Epididymal protein ASF is a d-galactose-specific lectin with apoptotic effect on human breast cancer cell line MCF7

• Epididymal ASF at a specified condition acts as a d-galactose specific lectin.
• At the same condition ASF shows strong affinity for ECM protein fibronectin.
• Binding with fibronectin ASF block fibronectin-MCF7 interaction.
• Inhibiting MCF7 adhesion ASF promote adhesion dependent apoptosis to MCF7.

Isolated caprine epididymal plasma glycoprotein “anti sticking factor” (ASF) interacts with caudal sperm surface in a d-galactose dependent manner. ASF acts as a Ca2+ dependent soluble lectin principally activated in acidic pH. As a d-galactose specific lectin, it has a specific affinity for fibronectin as well as fibronectin receptor, i.e. integrins α5β3 and α5β1. By virtue of this particular property, it hampers the in vitro adhesion of the adherent breast cancer cell MCF7 with fibronectin. The effective anti-adhesive concentration of ASF promotes p53 dependent apoptosis in MCF7, which was established by Hoechst 33342 staining, DNA fragmentation assay, FITC tagged Annexin-V flowcytometry and western blot analysis. We suggest that ASF inhibits fibronectin–integrin interactions by binding with them and induces adhesion dependent apoptosis on adherent MCF7.