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Papers In Press, published online ahead of print August 19, 2002
Institute of Immunology, VIRCC, Vienna A-1235
Corresponding Author: hannes.stockinger{at}univie.ac.at
Leukocyte migration to sites of inflammation is a multistep process involving transient adhesion to the endothelium followed by cell surface-controlled proteolysis for transmigration through the vessel wall and chemotactic movement within tissues. One of the key players in this machinery appears to be the uPA/uPA-R system. The role of uPA (urokinase–type plasminogen activator) and its receptor uPA-R (CD87) in plasminogen (Plg) activation, cell adhesion and chemotaxis is well established, however, less is known of how these activities are regulated. Here we provide evidence that the mannose 6-phosphate/insulin-like growth factor 2 receptor (M6P/IGF2-R, CD222) controls CD87-mediated functions. Expression of human CD222 in CD222-/- mouse fibroblasts downregulated Plg activation, cell adhesion and chemotaxis induced by the uPA/CD87 system. In addition, we demonstrate that the N-terminal region of CD222, which is similar to the Plg-binding site of streptokinase, plays a crucial role in binding of CD87 and Plg. A peptide derived from this region in CD222 is able to disrupt the physical interaction of CD222 with CD87 and, furthermore, mimics the inhibitory effects of CD222 on CD87 functions. Taken together, our results indicate a novel role for CD222 in regulation of fibrinolysis, cell adhesion and migration.
J. Biol. Chem, 10.1074/jbc.M207979200
Submitted on August 5, 2002
Revised on August 19, 2002
Accepted on August 19, 2002
The N-terminus of mannose 6-phosphate/Insulin-like growth factor 2 receptor in regulation of fibrinolysis and cell migration
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