rdf:type |
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lifeskim:mentions |
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pubmed:issue |
35
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pubmed:dateCreated |
1989-1-20
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pubmed:abstractText |
IL2-PE40 is a chimeric protein composed of human interleukin 2 (IL2) genetically fused to the amino terminus of a modified form of pseudomonas exotoxin (PE). Internalization of IL2 via the individual p55 and p70 subunits of the IL2 receptor was studied using IL2-PE40 on several mouse and human cell lines expressing either the p55, the p70, or both IL2 receptor subunits. Internalization was assessed by measuring inhibition of protein synthesis caused by the toxin moiety of IL2-PE40. The results demonstrate that IL2 internalization is mediated by either the p55 receptor subunit or by the p70 subunit but is much more efficient when high affinity receptors composed of both subunits are present. IL2-PE40 is a powerful reagent for studying IL2 receptor interactions and for analyzing pathways of the immune response and its regulation.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADP Ribose Transferases,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Exotoxins,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Macromolecular Substances,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Transferrin,
http://linkedlifedata.com/resource/pubmed/chemical/Virulence Factors,
http://linkedlifedata.com/resource/pubmed/chemical/toxA protein, Pseudomonas aeruginosa
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author |
|
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
263
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
18650-6
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:3143716-ADP Ribose Transferases,
pubmed-meshheading:3143716-Animals,
pubmed-meshheading:3143716-Antibody Formation,
pubmed-meshheading:3143716-Bacterial Toxins,
pubmed-meshheading:3143716-Binding, Competitive,
pubmed-meshheading:3143716-Cell Line,
pubmed-meshheading:3143716-Cell Survival,
pubmed-meshheading:3143716-Exotoxins,
pubmed-meshheading:3143716-Haplorhini,
pubmed-meshheading:3143716-Humans,
pubmed-meshheading:3143716-Interleukin-2,
pubmed-meshheading:3143716-Macromolecular Substances,
pubmed-meshheading:3143716-Mice,
pubmed-meshheading:3143716-Molecular Weight,
pubmed-meshheading:3143716-Receptors, Interleukin-2,
pubmed-meshheading:3143716-Transferrin,
pubmed-meshheading:3143716-Virulence Factors
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pubmed:year |
1988
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pubmed:articleTitle |
Interleukin 2 (IL2) PE40 is cytotoxic to cells displaying either the p55 or p70 subunit of the IL2 receptor.
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pubmed:affiliation |
Laboratory of Molecular Biology, National Cancer Institute, Bethesda, Maryland 20892.
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pubmed:publicationType |
Journal Article
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