Linked Life Data

9414280

Source:http://linkedlifedata.com/resource/pubmed/id/9414280

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1998-2-2
pubmed:abstractText
Interactions between P-selectin and P-selectin glycoprotein ligand-1 (PSGL-1) mediate the earliest "rolling" of leukocytes on the lumenal surface of endothelial cells at sites of inflammation. Previously, PSGL-1 has been shown to be the primary mediator of interactions between neutrophils and P-selectin, but studies on the ability of PSGL-1 to mediate interactions between P-selectin and other subsets of leukocytes have yielded variable and conflicting results. A novel IgG monoclonal antibody (MoAb) to human PSGL-1 was generated, and the specificity of this MoAb was confirmed by both flow cytometric analysis and Western blotting of cells transfected with human PSGL-1. This newly developed MoAb, KPL1, inhibited interactions between P-selectin expressing COS cells and either HL60 cells, neutrophils, or lymphocytes. Furthermore, KPL1 completely inhibited interactions between P-selectin and either purified CD4 T cells or neutrophils in a flow assay under physiological conditions, but had no effect on interactions of T cells or neutrophils with E-selectin. In addition, KPL1 blocked interactions between lymphoid cells transfected with L-selectin and COS cells expressing PSGL-1. The KPL1 epitope was mapped to a site within a consensus tyrosine sulfation motif of PSGL-1, previously shown to be essential for interaction with P-selectin and now shown to be essential for interaction with L-selectin, and to be distinct from the epitope identified by the PL1 function blocking anti-PSGL-1 MoAb. Two-color flow cytometry of normal leukocytes showed that while natural killer (NK) cells (CD16(+)), monocytes, CD4 and CD8 T cells, and alpha/beta and gamma/delta T cells were uniformly positive for PSGL-1, B cells expressed low levels of the KPL1 epitope. This low level of KPL1 staining was also observed immunohistologically in germinal centers, which had no detectable KPL1 staining, whereas T-cell areas (interfollicular region) were positive for KPL1. Interestingly, plasma cells in situ and interleukin-6-dependent myeloma cell lines were KPL1(+). Thus, PSGL-1 is expressed on essentially all blood neutrophils, NK cells, B cells, T cells, and monocytes. Variation in tyrosine sulfation during B-cell differentiation may affect the ability of B cells to interact with P- and L-selectin.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-4971
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
91
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
154-64
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:9414280-Animals, pubmed-meshheading:9414280-Antibodies, Monoclonal, pubmed-meshheading:9414280-Antibody Specificity, pubmed-meshheading:9414280-COS Cells, pubmed-meshheading:9414280-Cell Differentiation, pubmed-meshheading:9414280-Cell Movement, pubmed-meshheading:9414280-Consensus Sequence, pubmed-meshheading:9414280-DNA, Complementary, pubmed-meshheading:9414280-Epitopes, pubmed-meshheading:9414280-HL-60 Cells, pubmed-meshheading:9414280-Humans, pubmed-meshheading:9414280-L-Selectin, pubmed-meshheading:9414280-Ligands, pubmed-meshheading:9414280-Lymphocyte Subsets, pubmed-meshheading:9414280-Membrane Glycoproteins, pubmed-meshheading:9414280-Mice, pubmed-meshheading:9414280-Monocytes, pubmed-meshheading:9414280-Neutrophils, pubmed-meshheading:9414280-P-Selectin, pubmed-meshheading:9414280-Protein Processing, Post-Translational, pubmed-meshheading:9414280-Recombinant Fusion Proteins, pubmed-meshheading:9414280-Sulfates, pubmed-meshheading:9414280-Transfection, pubmed-meshheading:9414280-Tyrosine
pubmed:year
1998
pubmed:articleTitle
A novel P-selectin glycoprotein ligand-1 monoclonal antibody recognizes an epitope within the tyrosine sulfate motif of human PSGL-1 and blocks recognition of both P- and L-selectin.
pubmed:affiliation
Department of Microbiology/Immunology, Northwestern University Medical School, Chicago, IL 60611, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't