Proprotein convertases promote processing of VEGF-D, a critical step for binding the angiogenic receptor VEGFR-2.

@article{McColl2007ProproteinCP,
  title={Proprotein convertases promote processing of VEGF-D, a critical step for binding the angiogenic receptor VEGFR-2.},
  author={Bradley K. McColl and Karri Paavonen and Tara Karnezis and Nicole C Harris and Natalia Davydova and Julie Rothacker and Edouard C Nice and Kenneth W. Harder and Sally Roufail and Margaret L. Hibbs and Peter A. W. Rogers and Kari Alitalo and Steven A Stacker and Marc G. Achen},
  journal={FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
  year={2007},
  volume={21 4},
  pages={1088-98}
}
Vascular endothelial growth factor (VEGF)-D is a secreted glycoprotein that induces angiogenesis and lymphangiogenesis. It consists of a central domain, containing binding sites for VEGF receptor-2 (VEGFR-2) and VEGFR-3, and N- and C-terminal propeptides. It is secreted from the cell as homodimers of the full-length form that can be proteolytically processed to remove the propeptides. It was recently shown, using adenoviral gene delivery, that fully processed VEGF-D induces angiogenesis in vivo… CONTINUE READING