Source:http://linkedlifedata.com/resource/pubmed/id/10807781
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
2000-6-13
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pubmed:abstractText |
Selective eosinophil accumulation is a hallmark of diseases such as asthma. In a model of chronic eosinophilic inflammation, we have previously shown that the tethering step in eosinophil adhesion is mediated by PSGL-1 binding to P-selectin. The Th2-associated cytokine IL-13 is of potential importance in allergic disease. We have therefore investigated whether IL-13 can mediate eosinophil binding to human umbilical vein endothelial cells (HUVEC) through P-selectin. IL-13 caused dose- and time-dependent increases of P-selectin expression, as assessed by flow and laser scanning cytometry. A similar degree of expression was observed with IL-4. There was no effect on E-selectin or ICAM-1 expression. Tumor necrosis factor-alpha induced the expression of VCAM-1, E-selectin, and ICAM-1 but had no effect on P-selectin expression. IL-13 increased the production of mRNA for surface and soluble variants of P-selectin. Under flow conditions, eosinophils, but not neutrophils, showed enhanced binding to IL-13 and to IL-4-stimulated HUVEC compared to medium-cultured cells. Eosinophil adhesion was completely inhibited by a blocking monoclonal antibody against PSGL-1 and P-selectin. Anti-VLA-4 and anti-VCAM-1 antibodies inhibited binding to a lesser extent. Thus, at physiologic levels of expression induced by Th2 cytokines, P-selectin/PSGL-1 supported eosinophil but not neutrophil adhesion. This mechanism is likely to be a key event leading to the selective accumulation of eosinophils in allergic inflammation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-13,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/P-Selectin,
http://linkedlifedata.com/resource/pubmed/chemical/P-selectin ligand protein
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0006-4971
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
95
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3146-52
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:10807781-Animals,
pubmed-meshheading:10807781-Cell Adhesion,
pubmed-meshheading:10807781-Cell Differentiation,
pubmed-meshheading:10807781-Cells, Cultured,
pubmed-meshheading:10807781-Dose-Response Relationship, Drug,
pubmed-meshheading:10807781-Endothelium, Vascular,
pubmed-meshheading:10807781-Eosinophils,
pubmed-meshheading:10807781-Humans,
pubmed-meshheading:10807781-Interleukin-13,
pubmed-meshheading:10807781-Ligands,
pubmed-meshheading:10807781-Membrane Glycoproteins,
pubmed-meshheading:10807781-Mice,
pubmed-meshheading:10807781-Neutrophils,
pubmed-meshheading:10807781-P-Selectin
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pubmed:year |
2000
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pubmed:articleTitle |
Interleukin-13 induces PSGL-1/P-selectin-dependent adhesion of eosinophils, but not neutrophils, to human umbilical vein endothelial cells under flow.
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pubmed:affiliation |
Division of Respiratory Medicine, University of Leicester School of Medicine, Glenfield Hospital, Leicester, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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