ArticleThe EMBO journal1991
Molecular basis of a high affinity murine interleukin-5 receptor.
Article in The EMBO journal, 1991. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 112 citations in OpenAlex.
- Interleukin-5 receptor subunit oligomerization and rearrangement revealed by fluorescence resonance energy transfer imaging.The Journal of biological chemistry · 2008Article
- Cytokine receptor common beta chain as a potential activator of cytokine withdrawal-induced apoptosis.Molecular and cellular biology · 1999Article
- Review
- A critical role of Lyn and Fyn for B cell responses to CD38 ligation and interleukin 5.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- The murine DUB-1 gene is specifically induced by the betac subunit of interleukin-3 receptor.Molecular and cellular biology · 1996Article
- CD38 ligation induces tyrosine phosphorylation of Bruton tyrosine kinase and enhanced expression of interleukin 5-receptor alpha chain: synergistic effects with interleukin 5.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Detailed analysis of the IL-5-IL-5R alpha interaction: characterization of crucial residues on the ligand and the receptor.The EMBO journal · 1995Article
- Identification of receptor-binding domains on human interleukin 5 and design of an interleukin 5-derived receptor antagonist.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Impaired interleukin-3 (IL-3) response of the A/J mouse is caused by a branch point deletion in the IL-3 receptor alpha subunit gene.The EMBO journal · 1995Article
- Multi-colony stimulating activity of interleukin 5 (IL-5) on hematopoietic progenitors from transgenic mice that express IL-5 receptor alpha subunit constitutively.The Journal of experimental medicine · 1995Article
- IL-5 receptor-mediated tyrosine phosphorylation of SH2/SH3-containing proteins and activation of Bruton's tyrosine and Janus 2 kinases.The Journal of experimental medicine · 1994Article
- A critical cytoplasmic domain of the interleukin-5 (IL-5) receptor alpha chain and its function in IL-5-mediated growth signal transduction.Molecular and cellular biology · 1994Article
- Activation and inhibition of erythropoietin receptor function: role of receptor dimerization.Molecular and cellular biology · 1994Article
- Reconstitution of the functional receptors for murine and human interleukin 5.The Journal of experimental medicine · 1993Article
- Reconstituted human granulocyte-macrophage colony-stimulating factor receptor transduces growth-promoting signals in mouse NIH 3T3 cells: comparison with signalling in BA/F3 pro-B cells.Molecular and cellular biology · 1993Article
- Cell-type specific interaction of Neu differentiation factor (NDF/heregulin) with Neu/HER-2 suggests complex ligand-receptor relationships.The EMBO journal · 1993Article
- Inactivation of erythropoietin receptor function by point mutations in a region having homology with other cytokine receptors.Molecular and cellular biology · 1993Article
- Distinct downstream signaling mechanism between erythropoietin receptor and interleukin-2 receptor.The EMBO journal · 1992Article
- Critical cytoplasmic domains of the common beta subunit of the human GM-CSF, IL-3 and IL-5 receptors for growth signal transduction and tyrosine phosphorylation.The EMBO journal · 1992Article
- Molecular basis of the membrane-anchored and two soluble isoforms of the human interleukin 5 receptor alpha subunit.Proceedings of the National Academy of Sciences of the United States of America · 1992Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mouse interleukin-5 receptor (mIL-5R) consists of two components one of which, the mIL-5R alpha-chain, binds mIL-5 with low affinity. Recently we demonstrated that monoclonal antibodies (Mabs) recognizing the second mIL-5R beta-chain, immunoprecipitate a p130-140 protein doublet which corresponds to the mIL-3R and the mIL-3R-like protein, the latter chain for which so far no ligand has been identified. In this study we show that a high affinity mIL-5R can be reconstituted on COS1 cells by co-expression of the mIL-5R alpha-chain with the mIL-3R-like protein (beta-chain). Cross-linking of 125I-labeled mIL-5 to the COS1 cells co-transfected with both cDNAs revealed the same pattern as in B13 cells, i.e. two proteins of 60 and 130 kd which correspond to the low affinity mIL-5R alpha-chain and the mIL-3R-like protein, respectively. The dissociation rate of mIL-5 from this reconstituted high affinity site was lower than that of the low affinity site, whereas the association rate was unchanged. Nonetheless, the apparent dissociation constant (Kd) for this reconstituted receptor was still 10-fold higher than the Kd observed for B13 cells. Although the mIL-3R is greater than 90% homologous to the mIL-3R-like protein, no increase in affinity for mIL-5 was detected on COS1 cells co-transfected with the cDNAs for the mIL-5R alpha-chain and the mIL-3R protein.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.