| pubmed-article:1383198 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:1383198 | lifeskim:mentions | umls-concept:C0699040 | lld:lifeskim |
| pubmed-article:1383198 | lifeskim:mentions | umls-concept:C0282651 | lld:lifeskim |
| pubmed-article:1383198 | lifeskim:mentions | umls-concept:C0022023 | lld:lifeskim |
| pubmed-article:1383198 | lifeskim:mentions | umls-concept:C0023206 | lld:lifeskim |
| pubmed-article:1383198 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:1383198 | lifeskim:mentions | umls-concept:C1514562 | lld:lifeskim |
| pubmed-article:1383198 | lifeskim:mentions | umls-concept:C1883221 | lld:lifeskim |
| pubmed-article:1383198 | lifeskim:mentions | umls-concept:C0023688 | lld:lifeskim |
| pubmed-article:1383198 | lifeskim:mentions | umls-concept:C0596235 | lld:lifeskim |
| pubmed-article:1383198 | lifeskim:mentions | umls-concept:C1883204 | lld:lifeskim |
| pubmed-article:1383198 | lifeskim:mentions | umls-concept:C1880389 | lld:lifeskim |
| pubmed-article:1383198 | pubmed:issue | 28 | lld:pubmed |
| pubmed-article:1383198 | pubmed:dateCreated | 1992-11-16 | lld:pubmed |
| pubmed-article:1383198 | pubmed:abstractText | Selectins are receptors that mediate leukocyte adhesion to platelets or endothelial cells through Ca(2+)-dependent interactions with cell surface oligosaccharides. We found that peptides corresponding to residues 23-30, 54-63, and 70-79 of the N-terminal lectin domain of P-selectin inhibited leukocyte adhesion to P-selectin. Peptides corresponding to the homologous 23-30 and 54-63 regions of E-selectin and L-selectin also prevented cell binding to P-selectin. Immobilized albumin conjugates of the three P-selectin peptides supported adhesion of myeloid cells and certain other cells expressing fucosylated oligosaccharides. Ca2+ was required for optimal cell adhesion to the conjugates containing the 23-30 and 54-63 sequences. Furthermore, Ca2+ interacted with the 23-30 and 54-63 peptides of all three selectins, as detected by changes in intrinsic fluorescence emission intensity. These data suggest that residues contained within the 23-30 and 54-63 regions of the selectins represent contact sites for carbohydrate structures on target cells. Furthermore, binding of Ca2+ to these sequences may directly enhance their ability to interact with cell surface ligands. | lld:pubmed |
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| pubmed-article:1383198 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:1383198 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:1383198 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:1383198 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:1383198 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:1383198 | pubmed:author | pubmed-author:HeavnerG AGA | lld:pubmed |
| pubmed-article:1383198 | pubmed:author | pubmed-author:McEverR PRP | lld:pubmed |
| pubmed-article:1383198 | pubmed:author | pubmed-author:HONGS SSS | lld:pubmed |
| pubmed-article:1383198 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:1383198 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:1383198 | pubmed:volume | 267 | lld:pubmed |
| pubmed-article:1383198 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:1383198 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:1383198 | pubmed:pagination | 19846-53 | lld:pubmed |
| pubmed-article:1383198 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
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| pubmed-article:1383198 | pubmed:year | 1992 | lld:pubmed |
| pubmed-article:1383198 | pubmed:articleTitle | Lectin domain peptides from selectins interact with both cell surface ligands and Ca2+ ions. | lld:pubmed |
| pubmed-article:1383198 | pubmed:affiliation | Department of Medicine, W. K. Warren Medical Research Institute, University of Oklahoma Health Sciences Center, Oklahoma City. | lld:pubmed |
| pubmed-article:1383198 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:1383198 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:1383198 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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