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: Baseras, Billur (Author) , Gaida, Matthias (Author) , Kahle, Nadine (Author) , Schuppel, Ann-Kathrin (Author) , Kathrey, Diana (Author) , Prior, Birgit (Author) , Wente, Moritz N. (Author) , Hänsch, Gertrud Maria (Author)
Format: Article (Journal)
Language:English
Published: 2012
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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