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The urokinase receptor (uPAR) was discovered in 1985 and has been the subject of much recent research. This receptor is overexpressed on many tumour cells, and several mechanisms for its action in cancer have been proposed. uPAR mediates cell migration and invasion, cell adhesion and angiogenesis, and in tumours, it may promote tumour growth. The uPAR receptor binds various protein ligands that include uPA, vitronectin, and the serine proteinase plasmin. However, there are many gaps in our knowledge of how these interactions affect tumour cell biology. The uPAR receptor is a target for both antibody-based therapies and small-molecule inhibitors, and this review aims to provide an up-to-date summary of the advances in targeting uPAR. The uPAR-mediated signaling pathways have implications for both clinical diagnosis and treatment of cancer.Shedding of secreted mucins from cultured human tracheal epithelial cells.
The levels of glycoprotein mucins (MUC) in conditioned media from cultured human tracheal epithelial cells were measured by an enzyme-linked immunosorbent assay and a reversed-phase high performance liquid chromatographic method. By the enzyme-linked immunosorbent assay, the levels of MUC1, MUC2, and MUC5B in the conditioned media increased as a function of time. The same amount of MUC2 and MUC5B increased more rapidly than did MUC1, and the MUC2/MUC5B ratio increased. The MUC5B in the conditioned media was in a more complex form than that of MUC5AC, with the oligosaccharides ranging in size from 2.6 x 10(6) to 4.2 x 10(4) Da. The level of the MUC2 glycoprotein was increased by the addition of exogenous porcine pancreatic elastase. The 0b46394aab