A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific α chain and a β chain shared with the receptor for GM-CSF

  title={A human high affinity interleukin-5 receptor (IL5R) is composed of an IL5-specific $\alpha$ chain and a $\beta$ chain shared with the receptor for GM-CSF},
  author={Jan Tavernier and Rene Devos and Sigrid Cornelis and Tania Tuypens and Jos{\'e} Van der Heyden and Walter Fiers and Geert Plaetinck},
A mutation of the common receptor subunit for interleukin-3 (IL-3), granulocyte-macrophage colony-stimulating factor, and IL-5 that leads to ligand independence and tumorigenicity.
The isolation of a mutant form of h beta c, from growth factor-independent cells, that arose spontaneously after infection of a murine factor-dependent hematopoietic cell line (FDC-P1) with a retroviral hbeta c expression construct is reported, suggesting that the large family of cytokine receptors has the capacity to become oncogenically active.
Functional reconstitution of the human interleukin-3 receptor.
Results indicate that human beta c is essential for hIL-3 signaling and that AIC2B is a murine equivalent of humanbeta c.
Interleukin-3 Binding to the Murine βIL-3 and Human βc Receptors Involves Functional Epitopes Formed by Domains 1 and 4 of Different Protein Chains*
It is shown that the domain 1 residues of the hβc receptor are important for high affinity IL-3 binding and receptor activation as shown previously for the related cytokines, interleukin-5 and granulocyte-macrophage colony-stimulating factor, which also signal through this receptor subunit.
Monoclonal Antibody Against the Common p Subunit ( Pc ) of the Human Interleukin-3 ( IL-3 ) , IL-5 , and Granulocyte-Macrophage Colony-Stimulating Factor Receptors Shows Upregulation of pc by IL-1 and Tumor Necrosis Factor-a By
Using a transfectant of NIH3T3 cells expressing the high-affinity human GM-CSF receptor, monoclonal antibodies (MoAbs) against pc were generated and expression of pc was examined.
A Single Tyrosine Residue in the Membrane-proximal Domain of the Granulocyte-Macrophage Colony-stimulating Factor, Interleukin (IL)-3, and IL-5 Receptor Common β-Chain Is Necessary and Sufficient for High Affinity Binding and Signaling by All Three Ligands*
Results show for the first time that a single residue in a shared receptor subunit acts as a binding determinant for different ligands and may have implications for other receptor systems where communal receptor subunits exhibit hydrophobic residues in their putative F′-G′ loops.
Cloning and characterization of the human interleukin-3 (IL-3)/IL-5/ granulocyte-macrophage colony-stimulating factor receptor betac gene: regulation by Ets family members.
These findings, together with the observation that cotransfection of PU.1 and other Ets family members enhances betac promoter activity in fibroblasts, reinforce the notion that GGAA elements play an important role in myeloid-specific gene regulation.
A critical cytoplasmic domain of the interleukin-5 (IL-5) receptor alpha chain and its function in IL-5-mediated growth signal transduction
Analysis using chimeric receptors suggested that dimerization of the cytoplasmic domain of beta c may be an important step in activating the IL-5R complex and transducing intracellular growth signals.
Molecular structure of the IL-3, GM-CSF and IL-5 receptors.
  • A. Miyajima
  • Biology, Chemistry
    International journal of cell cloning
  • 1992
Reconstitution of high-affinity receptors using molecularly cloned receptor subunits has revealed that the high-affinity receptors for interleukin 3 (IL-3), granulocyte-macrophage colony-stimulating
Characterization of potential antagonists of human interleukin 5 demonstrates their cross-reactivity with receptors for interleukin 3 and granulocyte-macrophage colony-stimulating factor.
The inhibition of the structurally closely related receptors for IL-5, IL-3 and GM-CSF by both compounds, while binding of interleukin-4 to its receptor was not affected, suggests that a similar reactive site exists in the ligand-binding domains of the receptor.
The cell surface expression level of the human interleukin-5 receptor alpha subunit determines the agonistic/antagonistic balance of the human interleukin-5 E13Q mutein.
It is shown that E13Q has a biological activity comparable to wild-type IL-5 only when a high number of alpha-chains is present on the cells, and treatment with suboptimal doses of a neutralising anti-IL-5R alpha antibody results in reduced activity of the mutant but not of wild- type IL- 5.


Characterization of high-affinity receptors for interleukin 5 on interleukin 5-dependent cell lines.
  • S. Mita, A. Tominaga, K. Takatsu
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1989
Interleukin 5 (IL-5) is a glycosylated polypeptide that acts as a key factor for B-cell growth and differentiation. We demonstrated previously that there are two classes (high and low affinity) of
Cloning and expression of a gene encoding an interleukin 3 receptor-like protein: identification of another member of the cytokine receptor gene family.
A monoclonal antibody to the interleukin 3 (IL-3) receptor (anti-Aic2) and a cDNA isolated from a mouse mast cell line which is homologous to the previously characterized gene for the IL-3 receptor (AIC2A) suggest a potential involvement of AIC2B in cytokine signal transduction.
Cloning of an interleukin-3 receptor gene: a member of a distinct receptor gene family.
A sequence comparison of the IL-3 receptor with other cytokine receptors revealed a common motif of a distinct receptor gene family, and additional components are required for a functional high affinity IL- 3 receptor.
Characterization of the murine IL-5 receptor complex with the use of a panel of monoclonal antibodies. Relationship to the murine IL-3 receptor.
The results presented here support a model for the mIL-5R consisting of the alpha-chain associated with the p140 (IL-3R-like), whereas the p130 (IL -3R) is not involved in the IL-5 R complex.
Signal transduction of the human granulocyte-macrophage colony-stimulating factor and interleukin-3 receptors involves tyrosine phosphorylation of a common set of cytoplasmic proteins.
The results suggest that tyrosine phosphorylation may be important for GM-CSF and IL-3 receptor-mediated signal transduction and that cell proliferation may be, at least partially, regulated by a balance between CSF-induced protein-tyrosine kinase activity and protein-Tyrosineosphatase activity.
Characterization of interleukin 5 receptors on eosinophilic sublines from human promyelocytic leukemia (HL-60) cells
The identification and characterization of human IL-5 receptors on HL-60 sublines should provide new insight into the role of this cytokine in eosinophil differentiation.
Molecular organization of the cytokine gene cluster, involving the human IL-3, IL-4, IL-5, and GM-CSF genes, on human chromosome 5.
P pulsed-field gel electrophoresis was used to prepare subchromosomal restriction maps surrounding these genes to define possible linkage more precisely and in situ hybridization evidence is presented that the human IL-4 gene is located at 5q23.3-31.2, suggesting that the four cytokine genes may be closely linked.
T Cell‐Replacing Factor (TRF)/Interleukin 5 (IL‐5): Molecular and Functional Properties
The translation product of murine TRF/IL-5 cDNA triggers resting as well as activated murine B cells for terminal differentiation into Ig-secreting cells (IgM, IgG1, or IgA) accompanied by increased mRNA expression for secreted forms of relevant Ig heavy chain (mu, gamma, or alpha).