Galectin-3 inhibits the chemotaxis of human polymorphonuclear neutrophils in vitro
In the recent years, the participation of the animal lectin galectin (gal)-3 in inflammation and in host defence mechanisms was extensively studied. In vivo studies implied – among others – a role of gal-3 in the recruitment of polymorphonuclear neutrophils (PMN) to sites of bacterial infection. In...
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| Main Authors: | , , , , , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
2012
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| In: |
Immunobiology
Year: 2012, Volume: 217, Issue: 1, Pages: 83-90 |
| ISSN: | 1878-3279 |
| DOI: | 10.1016/j.imbio.2011.07.031 |
| Online Access: | Verlag, Volltext: http://dx.doi.org/10.1016/j.imbio.2011.07.031 Verlag, Volltext: http://www.sciencedirect.com/science/article/pii/S0171298511001720 
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| Author Notes: | Billur Baseras, Matthias M. Gaida, Nadine Kahle, Ann-Kathrin Schuppel, Diana Kathrey, Birgit Prior, Moritz Wente, Gertrud Maria Hänsch |
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| 520 | |a In the recent years, the participation of the animal lectin galectin (gal)-3 in inflammation and in host defence mechanisms was extensively studied. In vivo studies implied – among others – a role of gal-3 in the recruitment of polymorphonuclear neutrophils (PMN) to sites of bacterial infection. In that context, we asked the question whether gal-3 was chemotactic for PMN. Functional assays revealed that gal-3 was not chemotactic for PMN, but that it inhibited the spontaneous migration and the chemotaxis of PMN towards complement C5a, interleukin (IL)-8, or ATP. Moreover, gal-3 inhibited the shape change and the actin polymerisation of PMN that occurs in response to C5a or IL-8. By use of FITC-labelled gal-3, we found that it attached rapidly to the PMN membrane in a lactose-sensitive manner. In response to gal-3 the MAP kinase p38 was phosphorylated. This kinase is crucial for the migration of PMN towards end-target chemokines, such as C5a, and is activated in response to C5a or IL-8. When PMN were preincubated with gal-3, the C5a-induced p38 phosphorylation was transiently enhanced, but eventually down-modulated. We conclude that by interfering with the chemokine-induced p38 phosphorylation gal-3 inhibits chemotaxis of PMN. | ||
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