Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
37
|
| pubmed:dateCreated |
1994-10-11
|
| pubmed:abstractText |
We previously demonstrated that P-selectin binds with high affinity to a trace, homodimeric glycoprotein ligand on human myeloid cells. The ligand carries the sialyl Lewis x (sLe(x)) epitope, a limited number of N-linked glycans, and clustered, sialylated O-linked glycans. In this study we demonstrate that the polypeptide component of this ligand is identical to that of P-selectin glycoprotein ligand-1 (PSGL-1), a molecule recently identified by expression cloning from a human myeloid cell cDNA library. We have examined the effects of glycosidases on purified, radioiodinated PSGL-1 from human neutrophils to further characterize the structure and function of the attached oligosaccharides. We found that PSGL-1 had poly-N-acetyllactosamine, only some of which could be removed with endo-beta-galactosidase. The majority of the Le(x) and sLe(x) structures were on endo-beta-galactosidase-sensitive chains. Peptide:N-glycosidase F (PNGaseF) treatment removed at least two of the three possible N-linked oligosaccharides from PSGL-1. Expression of Le(x) and sLe(x) was not detectably altered by PNGaseF digestion, indicating that these structures were primarily on O-linked poly-N-acetyllactosamine. Endo-beta-galactosidase-treated PSGL-1 retained the ability to bind to P-selectin, suggesting that some of the oligosaccharides recognized by P-selectin were either on enzyme-resistant poly-N-acetyllactosamine or on chains which lack poly-N-acetyllactosamine. PNGaseF treatment did not affect the ability of PSGL-1 to bind to P-selectin, demonstrating that the oligosaccharides required for P-selectin recognition are O-linked. PSGL-1 also bound to E-selectin, but with at least 50-fold lower affinity than to P-selectin. These data suggest that PSGL-1 from human neutrophils displays complex, sialylated, and fucosylated O-linked poly-N-acetyllactosamine that promote high affinity binding to P-selectin, but not to E-selectin.
|
| pubmed:grant | |
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/E-Selectin,
http://linkedlifedata.com/resource/pubmed/chemical/Fucose,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoside Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Immune Sera,
http://linkedlifedata.com/resource/pubmed/chemical/N-Acetylneuraminic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Oligodeoxyribonucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Oligosaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/P-Selectin,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Platelet Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Polysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/Sialic Acids,
http://linkedlifedata.com/resource/pubmed/chemical/poly-N-acetyllactosamine
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Sep
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
16
|
| pubmed:volume |
269
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
23318-27
|
| pubmed:dateRevised |
2007-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:7521878-Amino Acid Sequence,
pubmed-meshheading:7521878-Animals,
pubmed-meshheading:7521878-Base Sequence,
pubmed-meshheading:7521878-CHO Cells,
pubmed-meshheading:7521878-Carbohydrate Sequence,
pubmed-meshheading:7521878-Cell Adhesion Molecules,
pubmed-meshheading:7521878-Cricetinae,
pubmed-meshheading:7521878-E-Selectin,
pubmed-meshheading:7521878-Fucose,
pubmed-meshheading:7521878-Glycoproteins,
pubmed-meshheading:7521878-Glycoside Hydrolases,
pubmed-meshheading:7521878-Humans,
pubmed-meshheading:7521878-Immune Sera,
pubmed-meshheading:7521878-Molecular Sequence Data,
pubmed-meshheading:7521878-N-Acetylneuraminic Acid,
pubmed-meshheading:7521878-Neutrophils,
pubmed-meshheading:7521878-Oligodeoxyribonucleotides,
pubmed-meshheading:7521878-Oligosaccharides,
pubmed-meshheading:7521878-P-Selectin,
pubmed-meshheading:7521878-Peptides,
pubmed-meshheading:7521878-Platelet Membrane Glycoproteins,
pubmed-meshheading:7521878-Polysaccharides,
pubmed-meshheading:7521878-Sialic Acids
|
| pubmed:year |
1994
|
| pubmed:articleTitle |
The P-selectin glycoprotein ligand from human neutrophils displays sialylated, fucosylated, O-linked poly-N-acetyllactosamine.
|
| pubmed:affiliation |
Department of Medicine, University of Oklahoma Health Sciences Center, Oklahoma City.
|
| pubmed:publicationType |
Journal Article,
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
|