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 - PubMed (original) (raw)

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

A Estreicher et al. J Cell Biol. 1990 Aug.

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.

PubMed Disclaimer

Cited by

Regulation of cell signalling by uPAR.
Smith HW, Marshall CJ. Smith HW, et al. Nat Rev Mol Cell Biol. 2010 Jan;11(1):23-36. doi: 10.1038/nrm2821. Nat Rev Mol Cell Biol. 2010. PMID: 20027185 Review.
Chondrocyte moves: clever strategies?
Morales TI. Morales TI. Osteoarthritis Cartilage. 2007 Aug;15(8):861-71. doi: 10.1016/j.joca.2007.02.022. Epub 2007 Apr 30. Osteoarthritis Cartilage. 2007. PMID: 17467303 Free PMC article. Review.
Urokinase plasminogen activator inhibits HIV virion release from macrophage-differentiated chronically infected cells via activation of RhoA and PKCε.
Graziano F, Elia C, Laudanna C, Poli G, Alfano M. Graziano F, et al. PLoS One. 2011;6(8):e23674. doi: 10.1371/journal.pone.0023674. Epub 2011 Aug 17. PLoS One. 2011. PMID: 21858203 Free PMC article.
Proteolytic cleavage of the urokinase receptor substitutes for the agonist-induced chemotactic effect.
Resnati M, Guttinger M, Valcamonica S, Sidenius N, Blasi F, Fazioli F. Resnati M, et al. EMBO J. 1996 Apr 1;15(7):1572-82. EMBO J. 1996. PMID: 8612581 Free PMC article.

References

1. Nature. 1970 Aug 15;227(5259):680-5 - PubMed
1. Biochem Biophys Res Commun. 1967 Nov 30;29(4):508-14 - PubMed
1. J Clin Invest. 1978 Apr;61(4):1057-70 - PubMed
1. J Cell Physiol. 1978 Sep;96(3):361-9 - PubMed
1. J Clin Invest. 1979 Jun;63(6):1249-61 - PubMed

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 - PubMed (original) (raw)