| Autor: |
Furlan F; Department of Molecular Biology and Functional Genomics, San Raffaele Scientific Institute, Milan, 20132, Italy., Orlando S, Laudanna C, Resnati M, Basso V, Blasi F, Mondino A |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of cell science [J Cell Sci] 2004 Jun 15; Vol. 117 (Pt 14), pp. 2909-16. Date of Electronic Publication: 2004 Jun 01. |
| DOI: |
10.1242/jcs.01149 |
| Abstrakt: |
We have previously shown that chymotrypsin-cleaved soluble uPAR (D2D3(88-274)) elicits migration of monocytic cells through interaction with FPRL-1, a G protein-coupled receptor that is homologous to the fMLP receptor. Here, we report that D2D3(88-274) also modulates the ability of monocytes to migrate in response to other chemokines. Pretreatment of monocytes with increasing amounts of D2D3(88-274) prevents cell migration in response to MCP-1, RANTES and fMLP. We demonstrate that D2D3(88-274) does not inhibit MCP-1 receptor binding, elicit CCR2 internalization and prevent MCP-1-induced intracellular Ca(2+) increase. Thus, CCR2 receptor desensitization cannot account for D2D3(88-274)-mediated inhibition of MCP-1-induced cell migration. Rather, we show that pretreatment of monocytes with D2D3(88-274) dramatically decreases chemokine-induced integrin-dependent rapid cell adhesion by interacting with FPRL-1. Together, our results indicate that chemokine-dependent cell migration can be regulated not only by homologous and heterologous receptor desensitization, but also by inhibition of integrin-dependent cell adhesion, an important step in cell transmigration. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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