Abstract
Radiolabeled pro-urokinase plasminogen activator (pro-uPA) was cross-linked to a specific protein on the surface of human monocyte-like U937 cells in a reaction catalyzed by tissue transglutaminase. The conjugate formed with this unknown component had a much higher molecular weight (apparent M(r) 250,000-300,000) than the complex of pro-uPA and the urokinase plasminogen activator receptor (uPAR). There was a strong preference for the pro-form of uPA. The conjugate was recognized by antibodies against uPA but not by anti-uPAR antibodies. Nevertheless, the blocking of uPAR with a monoclonal antibody abolished the formation of the conjugate, thus showing a role of uPAR in this process.
| Originalsprog | Engelsk |
|---|---|
| Tidsskrift | FEBS Letters |
| Vol/bind | 336 |
| Udgave nummer | 3 |
| Sider (fra-til) | 394-6 |
| Antal sider | 3 |
| ISSN | 0014-5793 |
| Status | Udgivet - 28 dec. 1993 |
| Udgivet eksternt | Ja |