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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 24
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pubmed:dateCreated |
2004-11-11
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pubmed:abstractText |
P-selectin glycoprotein ligand-1 (PSGL-1), a glycoprotein expressed on the cell surface of leukocytes, binds to selectins and mediates leukocyte rolling on the vascular endothelium. Here we report that PSGL-1 binds to the C-terminal (G3 domain) of the extracellular proteoglycan PG-M/versican. Cells transfected with PSGL-1 or a shorter form containing the binding site, or cells expressing endogenous PSGL-1 aggregate in the presence of versican or G3 product. The aggregation appears to be induced by G3 multimers that bind to PSGL-1 and form a network. Endogenous versican and/or G3-containing fragments also bind to PSGL-1 in human plasma. Removal of the endogenous G3-containing fragments reduces the effect of plasma on leukocyte aggregation. Finally, the roles of G3-containing fragments in leukocyte aggregation were confirmed in a mouse model. Taken together, our results strongly support a physiologically relevant role for PSGL-1/versican binding and may have implications in the immunoresponse.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Chondroitin Sulfate Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Cspg2 protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Disulfides,
http://linkedlifedata.com/resource/pubmed/chemical/Dithiothreitol,
http://linkedlifedata.com/resource/pubmed/chemical/Glutathione Transferase,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Matrix Metalloproteinases,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/P-selectin ligand protein,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/VCAN protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Versicans
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0021-9533
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
117
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5887-95
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:15522894-Amino Acid Motifs,
pubmed-meshheading:15522894-Binding Sites,
pubmed-meshheading:15522894-Cell Adhesion,
pubmed-meshheading:15522894-Cell Line, Tumor,
pubmed-meshheading:15522894-Cell Membrane,
pubmed-meshheading:15522894-Chondroitin Sulfate Proteoglycans,
pubmed-meshheading:15522894-DNA, Complementary,
pubmed-meshheading:15522894-DNA Primers,
pubmed-meshheading:15522894-Disulfides,
pubmed-meshheading:15522894-Dithiothreitol,
pubmed-meshheading:15522894-Gene Library,
pubmed-meshheading:15522894-Glutathione Transferase,
pubmed-meshheading:15522894-Glycoproteins,
pubmed-meshheading:15522894-Humans,
pubmed-meshheading:15522894-Leukocytes,
pubmed-meshheading:15522894-Matrix Metalloproteinases,
pubmed-meshheading:15522894-Membrane Glycoproteins,
pubmed-meshheading:15522894-Models, Biological,
pubmed-meshheading:15522894-Nerve Tissue Proteins,
pubmed-meshheading:15522894-Protein Binding,
pubmed-meshheading:15522894-Protein Structure, Tertiary,
pubmed-meshheading:15522894-Recombinant Fusion Proteins,
pubmed-meshheading:15522894-Recombinant Proteins,
pubmed-meshheading:15522894-Signal Transduction,
pubmed-meshheading:15522894-Transfection,
pubmed-meshheading:15522894-Two-Hybrid System Techniques,
pubmed-meshheading:15522894-Versicans
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pubmed:year |
2004
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pubmed:articleTitle |
PG-M/versican binds to P-selectin glycoprotein ligand-1 and mediates leukocyte aggregation.
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pubmed:affiliation |
Sunnybrook and Women's College Health Sciences Centre, 2075 Bayview Avenue, Toronto, ON M4N 3M5, Canada.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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