Receptors for T cell-replacing factor/interleukin 5. Specificity, quantitation, and its implication.

Mita, Seiji; Harada, Nobuyuki; Naomi, Shojiro; Hitoshi, Yasumichi; Saito, Kiyoshi; Akagi, Masanobu; Tominaga, Akira; Takatsu, Kiyoshi

doi:10.1084/jem.168.3.863

Cited by 76 publications

(32 citation statements)

References 50 publications

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“…At present, we have no definite evidence supporting either of these models. In our previous studies using chemical cross-linking of radiolabeled IL-S to IL-S-responsive cells, we detected only two complexes, consisting of IL-S and IL-5Ra or of IL-S and ,c (21,22,37,38).…”

Section: Discussionmentioning

confidence: 99%

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: Discussionmentioning

confidence: 99%

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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“…The murine B cell leukemia cell line Bcl1 can be stimulated to differentiate to an antibody-secreting cell using lipopolysaccharide (LPS) and cytokines (39,40). We tested combinations of previously described differentiation stimuli including IL-2, IL-5, and LPS and found that the combination of IL-5 and LPS was as efficient a differentiation stimulus as the combination of all three (not shown).…”

Section: Il-5 and Lps Treatment Induces Differentiation In Bcl1 Cells-mentioning

confidence: 99%

Bcl-xL Protein Protects from C/EBP Homologous Protein (CHOP)-dependent Apoptosis during Plasma Cell Differentiation

Gaudette

Iwakoshi

Boise

2014

Journal of Biological Chemistry

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Background: UPR-associated death signals are activated during plasma cell differentiation. Results: Bcl-x L sequesters Bim during plasma cell differentiation, preventing apoptosis. Conclusion: Bcl-x L dependence during plasma cell differentiation protects the cell from the UPR activation necessary for ER remodeling. Significance: Bcl-2 family dynamics are crucial for both the development of plasma cells and the treatment of diseases of abnormal plasma cells.

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“…Binding studies using radiolabled murine IL-5 have shown that high-and low-affinity IL-5 receptors arc expressed on BCL1-B20 cells and other B lineage cells (17). Furthermore, we detected the phosphorylation of several proteins with IL-5 stimulation (33).…”

Section: Discussionmentioning

confidence: 66%

“…Binding assay was performed according to the protocol described by Mita et al (17). Briefly, after BCL1-B20 cells were incubated at 37 C with various amounts of 1251-IL-5 for 10 min, unbound IL-5 was removed and then radioactivity was counted.…”

Section: Methodsmentioning

confidence: 99%

“…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%

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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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Receptors for T cell-replacing factor/interleukin 5. Specificity, quantitation, and its implication.

Cited by 76 publications

References 50 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.

Bcl-xL Protein Protects from C/EBP Homologous Protein (CHOP)-dependent Apoptosis during Plasma Cell Differentiation

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

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