Characterization of high-affinity receptors for interleukin 5 on interleukin 5-dependent cell lines.

Mita, Seiji; Tominaga, Akira; Hitoshi, Yasumichi; Saito, Kiyoshi; Honjo, Tasuku; Akagi, Masanobu; Kikuchi, Yuji; Yamaguchi, Naoto; Takatsu, Kiyoshi

doi:10.1073/pnas.86.7.2311

Cited by 95 publications

(52 citation statements)

References 27 publications

(23 reference statements)

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“…Binding data were analyzed by Scatchard analysis with the EBDA and LIGAND computer programs (Elsevier-BIOSOFT, Cambridge, United Kingdom). Cross-linking experiments were performed by a method described previously (22). In brief, 5 x 106 cells were incubated with "2I-labeled mIL-5, collected, and resuspended in 500 RI of Hanks balanced salt solution (HBSS) containing 1 mM disuccinimidyl tartarate (Pierce Chemical Co.).…”

Section: Methodsmentioning

confidence: 99%

“…Binding of mIL-5 to transfected cells was achieved with '251-labeled mIL-5 as described previously (22). Binding data were analyzed by Scatchard analysis with the EBDA and LIGAND computer programs (Elsevier-BIOSOFT, Cambridge, United Kingdom).…”

Section: Methodsmentioning

confidence: 99%

“…Murine IL-5 (mIL-5) was prepared and purified with anti-mIL-5 monoclonal antibody (MAb)-coupled beads as described previously (22). Rat MAb against mIL-SRa (H7) (12,44) Cells and transfection.…”

Section: Methodsmentioning

confidence: 99%

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A critical cytoplasmic domain of the interleukin-5 (IL-5) receptor alpha chain and its function in IL-5-mediated growth signal transduction.

Takaki¹,

Kanazawa²,

Shiiba³

et al. 1994

Mol. Cell. Biol.

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124

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Interleukin-5 (IL-5) regulates the production and function of B cells, eosinophils, and basophils. The IL-S receptor (IL-5R) consists of two distinct membrane proteins, a and P. The a chain (IL-5Ra) is specific to IL-5.The chain is the common ,1 chain (Ic) of receptors for IL-3 and granulocyte-macrophage colony-stimulating factor (GM-CSF). The cytoplasmic domains of both a and I1 chains are essential for signal transduction. In this study, we generated cDNAs of IL-5Ra having various mutations in their cytoplasmic domains and examined the function of these mutants by expressing them in IL-3-dependent FDC-P1 cells. The membraneproximal proline-rich sequence of the cytoplasmic domain of IL-5Ra, which is conserved among the a chains of IL-SR, IL-3R, and GM-CSF receptor (GM-CSFR), was found to be essential for the IL-5-induced proliferative response, expression of nuclear proto-oncogenes such as c-jun, c-fos, and c-myc, and tyrosine phosphorylation of cellular proteins including JAK2 protein-tyrosine kinase. In addition, analysis using chimeric receptors which consist of the extracellular domain of IL-5Ra and the cytoplasmic domain of Dc suggested that dimerization of the cytoplasmic domain of ,c may be an important step in activating the IL-5R complex and transducing intracellular growth signals.Interleukin-5 (IL-5) is a cytokine that regulates the production and function of B cells, eosinophils, and basophils (40). The IL-5 receptor (IL-5R) consists of two distinct membrane proteins, ao and P. IL-SRa alone specifically binds IL-5 but with low affinity (27,39). While the P chain does not bind IL-5 by itself, it does form a high-affinity IL-SR in combination with IL-5Rox (6, 37, 38,41). The P chain is the common P3 chain (,c) of receptors for IL-3 and granulocyte-macrophage colonystimulating factor (GM-CSF) (23). 1c forms high-affinity receptors for IL-3 and GM-CSF, the ligands of which bind specifically with IL-3Ra and the a chain of GM-CSF receptor (GM-CSFRa), respectively (7,9,10,16,29). Pc is not only required for high-affinity binding but also essential for signal transduction. IL-5, IL-3, and GM-CSF have several overlapping functions, especially in eosinophils (23,33,40). The ,c shared by the receptors of these three cytokines provides a molecular basis for the functional redundancy of these cytokines.The extracellular domains of the a chains and ,c are similar among members of the cytokine receptor superfamily. The a. chains have a short cytoplasmic domain (-55 amino acid residues) with a short amino acid sequence which is conserved among these a chains (16,39). In contrast, ,3c has a relatively large cytoplasmic domain (-440 amino acid residues). Although the cytoplasmic domains of the a chains and ,Bc have no homology with signaling molecules such as kinases, phosphatases, nucleotide-binding proteins, and src homology domains, it has been well established that IL-5, IL-3, and GM-CSF induce rapid tyrosine phosphorylation of cellular proteins (13,24,28) as well as transcription of nuclear proto-oncogenes (3). ...

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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A critical cytoplasmic domain of the interleukin-5 (IL-5) receptor alpha chain and its function in IL-5-mediated growth signal transduction.

Takaki¹,

Kanazawa²,

Shiiba³

et al. 1994

Mol. Cell. Biol.

