

Other version: http://jcb.rupress.org/content/111/2/783.full.pdf
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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 |
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Published in | The Journal of Cell Biology. 1990, vol. 111, no. 2, p. 783-792 | |
Abstract | 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. | |
Keywords | Cell Line — Cell Membrane/ultrastructure — Chemotaxis, Leukocyte — Enzyme Precursors/ genetics — Humans — Kinetics — Microscopy, Electron — Monocytes/ physiology/ultrastructure — Plasminogen Activators/ genetics/metabolism — Plasminogen Inactivators/metabolism — Receptors, Cell Surface/ physiology/ultrastructure — Receptors, Urokinase Plasminogen Activator — Urokinase-Type Plasminogen Activator/ genetics/metabolism | |
Identifiers | PMID: 2166055 | |
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Citation (ISO format) | ESTREICHER, A. et al. 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. In: The Journal of Cell Biology, 1990, vol. 111, n° 2, p. 783-792. doi: 10.1083/jcb.111.2.783 https://archive-ouverte.unige.ch/unige:8738 |