Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6122
|
| pubmed:dateCreated |
1987-7-9
|
| pubmed:abstractText |
Although activated human T and B lymphocytes express both high-affinity and low-affinity membrane receptors for interleukin-2 (IL-2), the structural features that distinguish these receptors have remained unresolved. The high-affinity receptors appear to mediate IL-2 induced T cell growth and internalization of IL-2, whereas no function has yet been ascribed to the low-affinity receptors. The Tac antigen is an IL-2 binding protein of relative molecular mass 55,000 (Mr 55K) that participates in the formation of both high- and low-affinity receptors. But Tac complementary DNA transfection and membrane fusion studies have suggested that additional T-cell components are required to produce high-affinity IL-2 receptors. In this study, we report the identification of a second human IL-2 binding protein that (1) has an Mr of approximately 70K, (2) lacks reactivity with the anti-Tac antibody, (3) binds IL-2 with intermediate affinity and (4) is present on the surface of resting T cells, large granular lymphocytes (natural killer cells), and certain T and B cell lines in the absence of the Tac antigen. Chemical crosslinking of 125I-labelled IL-2 bound to high-affinity IL-2 receptors produces labelling of both the p70 protein and the Tac antigen and the anti-Tac antibody blocks the crosslink detection of both of these proteins. Expression of Tac cDNA in a T cell line expressing the p70 protein, but lacking both Tac and high-affinity receptors, results in the reconstitution of high-affinity IL-2 receptors in these cells. Together, these findings suggest that the high-affinity human IL-2 receptor may be a membrane complex composed of at least the p70 protein and Tac antigen.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:issn |
0028-0836
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
327
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
518-22
|
| pubmed:dateRevised |
2003-11-14
|
| pubmed:meshHeading |
pubmed-meshheading:3108674-Animals,
pubmed-meshheading:3108674-B-Lymphocytes,
pubmed-meshheading:3108674-Cell Line,
pubmed-meshheading:3108674-Interleukin-2,
pubmed-meshheading:3108674-Kinetics,
pubmed-meshheading:3108674-Molecular Weight,
pubmed-meshheading:3108674-Receptors, Immunologic,
pubmed-meshheading:3108674-Receptors, Interleukin-2,
pubmed-meshheading:3108674-Recombinant Proteins,
pubmed-meshheading:3108674-T-Lymphocytes
|
| pubmed:articleTitle |
A second human interleukin-2 binding protein that may be a component of high-affinity interleukin-2 receptors.
|
| pubmed:publicationType |
Journal Article
|