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Activation of the neutrophil nicotinamide adenine dinucleotide phosphate oxidase by galectin-1

Almkvist, J; Dahlgren, C; Leffler, Hakon LU and Karlsson, A (2002) In Journal of Immunology 168(8). p.4034-4041
Abstract
Galectins are a group of lactose-binding proteins widely distributed in nature. Twelve mammalian galectins have so far been identified, but their functions are to a large extent unknown. In this work we study galectin-1 in its interaction with human neutrophils, with regard to both cell surface binding and activation of the superoxide-producing NADPH-oxidase. We show that galectin-1 is able to activate the neutrophil NADPH-oxidase, provided that the cells have been primed by extravasation from the blood into the tissue, an activation pattern that is similar to that of galectin-3. Using In vitro priming protocols, the galectin-1 responsiveness was found to correlate to granule mobilization and galectin-1 binding to the cells, suggesting the... (More)
Galectins are a group of lactose-binding proteins widely distributed in nature. Twelve mammalian galectins have so far been identified, but their functions are to a large extent unknown. In this work we study galectin-1 in its interaction with human neutrophils, with regard to both cell surface binding and activation of the superoxide-producing NADPH-oxidase. We show that galectin-1 is able to activate the neutrophil NADPH-oxidase, provided that the cells have been primed by extravasation from the blood into the tissue, an activation pattern that is similar to that of galectin-3. Using In vitro priming protocols, the galectin-1 responsiveness was found to correlate to granule mobilization and galectin-1 binding to the cells, suggesting the presence of granule-localized receptors that are up-regulated to the cell surface upon priming. By galectin-1 overlay of fractionated neutrophils we identified potential galectin-1 receptor candidates localized in the membranes of the secretory vesicle and gelatinase granules. The binding of galectin-1 and galectin-3 to neutrophil proteins was compared, as were the dose dependencies for activation by the two lectins. The results suggest that, although similarities are found between the two galectins, they appear to activate the NADPH-oxidase using different receptors. In conclusion, galectin-1 appears to have proinflammatory functions, mediated through activation of the neutrophil respiratory burst. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Immunology
volume
168
issue
8
pages
4034 - 4041
publisher
American Association of Immunologists
external identifiers
  • wos:000174913300046
  • pmid:11937561
  • scopus:0037090251
ISSN
1550-6606
language
English
LU publication?
yes
id
d187bc1a-da6f-40ad-8ba8-60533b84b286 (old id 340254)
alternative location
http://www.jimmunol.org/cgi/content/abstract/168/8/4034
date added to LUP
2007-08-02 10:44:04
date last changed
2017-08-13 04:13:17
@article{d187bc1a-da6f-40ad-8ba8-60533b84b286,
  abstract     = {Galectins are a group of lactose-binding proteins widely distributed in nature. Twelve mammalian galectins have so far been identified, but their functions are to a large extent unknown. In this work we study galectin-1 in its interaction with human neutrophils, with regard to both cell surface binding and activation of the superoxide-producing NADPH-oxidase. We show that galectin-1 is able to activate the neutrophil NADPH-oxidase, provided that the cells have been primed by extravasation from the blood into the tissue, an activation pattern that is similar to that of galectin-3. Using In vitro priming protocols, the galectin-1 responsiveness was found to correlate to granule mobilization and galectin-1 binding to the cells, suggesting the presence of granule-localized receptors that are up-regulated to the cell surface upon priming. By galectin-1 overlay of fractionated neutrophils we identified potential galectin-1 receptor candidates localized in the membranes of the secretory vesicle and gelatinase granules. The binding of galectin-1 and galectin-3 to neutrophil proteins was compared, as were the dose dependencies for activation by the two lectins. The results suggest that, although similarities are found between the two galectins, they appear to activate the NADPH-oxidase using different receptors. In conclusion, galectin-1 appears to have proinflammatory functions, mediated through activation of the neutrophil respiratory burst.},
  author       = {Almkvist, J and Dahlgren, C and Leffler, Hakon and Karlsson, A},
  issn         = {1550-6606},
  language     = {eng},
  number       = {8},
  pages        = {4034--4041},
  publisher    = {American Association of Immunologists},
  series       = {Journal of Immunology},
  title        = {Activation of the neutrophil nicotinamide adenine dinucleotide phosphate oxidase by galectin-1},
  volume       = {168},
  year         = {2002},
}