The urokinase-type plasminogen activator receptor mediates tyrosine phosphorylation of focal adhesion proteins and activation of mitogen-activated protein kinase in cultured endothelial cells.

@article{Tang1998TheUP,
  title={The urokinase-type plasminogen activator receptor mediates tyrosine phosphorylation of focal adhesion proteins and activation of mitogen-activated protein kinase in cultured endothelial cells.},
  author={Hua Tang and David M Kerins and Qin Hao and Tadashi Inagami and Douglas E. Vaughan},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 29},
  pages={18268-72}
}
Urokinase-type plasminogen activator (uPA) binds to cells via a specific glycosylphosphatidylinositol-anchored receptor. Although occupancy of the uPA receptor (uPAR) has been shown to alter cellular function and to induce gene expression, the signaling mechanism has not been characterized. Urokinase induced an increase in the tyrosine phosphorylation of multiple proteins in bovine aortic endothelial cells. In contrast, low molecular weight uPA did not induce this response. Analysis by… CONTINUE READING

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PTK2 protein, humanGene product plays role in biological processTyrosine Phosphorylation
Analysis by immunoblotting demonstrated tyrosine phosphorylation of focal adhesion kinase ( FAK ) , the focal adhesion - associated proteins paxillin and p130(cas ) , and mitogen - activated protein kinase ( MAPK ) following the occupancy of the uPAR by uPA .
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