Source:http://linkedlifedata.com/resource/pubmed/id/15814589
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2005-7-8
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pubmed:abstractText |
P-selectin glycoprotein ligand-1 (PSGL-1) has been proposed as an important tethering ligand for E-selectin and is expressed at a modest level on human leukocytes. Sialyl Lewis x (sLe(x))-like glycans bind to E-selectin and are expressed at a relatively high level on circulating leukocytes. It is unclear whether PSGL-1 has unique biochemical attributes that contribute to its role as an E-selectin ligand. To probe this issue, we conjugated microspheres with either sLe(x) or PSGL-1 purified from myeloid cells (neutrophils and HL-60) and compared their adhesion to endothelial expressed E-selectin under defined shear conditions. We found that both sLe(x) and PSGL-1 microspheres adhere to 4 h of IL-1beta-activated human umbilical vein endothelial cells predominantly through E-selectin. Analysis of the adhesion revealed that the rate of initial tethering of the PSGL-1 microspheres to E-selectin was significantly greater than the rate of initial tethering of the sLe(x) microspheres despite the fact that the sLe(x) microspheres tested had higher ligand densities than the PSGL-1 microspheres. We also found that pretreatment of the PSGL-1 or sLe(x) microspheres with HECA-452 had no significant effect on initial tethering to E-selectin. These results support the hypotheses that 1) PSGL-1 is a high-efficiency tethering ligand for E-selectin, 2) ligand biochemistry can significantly influence initial tethering to E-selectin, and 3) PSGL-1 tethering to E-selectin can occur via non-HECA-452 reactive epitopes.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/E-Selectin,
http://linkedlifedata.com/resource/pubmed/chemical/HECA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Neoplasm Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/P-selectin ligand protein
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0363-6143
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pubmed:author |
pubmed-author:DagiaNilesh MNM,
pubmed-author:GoetzDouglas JDJ,
pubmed-author:InterliggiKimberly AKA,
pubmed-author:LawrenceMichael BMB,
pubmed-author:LloydChristopher MCM,
pubmed-author:Shinde PatilVivek RVR,
pubmed-author:SmithLee ALA,
pubmed-author:TeesDavid F JDF,
pubmed-author:WalcheckBruceB,
pubmed-author:WargoMaureen JMJ,
pubmed-author:ZouXiaoyanX
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pubmed:issnType |
Print
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pubmed:volume |
289
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
C415-24
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:15814589-Cell Adhesion,
pubmed-meshheading:15814589-Cells, Cultured,
pubmed-meshheading:15814589-E-Selectin,
pubmed-meshheading:15814589-Endothelium, Vascular,
pubmed-meshheading:15814589-Flow Cytometry,
pubmed-meshheading:15814589-Humans,
pubmed-meshheading:15814589-Leukocyte Rolling,
pubmed-meshheading:15814589-Ligands,
pubmed-meshheading:15814589-Membrane Glycoproteins,
pubmed-meshheading:15814589-Microspheres,
pubmed-meshheading:15814589-Neoplasm Proteins,
pubmed-meshheading:15814589-Neutrophils,
pubmed-meshheading:15814589-Shear Strength
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pubmed:year |
2005
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pubmed:articleTitle |
PSGL-1 derived from human neutrophils is a high-efficiency ligand for endothelium-expressed E-selectin under flow.
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pubmed:affiliation |
Department of Chemical Engineering, 172 Stocker Center, Ohio University, Athens, OH 45701, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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