Self Cite

124

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“…IL-5, mainly produced by activated Th2 cells and mast cells, acts on B-1 and B-2 cells to induce proliferation and differentiation into Ig-producing cells (22)(23)(24)(25). IL-5 also controls the production and functions of eosinophils and basophils.…”

mentioning

confidence: 99%

The Role of IL-5 for Mature B-1 Cells in Homeostatic Proliferation, Cell Survival, and Ig Production

Moon¹,

Takaki²,

Miyake

et al. 2004

The Journal of Immunology

125

107

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B-1 cells, distinguishable from conventional B-2 cells by their cell surface marker, anatomical location, and self-replenishing activity, play an important role in innate immune responses. B-1 cells constitutively express the IL-5R α-chain (IL-5Rα) and give rise to Ab-producing cells in response to various stimuli, including IL-5 and LPS. Here we report that the IL-5/IL-5R system plays an important role in maintaining the number and the cell size as well as the functions of mature B-1 cells. The administration of anti-IL-5 mAb into wild-type mice, T cell-depleted mice, or mast cell-depleted mice resulted in reduction in the total number and cell size of B-1 cells to an extent similar to that of IL-5Rα-deficient (IL-5Rα−/−) mice. Cell transfer experiments have demonstrated that B-1 cell survival in wild-type mice and homeostatic proliferation in recombination-activating gene 2-deficient mice are impaired in the absence of IL-5Rα. IL-5 stimulation of wild-type B-1 cells, but not IL-5Rα−/− B-1 cells, enhances CD40 expression and augments IgM and IgG production after stimulation with anti-CD40 mAb. Enhanced IgA production in feces induced by the oral administration of LPS was not observed in IL-5Rα−/− mice. Our results illuminate the role of IL-5 in the homeostatic proliferation and survival of mature B-1 cells and in IgA production in the mucosal tissues.

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“…Cloning of cDNA for murine IL-5 and production of monoclonal antibodies against IL-5 and its receptor enabled us to characterize the IL-5 receptor on a variety of cells (10,13,17,18,34). Recently, we have investigated the intracellular mechanisms of the differentiation of B cells induced by IL-5 and found that activities of stimulatory and inhibitory kinases may be involved in the IL-5-mediated differentiation process (33).…”

mentioning

confidence: 99%

Elevated Expression of Proto‐Oncogenes during Interleukin‐5‐Induced Growth and Differentiation of Murine B Lineage Cells

Migita

Yamaguchi²,

Katoh³

et al. 1990

Microbiology and Immunology

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Interleukin 5 (IL-5), a lymphokine produced by helper T cells, is involved in the regulation of growth and differentiation of B cells and other hematopoietic cells. To elucidate IL-5-mediated intracellular mechanisms, we have established. IL-5-dependent and -independent murine early B cell lines, J6 and MJ88-1, respectively, and examined the effect of IL-5 on the expression of proto-oncogenes during proliferation. Two-to 3.5-fold increases in the levels of c-myb, c-myc, c-fos, and mRNA were observed in J6 cells, compared with those in MJ88-1 cells. Further, a role of IL-5 in the proto-oncogene expression during differentiation was examined by using thymidine-treated murine B-cell chronic leukemia BCL1-B20 cells with growth arrest.After 4-day culture, the amount of IgM secreted from BCL1-B20 cells was augmented 4-6 fold in the presence of IL-5.Although expression of c-myb, c-fos, and c-fms mRNA did not change, only c-myc mRNA expression was elevated within 30 min of stimulation with IL-5 and reached a maximal level by 1 hr. Addition of phorbol 12-myristate 13-acetate (PMA) or IL-4 to the culture of BCL1-B20 cells inhibited both the IL-5-mediated augmentation of IgM secretion and the elevated expression of c-myc mRNA.These findings suggest that the IL-5 signal may be associated with the up-regulation of c-myc expression.Recently, proto-oncogenes have been in the forefront of potential factors involved in proliferation and differentiation of hematopoietic progenitor cells. The increased expression of c-myc, c-fos, and c-myb proto-oncogenes has been shown in the growth factor-induced proliferation of various cells including normal human T, B cells and mouse fibroblasts (9,15,26). In contrast, decreased expression of c-myc, c-myb proto-oncogenes was observed during the differentiation of human cell lines, HL-60, and U-937 into granulocytes and monocytes, respectively (5, 31).Interleukin-5 (IL-5) is a T cell-derived soluble factor that enhances the proliferation and differentiation of B cells as well as eosinophils (21,27,35). Cloning of cDNA for murine IL-5 and production of monoclonal antibodies against IL-5 937

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Characterization of high-affinity receptors for interleukin 5 on interleukin 5-dependent cell lines.

Cited by 95 publications

References 27 publications

A critical cytoplasmic domain of the interleukin-5 (IL-5) receptor alpha chain and its function in IL-5-mediated growth signal transduction.

A critical cytoplasmic domain of the interleukin-5 (IL-5) receptor alpha chain and its function in IL-5-mediated growth signal transduction.

The Role of IL-5 for Mature B-1 Cells in Homeostatic Proliferation, Cell Survival, and Ig Production

Elevated Expression of Proto‐Oncogenes during Interleukin‐5‐Induced Growth and Differentiation of Murine B Lineage Cells

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