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Galectin-3 functions as an opsonin and enhances the macrophage clearance of apoptotic neutrophils

Karlsson, Anna; Christenson, Karin; Matlak, Mustafa; Bjorstad, Ase; Brown, Kelly L.; Telemo, Esbjorn; Salomonsson, Emma LU ; Leffler, Hakon LU and Bylund, Johan (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)
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author
organization
publishing date
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
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
2009-03-06 13:59:09
date last changed
2017-07-23 04:13:57
@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},
  keyword      = {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},
  volume       = {19},
  year         = {2009},
}