Interaction of high-molecular-weight kininogen with endothelial cell binding proteins suPAR, gC1qR and cytokeratin 1 determined by surface plasmon resonance (BiaCore).

@article{Pixley2011InteractionOH,
  title={Interaction of high-molecular-weight kininogen with endothelial cell binding proteins suPAR, gC1qR and cytokeratin 1 determined by surface plasmon resonance (BiaCore).},
  author={Robin A. Pixley and Ricardo G. Espinola and Berhane Ghebrehiwet and Kusumam Joseph and A Kao and Khalil H Bdeir and Douglas B Cines and Robert W. Colman},
  journal={Thrombosis and haemostasis},
  year={2011},
  volume={105 6},
  pages={1053-9}
}
The physiologic activation of the plasma kallikrein-kinin system requires the assembly of its constituents on a cell membrane. High- molecular-weight kininogen (HK) and cleaved HK (HKa) both interact with at least three endothelial cell binding proteins: urokinase plasminogen activator receptor (uPAR), globular C1q receptor (gC1qR,) and cytokeratin 1 (CK1). The affinity of HK and HKa for endothelial cells are KD=7-52 nM. The contribution of each protein is unknown. We examined the direct… CONTINUE READING