The receptor for urokinase type plasminogen activator polarizes expression of the protease to the leading edge of migrating monocytes and promotes degradation of enzyme inhibitor complexes
| Autor: | Lelio Orci, Jean-Dominique Vassalli, J. Muhlhauser, A. Estreicher, Jean-Louis Carpentier |
|---|---|
| Rok vydání: | 1990 |
| Předmět: |
Plasmin
Cell Membrane/ultrastructure Receptors Cell Surface Biology In Vitro Techniques Monocytes Cell Line Receptors Urokinase Plasminogen Activator Plasminogen Activators/ genetics/metabolism Plasminogen Activators Plasminogen Inactivators medicine Humans Receptor Urokinase ddc:616 Enzyme Precursors Cell Membrane Monocytes/ physiology/ultrastructure Cell Biology Articles Molecular biology Urokinase-Type Plasminogen Activator Urokinase receptor Chemotaxis Leukocyte Kinetics Microscopy Electron Enzyme Precursors/ genetics Plasminogen activator inhibitor-2 Plasminogen Inactivators/metabolism Urokinase-Type Plasminogen Activator/ genetics/metabolism Receptors Cell Surface/ physiology/ultrastructure Plasminogen activator Extracellular Matrix Degradation medicine.drug |
| Zdroj: | The Journal of Cell Biology The Journal of Cell Biology, Vol. 111, No 2 (1990) pp. 783-792 |
| ISSN: | 0021-9525 |
| Popis: | Receptor-bound urokinase-type plasminogen activator (uPA) remains associated to the surface of human monocytes for many hours. Monocytes induced to migrate in a chemotactic gradient of f-Met-Leu-Phe rapidly polarize their uPA receptors to the leading front of the cells. Receptor-bound enzyme can be inhibited by plasminogen activator inhibitor 2 (PAI-2), with a kinetics comparable to that determined for the free enzyme, and uPA/PAI-2 complexes can bind to the uPA receptor. In contrast to the active enzyme, the uPA/PAI-2 complex is rapidly cleared from the monocyte cell surface; this involves an initial cleavage of the complex at the cell surface, followed by endocytosis and degradation. These results indicate that the uPA receptor can function both to focus plasmin-mediated extracellular matrix degradation in front of migrating cells, and to target uPA/PAI-2 enzyme/inhibitor complexes for degradation; they suggest that this receptor is a key determinant in the control of uPA-catalyzed extracellular proteolysis. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|