| Autor: |
Stanton, Kimberly J., Frewin, Mary Beth, Gudewicz, Paul W. |
| Zdroj: |
Journal of Leukocyte Biology; April 1999, Vol. 65 Issue: 4 p515-522, 8p |
| Abstrakt: |
In this study, we have explored the mechanism for the desensitization of IL‐8‐mediated neutrophil chemotaxis by a cell‐binding fragment of fibronectin (120‐kDa FN). Preincubation of neutrophil suspensions with the 120‐kDa FN fragment resulted in a heterologous desensitization of IL‐8‐mediated chemotaxis while not affecting neutrophil chemotaxis to either fMLP or zymosan‐activated serum. Preincubation of neutrophils with the βx‐integrin‐activating antibody (TS2/16) mimicked the effects of the 120‐kDa FN fragment while preincubating neutrophils with the β1‐integrin blocking antibody (mAb13) abrogated the inhibitory effects of the 120‐kDa FN fragment on IL‐8‐mediated chemotaxis. Furthermore, we also demonstrated that the 120‐kDa FN fragment did not inhibit chemotaxis to the CXC chemokine MGSA/GROα which interacts with high affinity to the IL‐8 receptor B (CXCR2). By in vivophosphorylation of neutrophils and probing lysates with an anti‐CXCR1 antibody, we demonstrated that the addition of the cell‐binding fragment of fibronectin resulted in a time‐dependent phosphorylation of CXCR1. These findings suggest that the mechanism of heterologous desensitization of IL‐8‐mediated chemotaxis following ligation of FN‐dependent integrins is the result of phosphorylation of the CXCR1 receptor. J. Leukoc. Biol.65: 515–522; 1999. |
| Databáze: |
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