| pubmed-article:7521878 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7521878 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:7521878 | lifeskim:mentions | umls-concept:C0027950 | lld:lifeskim |
| pubmed-article:7521878 | lifeskim:mentions | umls-concept:C1419941 | lld:lifeskim |
| pubmed-article:7521878 | lifeskim:mentions | umls-concept:C0870432 | lld:lifeskim |
| pubmed-article:7521878 | lifeskim:mentions | umls-concept:C1705417 | lld:lifeskim |
| pubmed-article:7521878 | lifeskim:mentions | umls-concept:C1555465 | lld:lifeskim |
| pubmed-article:7521878 | lifeskim:mentions | umls-concept:C0071488 | lld:lifeskim |
| pubmed-article:7521878 | pubmed:issue | 37 | lld:pubmed |
| pubmed-article:7521878 | pubmed:dateCreated | 1994-10-11 | lld:pubmed |
| pubmed-article:7521878 | 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. | lld:pubmed |
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| pubmed-article:7521878 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:7521878 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7521878 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7521878 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:7521878 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:7521878 | pubmed:author | pubmed-author:CummingsR DRD | lld:pubmed |
| pubmed-article:7521878 | pubmed:author | pubmed-author:LyonsD EDE | lld:pubmed |
| pubmed-article:7521878 | pubmed:author | pubmed-author:MooreK LKL | lld:pubmed |
| pubmed-article:7521878 | pubmed:author | pubmed-author:McEverR PRP | lld:pubmed |
| pubmed-article:7521878 | pubmed:author | pubmed-author:LichensteinH... | lld:pubmed |
| pubmed-article:7521878 | pubmed:author | pubmed-author:EatonS FSF | lld:pubmed |
| pubmed-article:7521878 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7521878 | pubmed:day | 16 | lld:pubmed |
| pubmed-article:7521878 | pubmed:volume | 269 | lld:pubmed |
| pubmed-article:7521878 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7521878 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7521878 | pubmed:pagination | 23318-27 | lld:pubmed |
| pubmed-article:7521878 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:7521878 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7521878 | pubmed:articleTitle | The P-selectin glycoprotein ligand from human neutrophils displays sialylated, fucosylated, O-linked poly-N-acetyllactosamine. | lld:pubmed |
| pubmed-article:7521878 | pubmed:affiliation | Department of Medicine, University of Oklahoma Health Sciences Center, Oklahoma City. | lld:pubmed |
| pubmed-article:7521878 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7521878 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:7521878 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:7521878 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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