Linked Life Data

1383198

Source:http://linkedlifedata.com/resource/pubmed/id/1383198

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
28
pubmed:dateCreated
1992-11-16
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
267
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19846-53
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Lectin domain peptides from selectins interact with both cell surface ligands and Ca2+ ions.
pubmed:affiliation
Department of Medicine, W. K. Warren Medical Research Institute, University of Oklahoma Health Sciences Center, Oklahoma City.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't