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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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