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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
8
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pubmed:dateCreated |
1989-1-23
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pubmed:abstractText |
The present study demonstrated that various reagents can specifically reduce the affinity of high-affinity interleukin 2 receptor (IL-2R) but not that of low-affinity IL-2R. They included lectins such as wheat germ agglutinin (WGA), concanavalin A and phytohemagglutinin, and a chemical cross-linker, glutaraldehyde, in addition to anti-IL-2R monoclonal antibodies, HIEI and H-47. The affinity of the high-affinity IL-2R was reduced when the cells were treated with WGA or H-47 before, but not after, addition of 125I-labeled interleukin 2 (IL-2). Their inhibitory effects were also demonstrated by the chemical cross-linking method. On treatment with the reagents, the IL-2 binding to both IL-2R alpha and beta chains was inhibited and these inhibitory effects were seen only when the reagents were added before IL-2 addition, like their high-affinity reducing effects. These results support a supposition that the high affinity IL-2R is generated by assembly of the alpha and beta chains, and suggest that the IL-2 binding to IL-2R alpha and beta chains could induce stable constitution of the high-affinity state of IL-2R, but these affinity modulating reagents could perturb the optimum association between alpha and beta chains to generate the high-affinity IL-2R.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents,
http://linkedlifedata.com/resource/pubmed/chemical/Glutaral,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Wheat Germ Agglutinins
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pubmed:status |
MEDLINE
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pubmed:issn |
0385-5600
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
857-67
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3143899-Antibodies, Monoclonal,
pubmed-meshheading:3143899-Binding Sites,
pubmed-meshheading:3143899-Cells, Cultured,
pubmed-meshheading:3143899-Cross-Linking Reagents,
pubmed-meshheading:3143899-Glutaral,
pubmed-meshheading:3143899-Interleukin-2,
pubmed-meshheading:3143899-Kinetics,
pubmed-meshheading:3143899-Lectins,
pubmed-meshheading:3143899-Molecular Weight,
pubmed-meshheading:3143899-Protein Conformation,
pubmed-meshheading:3143899-Receptors, Interleukin-2,
pubmed-meshheading:3143899-Wheat Germ Agglutinins
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pubmed:year |
1988
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pubmed:articleTitle |
Selective inhibition of high- but not low-affinity interleukin 2 binding by lectins and anti-interleukin 2 receptor alpha antibody.
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pubmed:affiliation |
Institute for Virus Research, Kyoto University.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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