Activation of the neutrophil nicotinamide adenine dinucleotide phosphate oxidase by galectin-1
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/340254
- author
- Almkvist, J ; Dahlgren, C ; Leffler, Hakon LU and Karlsson, A
- organization
- publishing date
- 2002
- 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
- 2016-04-01 15:19:11
- date last changed
- 2022-04-14 21:35:47
@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}}, url = {{http://www.jimmunol.org/cgi/content/abstract/168/8/4034}}, volume = {{168}}, year = {{2002}}, }