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Infection and Immunity, February 2001, p. 832-837, Vol. 69, No. 2
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.2.832-837.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Lipopolysaccharide-Induced Gelatinase Granule Mobilization Primes Neutrophils for Activation by Galectin-3 and Formylmethionyl-Leu-Phe

Jenny Almkvist,1 Jenny Fäldt,1 Claes Dahlgren,1 Hakon Leffler,2 and Anna Karlsson1,*

Phagocyte Research Laboratory, Department of Medical Microbiology and Immunology, University of Göteborg, Göteborg,1 and Section MIG, Institute of Laboratory Medicine, Lund University, Lund,2 Sweden

Received 13 April 2000/Returned for modification 15 June 2000/Accepted 8 November 2000

We have earlier shown that galectin-3, a lactose-binding mammalian lectin that is secreted from activated macrophages, basophils, and mast cells, induces activation of the NADPH oxidase in exudated but not in peripheral blood neutrophils (A. Karlsson, P. Follin, H. Leffler, and C. Dahlgren, Blood 91:3430-3438, 1998). The alteration in responsiveness occurring during extravasation correlated with mobilization of the gelatinase and/or specific granules to the cell surface, indicating a role for mobilizable galectin-3 receptors. In this study we have investigated galectin-3-induced NADPH oxidase activation, measured as superoxide production, in lipopolysaccharide (LPS)-primed neutrophils. Upon galectin-3 challenge, the LPS-primed cells produced superoxide, both extracellularly and intracellularly. A primed extracellular response to formylmethionyl-Leu-Phe (fMLF) was also achieved. The exposure of complement receptors 1 and 3 as well as the formyl peptide receptor on the cell surface was markedly increased after LPS treatment, indicating that granule fusion with the plasma membrane had occurred. Further assessment of specific markers for neutrophil granules showed that the LPS treatment had mobilized the gelatinase granules but only a minor fraction of the specific granules. We thus suggest that the mechanism behind LPS priming lies at the level of granule (receptor) mobilization for galectin-3 as well as for fMLF.

* Corresponding author. Mailing address: Phagocyte Research Laboratory, Department of Medical Microbiology and Immunology, Box 435, S-405 30 Göteborg, Sweden. Phone: 46-31-342 46 35. Fax: 46-31-82 88 98. E-mail: anna.karlsson{at}microbio.gu.se.

Infection and Immunity, February 2001, p. 832-837, Vol. 69, No. 2
0019-9567/01/$04.00+0   DOI: 10.1128/IAI.69.2.832-837.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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