Galectin-3 functions as an opsonin and enhances the macrophage clearance of apoptotic neutrophils
(2009) In Glycobiology 19(1). p.16-20- Abstract
- Galectin-3, a beta-galactoside binding, endogenous lectin, takes part in various inflammatory events and is produced in substantial amounts at inflammatory foci. We investigated whether extracellular galectin-3 could participate in the phagocytic clearance of apoptotic neutrophils by macrophages, a process of crucial importance for termination of acute inflammation. Using human leukocytes, we show that exogenously added galectin-3 increased the uptake of apoptotic neutrophils by monocyte-derived macrophages (MDM). Both the proportion of MDM that engulfed apoptotic prey and the number of apoptotic neutrophils that each MDM engulfed were enhanced in the presence of galectin-3. The effect was lactose-inhibitable and required galectin-3... (More)
- Galectin-3, a beta-galactoside binding, endogenous lectin, takes part in various inflammatory events and is produced in substantial amounts at inflammatory foci. We investigated whether extracellular galectin-3 could participate in the phagocytic clearance of apoptotic neutrophils by macrophages, a process of crucial importance for termination of acute inflammation. Using human leukocytes, we show that exogenously added galectin-3 increased the uptake of apoptotic neutrophils by monocyte-derived macrophages (MDM). Both the proportion of MDM that engulfed apoptotic prey and the number of apoptotic neutrophils that each MDM engulfed were enhanced in the presence of galectin-3. The effect was lactose-inhibitable and required galectin-3 affinity for N-acetyllactosamine, a saccharide typically found on cell surface glycoproteins, since a mutant lacking this activity was without effect. The enhanced uptake relied on the presence of galectin-3 during the cellular interaction and was paralleled by lectin binding to apoptotic cells as well as MDM in a lactose-dependent manner. These findings suggest that galectin-3 functions as a bridging molecule between phagocyte and apoptotic prey, acting as an opsonin. The process of clearance, whereby apoptotic neutrophils are removed by macrophages, is crucial for the resolution of acute inflammation and our data imply that the increased levels of galectin-3 often found at inflammatory sites could potently affect this process. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1313802
- author
- Karlsson, Anna ; Christenson, Karin ; Matlak, Mustafa ; Bjorstad, Ase ; Brown, Kelly L. ; Telemo, Esbjorn ; Salomonsson, Emma LU ; Leffler, Hakon LU and Bylund, Johan
- organization
- publishing date
- 2009
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- phagocytosis, mdm, clearance, inflammation
- in
- Glycobiology
- volume
- 19
- issue
- 1
- pages
- 16 - 20
- publisher
- Oxford University Press
- external identifiers
-
- wos:000261679900002
- scopus:57649166561
- pmid:18849325
- ISSN
- 1460-2423
- DOI
- 10.1093/glycob/cwn104
- language
- English
- LU publication?
- yes
- id
- f43c3030-f170-4ee8-89f0-be89a5c78dfc (old id 1313802)
- date added to LUP
- 2016-04-01 13:57:13
- date last changed
- 2022-04-22 00:32:47
@article{f43c3030-f170-4ee8-89f0-be89a5c78dfc,
abstract = {{Galectin-3, a beta-galactoside binding, endogenous lectin, takes part in various inflammatory events and is produced in substantial amounts at inflammatory foci. We investigated whether extracellular galectin-3 could participate in the phagocytic clearance of apoptotic neutrophils by macrophages, a process of crucial importance for termination of acute inflammation. Using human leukocytes, we show that exogenously added galectin-3 increased the uptake of apoptotic neutrophils by monocyte-derived macrophages (MDM). Both the proportion of MDM that engulfed apoptotic prey and the number of apoptotic neutrophils that each MDM engulfed were enhanced in the presence of galectin-3. The effect was lactose-inhibitable and required galectin-3 affinity for N-acetyllactosamine, a saccharide typically found on cell surface glycoproteins, since a mutant lacking this activity was without effect. The enhanced uptake relied on the presence of galectin-3 during the cellular interaction and was paralleled by lectin binding to apoptotic cells as well as MDM in a lactose-dependent manner. These findings suggest that galectin-3 functions as a bridging molecule between phagocyte and apoptotic prey, acting as an opsonin. The process of clearance, whereby apoptotic neutrophils are removed by macrophages, is crucial for the resolution of acute inflammation and our data imply that the increased levels of galectin-3 often found at inflammatory sites could potently affect this process.}},
author = {{Karlsson, Anna and Christenson, Karin and Matlak, Mustafa and Bjorstad, Ase and Brown, Kelly L. and Telemo, Esbjorn and Salomonsson, Emma and Leffler, Hakon and Bylund, Johan}},
issn = {{1460-2423}},
keywords = {{phagocytosis; mdm; clearance; inflammation}},
language = {{eng}},
number = {{1}},
pages = {{16--20}},
publisher = {{Oxford University Press}},
series = {{Glycobiology}},
title = {{Galectin-3 functions as an opsonin and enhances the macrophage clearance of apoptotic neutrophils}},
url = {{http://dx.doi.org/10.1093/glycob/cwn104}},
doi = {{10.1093/glycob/cwn104}},
volume = {{19}},
year = {{2009}},
}