Potential Role of Kringle-Integrin Interaction in Plasmin and uPA Actions (A Hypothesis)
Figure 4
Integrin-dependent plasminogen activation on the cell surface. Parental CHO cells and -CHO cells in wells of 96-well plates were treated with PIPLC to deplete uPAR, and incubated with wt or delta kringle () uPA in the cold binding buffer for 1 h at 4°C. The cells were washed with the binding buffer, and plasminogen activation was determined using Glu-plasminogen and SpectrozymePL chromogenic substrate at 37°C. We found that -CHO cells showed much higher ability to activate plasminogen in a manner dependent on the uPA added. Deletion of the kringle domain (with -uPA) markedly reduced the plasminogen activation on -CHO, indicating that and uPA-dependent plasminogen activation required the kringle domain of uPA. These results suggest that the binding of uPA kringle to integrin induces plasminogen activation [38].
