Peptide-derived antagonists of the urokinase receptor. affinity maturation by combinatorial chemistry, identification of functional epitopes, and inhibitory effect on cancer cell intravasation.

@article{Ploug2001PeptidederivedAO,
  title={Peptide-derived antagonists of the urokinase receptor. affinity maturation by combinatorial chemistry, identification of functional epitopes, and inhibitory effect on cancer cell intravasation.},
  author={Michael Ploug and S{\o}ren {\O}stergaard and Henrik G{\aa}rdsvoll and Katherine A Kovalski and Claus Holst-Hansen and Adam Holm and Laura L. Ossowski and Keld Dan{\o}},
  journal={Biochemistry},
  year={2001},
  volume={40 40},
  pages={
          12157-68
        }
}
The high-affinity interaction between urokinase-type plasminogen activator (uPA) and its glycolipid-anchored receptor (uPAR) plays an important role in pericellular plasminogen activation. Since proteolytic degradation of the extracellular matrix has an established role in tumor invasion and metastasis, the uPA-uPAR interaction represents a potential target for therapeutic intervention. By affinity maturation using combinatorial chemistry we have now developed and characterized a 9-mer, linear… CONTINUE READING
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A flexible multidomain structure drives the function of the urokinase-type plasminogen activator receptor (uPAR).

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