The cell surface hyaluronate binding sites of invasive human bladder carcinoma cells.
High-affinity, cell surface binding sites for hyaluronate were demonstrated on highly invasive human bladder carcinoma cells. These binding sites were shown to be specific for hyaluronate, saturable and exhibit a Km of 0.94 x 10(-9) M and a Bmax of 65 ng hyaluronate/10(6) cells. The binding of [3H]hyaluronate to a fixed cell-affinity column was competed with unlabeled hyaluronate and hyaluronate-hexasaccharide but not with hyaluronate-tetrasaccharide, chondroitin sulfate, heparin or non-sulfated dextran. Pre-treatment of cells with protease destroyed the binding activity whereas pretreatment with Streptomyces hyaluronidase to reveal occupied binding sites had no effect. No hyaluronate-binding activity was observed on normal human fibroblasts.
D001667:Binding, Competitive; D002295:Carcinoma, Transitional Cell / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D006025:Glycosaminoglycans / Q000378:metabolism; D006801:Humans; D018960:Hyaluronan Receptors; D006820:Hyaluronic Acid / Q000378:metabolism*; D006821:Hyaluronoglucosaminidase / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000494:pharmacology; D011956:Receptors, Cell Surface / Q000378:metabolism*; D014407:Tumor Cells, Cultured; D001749:Urinary Bladder Neoplasms / Q000378:metabolism*
D006025:Glycosaminoglycans; D018960:Hyaluronan Receptors; D011956:Receptors, Cell Surface; D006820:Hyaluronic Acid; D006821:Hyaluronoglucosaminidase; D010447:Peptide Hydrolases