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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
10
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pubmed:dateCreated |
1986-2-14
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pubmed:abstractText |
Two new murine monoclonal IgG1 antibodies, H-31 and H-A26, were characterized in comparison with two previously obtained monoclonal antibodies against human interleukin 2 (IL-2) receptor (IL-2 R), anti-Tac and HIEI. In immunofluorescence assays with various human hematopoietic cells, H-31 and H-A26 antibodies both reacted with only IL-2 R-positive cells, and they precipitated IL-2 R molecules, glycoproteins with molecular weights of 60K and 53K daltons (gp60/gp53), from human T-cell leukemia virus type I (HTLV-I)-carrying MT-2 cells, as demonstrated by sequential immunoprecipitation after absorption of IL-2 R with anti-Tac. Antibody-binding competition assays showed that H-31 and anti-Tac, and H-A26 and HIEI, respectively, competed reciprocally in binding to the cells, and that anti-Tac also inhibited the binding of HIEI but not vice versa. H-31, like anti-Tac, strongly inhibited the IL-2-dependent proliferation of normal activated T-cells, absorption of IL-2 and direct binding of IL-2 to the cells, while H-A26, like HIEI, inhibited those processes only weakly. The spectra of reactivities of these antibodies with various simian cell lines derived by HTLV-I infection were different, as revealed by immunofluorescence studies. Human IL-2 R was shown to express a unique antigenic determinant, detected with HIEI, that was not detectable in IL-2 R molecules of Old and New World monkeys, and also to express determinants common to simian IL-2 R molecules. These observations indicate that H-31 and H-A26 recognize human IL-2 R molecules and that the antigenic sites on the IL-2 R molecule defined by H-31, H-A26, anti-Tac, and HIEI are different.
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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/Antigens, CD27,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Phytohemagglutinins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Interleukin-2
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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 |
29
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
959-72
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:2417094-Animals,
pubmed-meshheading:2417094-Antibodies, Monoclonal,
pubmed-meshheading:2417094-Antibody Specificity,
pubmed-meshheading:2417094-Antigens, CD27,
pubmed-meshheading:2417094-Antigens, Surface,
pubmed-meshheading:2417094-Binding, Competitive,
pubmed-meshheading:2417094-Cell Transformation, Viral,
pubmed-meshheading:2417094-Deltaretrovirus,
pubmed-meshheading:2417094-Epitopes,
pubmed-meshheading:2417094-Haplorhini,
pubmed-meshheading:2417094-Humans,
pubmed-meshheading:2417094-Lymphocyte Activation,
pubmed-meshheading:2417094-Mice,
pubmed-meshheading:2417094-Phytohemagglutinins,
pubmed-meshheading:2417094-Receptors, Immunologic,
pubmed-meshheading:2417094-Receptors, Interleukin-2,
pubmed-meshheading:2417094-Species Specificity,
pubmed-meshheading:2417094-T-Lymphocytes
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pubmed:year |
1985
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pubmed:articleTitle |
Distinct reactivities of four monoclonal antibodies with human interleukin 2 receptor.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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