Urokinase plasminogen activator cleaves its cell surface receptor releasing the ligand-binding domain.

@article{HyerHansen1992UrokinasePA,
  title={Urokinase plasminogen activator cleaves its cell surface receptor releasing the ligand-binding domain.},
  author={Gunilla H\oyer-Hansen and Ebbe R\onne and Helene Solberg and Niels Behrendt and Michael Ploug and Leif R\oge Lund and Vincent Ellis and Keld Dan\o},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 25},
  pages={18224-9}
}
The cellular receptor for urokinase-type plasminogen activator (uPAR) is a glycolipid-anchored three-domain membrane protein playing a central role in pericellular plasminogen activation. We have found that urokinase (uPA) can cleave its receptor between domains 1 and 2 generating a cell-associated uPAR variant without ligand-binding properties. In extracts of U937 cells there are two uPAR variants which after complete deglycosylation have apparent molecular masses of 35,000 and 27,000… CONTINUE READING