Identification of a Novel Hyaluronic Acid Binding Protein in Human Breast Cancer Using a Monoclonal Antibody

The ubiquitous hyaluronan has diverse biological roles in vertebrates. These include acting as a vital structural component of connective tissues, the formation of loose hydrated matrices that allow cells to divide and migrate (e.g. during development), cell-cell interaction and a role in intracellular signaling. The interaction between hyaluronan and its binding proteins HABP (Hyaladherins) are known to be directly associated with metastasis. Multiple HABP’s have been reported to play a vital role in carcinogenesis. In the present study we have developed a hybridoma and selected a clone H B C which recognized a very distinct molecular weight 11 2 2 protein of 57kDa from breast tumors by western blot. The affinity between the H B C mAb and HABP was 11 2 2 confirmed by reaction with biotinylated HA and competition with HA oligosaccharides. The blocking of the reaction between the H B C mAb and 57kDa antigen by HA oligosaccharides confirms that this antigen is a 11 2 2 hyaluronic acid binding protein and is different from all HABP’s that have been documented earlier.