The beta-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
(2008) In Glycobiology 18(11). p.905-912- Abstract
- Neutrophils interacting with a chemoattractant gradually become nonresponsive 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 beta-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... (More)
- Neutrophils interacting with a chemoattractant gradually become nonresponsive 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 beta-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 galectin-3 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1377074
- author
- Forsman, Huamei ; Salomonsson, Emma LU ; Onnheim, Karin ; Karlsson, Jennie ; Bjorstad, Ase ; Leffler, Hakon LU ; Bylund, Johan ; Karlsson, Anna and Dahlgren, Claes
- organization
- publishing date
- 2008
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- myeloperoxidase, hydrogen peroxide, lectin, formylpeptide receptors, oxidants
- in
- Glycobiology
- volume
- 18
- issue
- 11
- pages
- 905 - 912
- publisher
- Oxford University Press
- external identifiers
-
- wos:000260141400008
- scopus:54549120499
- pmid:18725453
- ISSN
- 1460-2423
- DOI
- 10.1093/glycob/cwn081
- language
- English
- LU publication?
- yes
- id
- c368b619-8153-4ab1-ba90-379b45486175 (old id 1377074)
- date added to LUP
- 2016-04-01 14:34:54
- date last changed
- 2022-04-14 18:33:46
@article{c368b619-8153-4ab1-ba90-379b45486175,
abstract = {{Neutrophils interacting with a chemoattractant gradually become nonresponsive 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 beta-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 galectin-3 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.}},
author = {{Forsman, Huamei and Salomonsson, Emma and Onnheim, Karin and Karlsson, Jennie and Bjorstad, Ase and Leffler, Hakon and Bylund, Johan and Karlsson, Anna and Dahlgren, Claes}},
issn = {{1460-2423}},
keywords = {{myeloperoxidase; hydrogen peroxide; lectin; formylpeptide receptors; oxidants}},
language = {{eng}},
number = {{11}},
pages = {{905--912}},
publisher = {{Oxford University Press}},
series = {{Glycobiology}},
title = {{The beta-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}},
url = {{http://dx.doi.org/10.1093/glycob/cwn081}},
doi = {{10.1093/glycob/cwn081}},
volume = {{18}},
year = {{2008}},
}