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  Identification of neutrophil granule glycoproteins as Lewisx-containing ligands cleared by the scavenger receptor C-type lectin

Graham, S. A., Antonopoulos, A., Hitchen, P. G., Haslam, S. M., Dell, A., Drickamer, K., et al. (2011). Identification of neutrophil granule glycoproteins as Lewisx-containing ligands cleared by the scavenger receptor C-type lectin. Journal of Biological Chemistry, 286, 24336-24349. doi:10.1074/jbc.M111.244772.

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 Creators:
Graham, Sarah A.1, 2, Author              
Antonopoulos, Aristotelis1, Author
Hitchen, Paul G.1, Author
Haslam, Stuart M.1, Author
Dell, Anne1, Author
Drickamer, Kurt1, Author
Taylor, Maureen E.1, Author
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1Division of Molecular Biosciences, Department of Life Sciences, Imperial College London, United Kingdom, ou_792549              
2Language and Genetics Department, MPI for Psycholinguistics, Max Planck Society, Nijmegen, NL, ou_792549              

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 Abstract: The scavenger receptor C-type lectin (SRCL) is a glycan-binding receptor that has the capacity to mediate endocytosis of glycoproteins carrying terminal Lewis(x) groups (Galβ1-4(Fucα1-3)GlcNAc). A screen for glycoprotein ligands for SRCL using affinity chromatography on immobilized SRCL followed by mass spectrometry-based proteomic analysis revealed that soluble glycoproteins from secondary granules of neutrophils, including lactoferrin and matrix metalloproteinases 8 and 9, are major ligands. Binding competition and surface plasmon resonance analysis showed affinities in the low micromolar range. Comparison of SRCL binding to neutrophil and milk lactoferrin indicates that the binding is dependent on cell-specific glycosylation in the neutrophils, as the milk form of the glycoprotein is a much poorer ligand. Binding to neutrophil glycoproteins is fucose dependent and mass spectrometry-based glycomic analysis of neutrophil and milk lactoferrin was used to establish a correlation between high affinity binding to SRCL and the presence of multiple, clustered terminal Lewis(x) groups on a heterogeneous mixture of branched glycans, some with poly N-acetyllactosamine extensions. The ability of SRCL to mediate uptake of neutrophil lactoferrin was confirmed using fibroblasts transfected with SRCL. The common presence of Lewis(x) groups in granule protein glycans can thus target granule proteins for clearance by SRCL. PCR and immunohistochemical analysis confirms that SRCL is widely expressed on endothelial cells and thus represents a distributed system which could scavenge released neutrophil glycoproteins both locally at sites of inflammation or systemically when they are released in the circulation.

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Language(s): eng - English
 Dates: 2011-05-112011-07-08
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1074/jbc.M111.244772
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Title: Journal of Biological Chemistry
  Other : J. Biol. Chem.
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 286 Sequence Number: - Start / End Page: 24336 - 24349 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826