Galectin-3 inhibits the chemotaxis of human polymorphonuclear neutrophils in vitro

• Published in: Immunobiology (1979) Vol. 217; no. 1; pp. 83 - 90
• Main Authors: Baseras, Billur, Gaida, Matthias M, Kahle, Nadine, Schuppel, Ann-Kathrin, Kathrey, Diana, Prior, Birgit, Wente, Moritz, Hänsch, Gertrud Maria
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier GmbH 01.01.2012
• Subjects: Actins - immunology; Actins - metabolism; Adenosine Triphosphate - immunology; Adenosine Triphosphate - metabolism; Advanced Basic Science; Allergy and Immunology; Animal lectins; Blotting, Western; Cells, Cultured; Chemotaxis; Chemotaxis, Leukocyte - drug effects; Chemotaxis, Leukocyte - immunology; Complement C5a - immunology; Complement C5a - metabolism; Complement C5a - pharmacology; Flow Cytometry; Fluorescein-5-isothiocyanate - analysis; Galectin; Galectin 3 - immunology; Galectin 3 - metabolism; Galectin 3 - pharmacology; Humans; Immunity, Innate; Inflammation - immunology; Inflammation - metabolism; Interleukin-8 - immunology; Interleukin-8 - metabolism; Interleukin-8 - pharmacology; MAP kinase p38; Neutrophils; Neutrophils - cytology; Neutrophils - drug effects; Neutrophils - immunology; Neutrophils - metabolism; p38 Mitogen-Activated Protein Kinases - immunology; p38 Mitogen-Activated Protein Kinases - metabolism; Phosphorylation - drug effects; Phosphorylation - immunology; Polymerization; Signal Transduction - drug effects; Signal Transduction - immunology; Galectin; Chemotaxis; Animal lectins; MAP kinase p38; Neutrophils
• ISSN: 0171-2985; 1878-3279
• DOI: 10.1016/j.imbio.2011.07.031

Abstract 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.