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Different affinity of galectins for human serum glycoproteins: galectin-3 binds many protease inhibitors and acute phase proteins.

Cederfur, Cecilia LU ; Salomonsson, Emma LU ; Nilsson, Jonas; Halim, Adnan; Öberg, Christopher LU ; Larson, Göran; Nilsson, Ulf LU and Leffler, Hakon LU (2008) In Glycobiology 18(5). p.384-394
Abstract
Here we report the first survey of galectin binding to glycoproteins of human serum. Serum was subjected to affinity chromatography using immobilized galectins, and the bound glycoproteins were analyzed by electrophoresis, Western blotting, and mass spectrometry. Galectins-3, -8 and -9 bound a much broader range of ligands in serum than previously known, galectin-1 bound less, and galectins-2, -4 and -7 bound only traces or no serum ligands. Galectin-3 bound most major glycoproteins, including alpha-2 macroglobulin and acute phase proteins such as haptoglobin. It bound only a selected minor fraction of transferrin, and bound none or little of IgG. Galectin-8 and -9 bound a similar range of glycoproteins as galectin-3, but in lower amounts,... (More)
Here we report the first survey of galectin binding to glycoproteins of human serum. Serum was subjected to affinity chromatography using immobilized galectins, and the bound glycoproteins were analyzed by electrophoresis, Western blotting, and mass spectrometry. Galectins-3, -8 and -9 bound a much broader range of ligands in serum than previously known, galectin-1 bound less, and galectins-2, -4 and -7 bound only traces or no serum ligands. Galectin-3 bound most major glycoproteins, including alpha-2 macroglobulin and acute phase proteins such as haptoglobin. It bound only a selected minor fraction of transferrin, and bound none or little of IgG. Galectin-8 and -9 bound a similar range of glycoproteins as galectin-3, but in lower amounts, and galectin-8 had a relative preference for IgA. Galectin-1 bound mainly a fraction of alpha-2 macroglobulin and only traces of other glycoproteins. The binding of galectin-3 to serum glycoproteins requires affinity for LacNAc, since a mutant (R186S), which has lost this affinity, did not bind any serum glycoproteins. The average affinity of galectin-3 for serum glycoproteins was estimated to correspond to K(d) approximately 1-5 muM by modelling of the affinity chromatography and a fluorescence anisotropy assay. Since galectins are expressed on endothelial cells and other cells exposed to serum components, this report gives new insight into function of galectins and the role of their different fine specificity giving differential binding to the serum glycoproteins. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Glycobiology
volume
18
issue
5
pages
384 - 394
publisher
Oxford University Press
external identifiers
  • pmid:18263896
  • wos:000255151000004
  • scopus:42449153703
ISSN
1460-2423
DOI
10.1093/glycob/cwn015
language
English
LU publication?
yes
id
6facd44b-296d-4bcc-a843-d6e1c595163f (old id 1042086)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/18263896?dopt=Abstract
date added to LUP
2008-03-04 08:53:23
date last changed
2017-03-12 03:43:40
@article{6facd44b-296d-4bcc-a843-d6e1c595163f,
  abstract     = {Here we report the first survey of galectin binding to glycoproteins of human serum. Serum was subjected to affinity chromatography using immobilized galectins, and the bound glycoproteins were analyzed by electrophoresis, Western blotting, and mass spectrometry. Galectins-3, -8 and -9 bound a much broader range of ligands in serum than previously known, galectin-1 bound less, and galectins-2, -4 and -7 bound only traces or no serum ligands. Galectin-3 bound most major glycoproteins, including alpha-2 macroglobulin and acute phase proteins such as haptoglobin. It bound only a selected minor fraction of transferrin, and bound none or little of IgG. Galectin-8 and -9 bound a similar range of glycoproteins as galectin-3, but in lower amounts, and galectin-8 had a relative preference for IgA. Galectin-1 bound mainly a fraction of alpha-2 macroglobulin and only traces of other glycoproteins. The binding of galectin-3 to serum glycoproteins requires affinity for LacNAc, since a mutant (R186S), which has lost this affinity, did not bind any serum glycoproteins. The average affinity of galectin-3 for serum glycoproteins was estimated to correspond to K(d) approximately 1-5 muM by modelling of the affinity chromatography and a fluorescence anisotropy assay. Since galectins are expressed on endothelial cells and other cells exposed to serum components, this report gives new insight into function of galectins and the role of their different fine specificity giving differential binding to the serum glycoproteins.},
  author       = {Cederfur, Cecilia and Salomonsson, Emma and Nilsson, Jonas and Halim, Adnan and Öberg, Christopher and Larson, Göran and Nilsson, Ulf and Leffler, Hakon},
  issn         = {1460-2423},
  language     = {eng},
  number       = {5},
  pages        = {384--394},
  publisher    = {Oxford University Press},
  series       = {Glycobiology},
  title        = {Different affinity of galectins for human serum glycoproteins: galectin-3 binds many protease inhibitors and acute phase proteins.},
  url          = {http://dx.doi.org/10.1093/glycob/cwn015},
  volume       = {18},
  year         = {2008},
}