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J. Biol. Chem., Vol. 269, Issue 4, 2411-2418, 01, 1994
SW Lee, V Ellis and DA Dichek
The characteristics of plasminogen activation by
glycosylphosphatidylinositol (GPI)-anchored urokinase were evaluated and
compared with those reported previously for receptor-bound urokinase. When
expressed in cultured bovine aortic endothelial cells, GPI anchoring of
single-chain urokinase plasminogen activator (scu-PA) potentiated plasmin
generation as compared with GPI-anchored scu-PA that had been released into
solution from the cell surface by enzymatic cleavage of the GPI anchor
("released" scu-PA). The potentiation of plasmin generation by GPI-anchored
scu-PA was inhibited in a dose- dependent manner by 6-aminohexanoic acid, a
lysine analog, suggesting that the augmentation of plasmin generation by
GPI-anchored scu-PA was dependent on simultaneous binding of plasminogen to
the cell surface. GPI-anchored two-chain urokinase (tcu)-PA cleaved a
peptide substrate at a rate equivalent to that of released urokinase.
However, at a plasminogen concentration of 0.5 microM, GPI-anchored tcu-PA
activated plasminogen less rapidly than did released urokinase. Modeling of
kinetics of individual reactions revealed that cell-associated plasminogen
activation by GPI-anchored tcu-PA was characterized by a Km of
approximately 0.15 microM. This value of Km was 70-fold below that for
activation of solution plasminogen by GPI-anchored urokinase. There was a
concomitant decrease in Vmax for plasminogen activation by anchored tcu-PA.
These alterations in kinetic parameters are similar to those reported
previously for the activation of plasminogen by receptor- bound tcu-PA. In
addition, GPI-anchored tcu-PA exhibited a modest resistance to plasminogen
activator inhibitor 1 inactivation. The enzymatic characteristics of
GPI-anchored urokinase reported here resemble closely those reported
previously for receptor-bound urokinase. These data suggest that the
urokinase receptor may regulate plasmin generation through a relatively
nonspecific localization of urokinase to the cell surface rather than
through any intrinsic property of the urokinase receptor.
Characterization of plasminogen activation by glycosylphosphatidylinositol-anchored urokinase
Molecular Hematology Branch, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892.
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