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Cited by 71

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

A novel role for the macrophage galactose-type lectin receptor in mediating von Willebrand factor clearance

Ward, Soracha E., O’Sullivan, Jamie M., Drakeford, Clive, Aguila, Sonia, Jondle, Christopher N., Sharma, Jyotika, Fallon, Padraic G., Brophy, Teresa M., Preston, Roger J. S., Smyth, Paul, Sheils, Orla, Chion, Alain, O’Donnell, James S.·2018·Blood
DOI 10.1182/blood-2017-06-787853
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Abstract

Key Points: VWF sialylation modulates in vivo clearance through Ashwell-Morrell independent pathways. VWF binding to MGL plays a novel role in facilitating VWF clearance.

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Crossref · 10.1182/blood-2017-06-787853

Cites

2 of 2 references verified0 citation errors · 0 not checkable

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  • The present data are the first to identify the secretory membrane-bound LDLR as a physiological target of ASGR1, as opposed to soluble desialylated glycoproteins such as von Willebrand factor.

    “The present data are the first to identify the secretory membrane-bound LDLR as a physiological target of ASGR1, as opposed to soluble desialylated glycoproteins, e.g., von Willebrand factor (24), normally thought to be sensitive to hepatocyte-derived ASGR1 regulation (11).”

    From Asialoglycoprotein receptor 1 is a novel PCSK9-independent ligand of liver LDLR cleaved by furin (2021) · cites this paper as [24]

