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Glycobiology Advance Access published online on August 25, 2008
Glycobiology, doi:10.1093/glycob/cwn081
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© The Author 2008. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

The β-galactoside binding immunomodulatory lectin Galectin-3 reverses the desensitized state induced in neutrophils by the chemotactic peptide f-Met-Leu-Phe: Role of reactive oxygen species generated by the NADPH-oxidase and inactivation of the agonist

Huamei Forsman1, Emma Salomonsson2, Karin Önnheim1, Jennie Karlsson1, Åse Björstad1, Hakon Leffler2, Johan Bylund1, Anna Karlsson1 and and Claes Dahlgren1,#

1 Department of Rheumatology and Inflammation Research, Göteborg University
2 Section for Microbiology, Immunology, Glycobiology, Department of Laboratory Medicine, University of Lund, Sweden

* Corresponding author: Claes Dahlgren, Department of Rheumatology and Inflammation Research, Guldhedsgatan 10 A, S-413 46 Gothenburg, Sweden. e-mail: Claes.Dahlgren{at}microbio.gu.se, phone: +46-31-342 46 83

Received on May 27, 2008; accepted on August 19, 2008

Neutrophils interacting with a chemoattractant gradually become non-responsive to further stimulation by the same agonist, a process known as desensitization. Receptor desensitization is a highly regulated process that involves different mechanisms depending on which receptor-ligand pair that is studied. Galectin-3, a member of a large family of β-galactoside-binding lectins, has been suggested to be a regulator of the inflammatory process, augmenting or directly triggering the neutrophil functional repertoire.

We show here that the desensitized state of neutrophils interacting with the chemotactic peptide fMLF is broken by galectin-3 and that this is achieved through an oxygen radical mediated inactivation of the chemoattractant. The effect was inhibited by the competitor lactose, and required the affinity of galectin-3 for N-acetyllactosamine, a saccharide typically found on cell surface glycoproteins. The latter was shown using a mutant that lacked N-acetyllactosamine binding activity, and this protein was not active. The mechanism behind the inactivation of the chemoattractant was found to depend on the ability of galectin-3 to induce a neutrophil generation/secretion of reactive oxygen species which in combined action with myeloperoxidase inactivated the peptides.

Key words: formylpeptide receptors / hydrogen peroxide / lectin / myeloperoxidase / oxidants


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