Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
5
|
| pubmed:dateCreated |
1998-8-17
|
| pubmed:abstractText |
Interleukin 2 (IL-2)- and IL-4-mediated stimulation of survival and growth, reflected by the induction of bcl2 and c-myc, respectively, depends on the integrity of the membrane-proximal region (S-region) in the IL-2 receptor beta-chain (IL-2R beta) and the haematopoietin homology box1-containing region of the IL-4 receptor alpha-chain (IL-4R alpha). In contrast to IL-4, IL-2 induces the expression of c-fos and c-jun family genes, mediated by the acidic region (A-region) within the cytoplasmic domain of IL-2R beta. A highly acidic motif is also present in IL-4R alpha, and evidence in favour and against its importance has been published. The authors have constructed chimeric receptors between IL-2R beta and IL-4R alpha by substitution of either the S-region or the A-region of IL-2R beta with sequences derived from IL-4R alpha. These chimeras were stably transfected into BA/F3 cells and assayed for the capacity to restore functions of IL-2 beta, such as growth mediation by IL-2 and the induction of proto-oncogenes (c-myc, c-junB and c-fos). Replacement of both the S- and A-region of IL-2R beta with IL-4R alpha derived regions of similar size and cytoplasmic location supported growth-stimulation by IL-2 as well as proto-oncogene induction. In contrast, all IL-2R functions were lost by exchange of the S-region with the corresponding part of IL-4R alpha. Induction of c-junB and c-fos RNA as an indicator of A-region function, however, was maintained in an IL-2R beta chimera containing the acidic box-bearing region of IL-4R alpha. These data indicate a functional role of the acidic region in the IL-4R alpha-chain.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
May
|
| pubmed:issn |
1043-4666
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
10
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
331-6
|
| pubmed:dateRevised |
2005-11-17
|
| pubmed:meshHeading |
pubmed-meshheading:9619370-Animals,
pubmed-meshheading:9619370-Binding Sites,
pubmed-meshheading:9619370-Cell Division,
pubmed-meshheading:9619370-Cell Line,
pubmed-meshheading:9619370-Cloning, Molecular,
pubmed-meshheading:9619370-Cytoplasm,
pubmed-meshheading:9619370-Gene Expression Regulation,
pubmed-meshheading:9619370-Genes, Immediate-Early,
pubmed-meshheading:9619370-Humans,
pubmed-meshheading:9619370-Mice,
pubmed-meshheading:9619370-Mutagenesis,
pubmed-meshheading:9619370-RNA, Messenger,
pubmed-meshheading:9619370-Receptors, Interleukin-2,
pubmed-meshheading:9619370-Receptors, Interleukin-4,
pubmed-meshheading:9619370-Recombinant Fusion Proteins
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Function of the human interleukin 4 receptor (IL-4R)-derived acidic motif revealed by cytoplasmic domain chimeras of the IL-4R alpha chain and the IL-2R beta chain.
|
| pubmed:affiliation |
Novartis Research Institute, Department of Immunology, Vienna, Austria.
|
| pubmed:publicationType |
Journal Article
|