest that galectin-3 is capable of regulating the interactions between cells and elastin.