Processing of complex between urokinase and its type-2 inhibitor on the cell surface. A possible regulatory mechanism of urokinase activity
|Published in||FEBS Letters. 1993, vol. 323, no. 3, p. 279-284|
|Abstract||Complexes between the urokinase-type plasminogen activator (uPA) and its type-2 inhibitor (PAI-2) are bound by a cell-surface receptor for uPA and rapidly cleaved into two fragments of 70 and 22 kDa. The 70-kDa fragment contains the active site of uPA and PAI-2, while the 22-kDa species was identified as the amino terminal fragment of uPA, that binds specifically to the receptor. When the experiment is performed at 4 degrees C, both fragments remain bound to the cell surface and can be eluted by acid treatment. We therefore postulate that after the binding of the uPA-PAI-2 complex, a new binding site for the 70-kDa species becomes available. This additional binding favours the cleavage of the complex into the 70-and 22-kDa fragments; the 70-kDa species is endocytosed or released, while the 22-kDa fragment remains on the cell surface to prevent the binding of intact uPA.|
|Keywords||Cell Line — Cell Membrane/metabolism — Electrophoresis, Polyacrylamide Gel — Homeostasis — Humans — Molecular Weight — Plasminogen Activator Inhibitor 2/isolation & purification/ metabolism — Protein Binding — Receptors, Cell Surface/metabolism — Receptors, Urokinase Plasminogen Activator — Urokinase-Type Plasminogen Activator/isolation & purification/ metabolism|
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|RAGNO, P. et al. Processing of complex between urokinase and its type-2 inhibitor on the cell surface. A possible regulatory mechanism of urokinase activity. In: FEBS Letters, 1993, vol. 323, n° 3, p. 279-284. doi: 10.1016/0014-5793(93)81357-6 https://archive-ouverte.unige.ch/unige:9250|