[HTML][HTML] Domain 2 of the urokinase receptor contains an integrin-interacting epitope with intrinsic signaling activity: generation of a new integrin inhibitor
B Degryse, M Resnati, RP Czekay, DJ Loskutoff… - Journal of Biological …, 2005 - ASBMB
We investigated the interaction between the urokinase receptor (uPAR) and the integrin
αvβ3. Vitronectin (VN) induces cell migration by binding to αvβ3, but expression of the uPAR
boosts its efficacy. Thus, uPAR may regulate VN-induced cell migration by interacting
laterally with αvβ3. In contrast, cells expressing a uPAR mutant lacking domain 2 do not
migrate in response to VN. This effect is overcome by D2A, a synthetic peptide derived from
the sequence of domain 2. In addition, D2A has chemotactic activity that requires αvβ3 and …
αvβ3. Vitronectin (VN) induces cell migration by binding to αvβ3, but expression of the uPAR
boosts its efficacy. Thus, uPAR may regulate VN-induced cell migration by interacting
laterally with αvβ3. In contrast, cells expressing a uPAR mutant lacking domain 2 do not
migrate in response to VN. This effect is overcome by D2A, a synthetic peptide derived from
the sequence of domain 2. In addition, D2A has chemotactic activity that requires αvβ3 and …