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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Hauptverfasser: Baseras, Billur (VerfasserIn) , Gaida, Matthias (VerfasserIn) , Kahle, Nadine (VerfasserIn) , Schuppel, Ann-Kathrin (VerfasserIn) , Kathrey, Diana (VerfasserIn) , Prior, Birgit (VerfasserIn) , Wente, Moritz N. (VerfasserIn) , Hänsch, Gertrud Maria (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 2012
In: Immunobiology
Year: 2012, Jahrgang: 217, Heft: 1, Pages: 83-90
ISSN:1878-3279
DOI:10.1016/j.imbio.2011.07.031
Online-Zugang:Verlag, Volltext: http://dx.doi.org/10.1016/j.imbio.2011.07.031
Verlag, Volltext: http://www.sciencedirect.com/science/article/pii/S0171298511001720
Volltext
Verfasserangaben:Billur Baseras, Matthias M. Gaida, Nadine Kahle, Ann-Kathrin Schuppel, Diana Kathrey, Birgit Prior, Moritz Wente, Gertrud Maria Hänsch
Beschreibung
Zusammenfassung: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.
Beschreibung:Available online 5 August 2011
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Beschreibung:Online Resource
ISSN:1878-3279
DOI:10.1016/j.imbio.2011.07.031