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 23

  1. Casari, 2013, Clearance of von Willebrand factor, J Thromb Haemost, 11, 202, 10.1111/jth.12226 · DOI
  2. Rawley, 2015, von Willebrand factor arginine 1205 substitution results in accelerated macrophage-dependent clearance in vivo, J Thromb Haemost, 13, 821, 10.1111/jth.12875 · DOI
  3. Canis, 2012, Mapping the N-glycome of human von Willebrand factor, Biochem J, 447, 217, 10.1042/BJ20120810 · DOI
  4. Canis, 2010, The plasma von Willebrand factor O-glycome comprises a surprising variety of structures including ABH antigens and disialosyl motifs, J Thromb Haemost, 8, 137, 10.1111/j.1538-7836.2009.03665.x · DOI
  5. McGrath, 2010, Expression of terminal alpha2-6-linked sialic acid on von Willebrand factor specifically enhances proteolysis by ADAMTS13, Blood, 115, 2666, 10.1182/blood-2009-09-241547 · DOI
  6. Sodetz, 1977, Relationship of sialic acid to function and in vivo survival of human factor VIII/von Willebrand factor protein, J Biol Chem, 252, 5538, 10.1016/S0021-9258(19)63384-3 · DOI
  7. van Schooten, 2007, Variations in glycosylation of von Willebrand factor with O-linked sialylated T antigen are associated with its plasma levels, Blood, 109, 2430, 10.1182/blood-2006-06-032706 · DOI
  8. O’Sullivan, 2016, N-linked glycan truncation causes enhanced clearance of plasma-derived von Willebrand factor, J Thromb Haemost, 14, 2446, 10.1111/jth.13537 · DOI
  9. Ellies, 2002, Sialyltransferase ST3Gal-IV operates as a dominant modifier of hemostasis by concealing asialoglycoprotein receptor ligands, Proc Natl Acad Sci USA, 99, 10042, 10.1073/pnas.142005099 · DOI
  10. Preston, 2013, Elucidating the role of carbohydrate determinants in regulating hemostasis: insights and opportunities, Blood, 121, 3801, 10.1182/blood-2012-10-415000 · DOI
  11. Chion, 2016, N-linked glycans within the A2 domain of von Willebrand factor modulate macrophage-mediated clearance, Blood, 128, 1959, 10.1182/blood-2016-04-709436 · DOI
  12. O’Sullivan, 2016, Galectin-1 and galectin-3 constitute novel-binding partners for factor VIII, Arterioscler Thromb Vasc Biol, 36, 855, 10.1161/ATVBAHA.115.306915 · DOI
  13. Wall, 1980, The galactose-specific recognition system of mammalian liver: the route of ligand internalization in rat hepatocytes, Cell, 21, 79, 10.1016/0092-8674(80)90116-6 · DOI
  14. Lodish, 1991, Recognition of complex oligosaccharides by the multi-subunit asialoglycoprotein receptor, Trends Biochem Sci, 16, 374, 10.1016/0968-0004(91)90154-N · DOI
  15. Higashi, 2002, Human macrophage lectin specific for galactose/N-acetylgalactosamine is a marker for cells at an intermediate stage in their differentiation from monocytes into macrophages, Int Immunol, 14, 545, 10.1093/intimm/dxf021 · DOI
  16. van Vliet, 2005, Carbohydrate profiling reveals a distinctive role for the C-type lectin MGL in the recognition of helminth parasites and tumor antigens by dendritic cells, Int Immunol, 17, 661, 10.1093/intimm/dxh246 · DOI · Paper page
  17. van Vliet, 2007, MGL-mediated internalization and antigen presentation by dendritic cells: a role for tyrosine-5, Eur J Immunol, 37, 2075, 10.1002/eji.200636838 · DOI
  18. Oo-puthinan, 2008, The amino acids involved in the distinct carbohydrate specificities between macrophage galactose-type C-type lectins 1 and 2 (CD301a and b) of mice, Biochim Biophys Acta, 1780, 89, 10.1016/j.bbagen.2007.10.017 · DOI
  19. Yamamoto, 1994, Interaction of immobilized recombinant mouse C-type macrophage lectin with glycopeptides and oligosaccharides, Biochemistry, 33, 8159, 10.1021/bi00192a021 · DOI
  20. Mortezai, 2013, Tumor-associated Neu5Ac-Tn and Neu5Gc-Tn antigens bind to C-type lectin CLEC10A (CD301, MGL), Glycobiology, 23, 844, 10.1093/glycob/cwt021 · DOI
  21. Tsuiji, 2002, Molecular cloning and characterization of a novel mouse macrophage C-type lectin, mMGL2, which has a distinct carbohydrate specificity from mMGL1, J Biol Chem, 277, 28892, 10.1074/jbc.M203774200 · DOI
  22. Pipe, 2016, Life in the shadow of a dominant partner: the FVIII-VWF association and its clinical implications for hemophilia A, Blood, 128, 2007, 10.1182/blood-2016-04-713289 · DOI
  23. Yang, 2015, An intrinsic mechanism of secreted protein aging and turnover, Proc Natl Acad Sci USA, 112, 13657, 10.1073/pnas.1515464112 · DOI · Paper page

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Metadata

Authors
Ward, S. E., O’Sullivan, J. M., Drakeford, C., Aguila, S., Jondle, C. N., Sharma, J., Fallon, P. G., Brophy, T. M., Preston, R. J. S., Smyth, P., Sheils, O., Chion, A., & O’Donnell, J. S.
Affiliations
  • Irish Centre for Vascular Biology, Molecular and Cellular Therapeutics, Royal College of Surgeons in Ireland, Dublin, Ireland;
  • Department of Basic Biomedical Sciences, University of North Dakota School of Medicine and Health Sciences, Grand Forks, ND;
  • Inflammation and Immunity Research Group, Trinity Translational Medicine Institute, and
  • Department of Histopathology, Trinity Translational Medicine Institute, Trinity College Dublin, St. James’s Hospital, Dublin, Ireland; and
Venue
Blood
Publisher
American Society of Hematology
Published
2018-02-22
Volume
131
Issue
8
Pages
911-916
ISSN
  • 0006-4971
  • 1528-0020
DOI
10.1182/blood-2017-06-787853
Cited by
71
References
2
Language
en

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