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Galectin-3 Activates the NADPH-Oxidase in Exudated but not
Peripheral Blood Neutrophils
Anna Karlsson,
Per Follin,
Hakon Leffler, and
Claes Dahlgren
From The Phagocyte Research Laboratory, the Department of Medical
Microbiology and Immunology, University of Göteborg,
Guldhedsgatan 10, S-413 46 Göteborg, Sweden; the Department of
Medical Microbiology and the Department of Infectious Diseases,
University of Linköping, Sweden; and Center for Neurobiology and
Psychiatry, University of California, San Francisco.
Galectin-3, a lactose-binding mammalian lectin that is secreted from
activated macrophages, basophils, and mast cells, was investigated with
respect to its ability to activate the human neutrophil NADPH-oxidase.
The galectin-3-induced activity was determined with in vivo exudated
cells (obtained from a skin chamber) and compared with that of
peripheral blood neutrophils. Galectin-3 was found to be a potent
activator of the NADPH-oxidase only in exudated neutrophils and the
binding of galectin-3 to the surface of these cells was increased
compared with peripheral blood cells. Different in vitro priming
protocols resulting in degranulation were used to mimic the exudation
process in terms of increasing the receptor exposure on the cell
surface. Galectin-3 could induce an oxidative response similar to that
in exudated cells only after a significant amount of the intracellular
organelles had been mobilized. This increase in oxidative response was
paralleled by an increased binding of galectin-3 to the surface of the
cells. The major conclusion of the study is that galectin-3 is a potent stimulus of the neutrophil respiratory burst, provided that the cells
have first experienced an extravasation process. The results also imply
that the neutrophil response to galectin-3 could be mediated through
receptors mobilized from intracellular granules, and we report the
presence of galectin-3-binding proteins in such organelles.
Blood, Vol. 91 No. 9 (May 1), 1998:
pp. 3430-3438
© 1998 by The American Society of Hematology.
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