Regulation of Interleukin-13 Receptor Constituents on Mature Human B Lymphocytes*

  title={Regulation of Interleukin-13 Receptor Constituents on Mature Human B Lymphocytes*},
  author={Haruki Ogata and Dwayne Ford and Nicola Mitri Kouttab and Thomas C. King and Natalio Vita and Adrian J. Minty and Johanna D. Stoeckler and D M Morgan and Christopher R. Girasole and John W Morgan and Abby L. Maizel},
  journal={The Journal of Biological Chemistry},
  pages={9864 - 9871}
Human B cells stimulated through both their immunoglobulin and CD40 receptors up-regulate 745 ± 51 interleukin (IL)-13 ligand binding sites with an affinity of 0.91 ± 0.08 nm within 24 h. IL-13 binds primarily to the IL-13Rα1 with subsequent sequestration of the IL-4Rα into the complex. IL-13Rα1 may also be found in those receptors capable of binding IL-4. γ chain (γc) participates in receptors capable of binding IL-4 but is not found in association with bound IL-13. Dimeric receptors composed… 

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IL-13 receptors and signaling pathways: an evolving web.

  • G. Hershey
  • Biology, Medicine
    The Journal of allergy and clinical immunology
  • 2003
The current understanding of the IL-13 receptors and signaling pathways is summarized, supported by many in vivo observations, including that administration ofIL-13 resulted in allergic inflammation, tissue-specific overexpression of IL- 13 in the lungs of transgenic mice resulted in airway inflammation and mucus hypersecretion.

The human B cell response to IL-13 is dependent on cellular phenotype as well as mode of activation.

Evaluation of proliferation, receptor message, ligand binding protein production, and the response to putatively synergistic cytokines reveals that IL-2 is the predominant lymphokine utilized by memory cells, in contradistinction to IL-13, which along with IL-4 are the predominant moieties for naive lymphocytes.

Induction of the IL-13 receptor α2-chain by IL-4 and IL-13 in human keratinocytes: involvement of STAT6, ERK and p38 MAPK pathways

It is demonstrated, for the first time, that IL-4 andIL-13 can induce IL-13Rα2 expression in keratinocytes, and that the ERK and p38 MAPK together with JAK2 and STAT6 play a critical role in this process.

IFN-γ, IL-4 and IL-13 modulate responsiveness of human airway smooth muscle cells to IL-13

Pre-treatment with IL-4 andIL-13, but not IFN-γ, induced desensitization of the HASM cells to IL-13 as measured by eotaxin secretion and calcium transients to histamine.

Characterization of IL-4 and IL-13 signals dependent on the human IL-13 receptor alpha chain 1: redundancy of requirement of tyrosine residue for STAT3 activation.

The results suggest that STAT3 activation is involved with IL-4 andIL-13 signals in human B cells along with the activation of STAT6, and that there is a unique sequence in IL-13R alpha 1 to activate STAT3.

A soluble form of IL-13 receptor alpha 1 promotes IgG2a and IgG2b production by murine germinal center B cells.

It is proposed that IL-13R alpha 1 is a molecule involved in B cell differentiation, using a mechanism that may involve regulation of IL-6-responsive elements and the ligand for the sIL-13r might be a component of the IL- 13R complex or a counterstructure yet to be defined.

Functional characterization of IL-13 receptor α2 gene promoter: a critical role of the transcription factor STAT6 for regulated expression

It is reported that TNFα synergizes with either IL-4 orIL-13 in inducing the IL-13Rα2 chain at both the mRNA and protein levels in the HaCaT human keratinocyte cell line.



Modulation of Interleukin (IL)-13 Binding and Signaling by the γc Chain of the IL-2 Receptor*

Although γchas been shown to enhance IL-4 binding and function in some cell types, its influence on IL-13R function in tumor cells appear to be largely negative.

Receptor for Interleukin 13

It is reported here that human renal cell carcinoma (RCC) cells express large numbers of functional IL-13R, which may be a novel subunit of the IL-4R, and that even in the absence of common chain IL-5 and IL-3 were able to up-regulate intracellular adhesion molecule-1 antigen on RCC cells.

Interleukin 13 is a B cell stimulating factor

It is shown that IL-13 acts at different stages of the B cell maturation pathway: (a) it enhances the expression of CD23/Fc epsilon RII and class II MHC antigens on resting B cells; (b) it stimulates B cell proliferation in combination with anti-Ig and anti-CD40 antibodies; and (c) it induces IgE synthesis.

Cloning and Characterization of a Specific Interleukin (IL)-13 Binding Protein Structurally Related to the IL-5 Receptor α Chain*

Cloned cDNA encoding an IL-13 binding protein with two consensus patterns characteristic of the hematopoietic cytokine receptor family and a short cytoplasmic tail shows homology with the IL-5 receptor, and to a lesser extent, with the prolactin receptor.

cDNA Cloning and Characterization of the Human Interleukin 13 Receptor α Chain*

Cloned cDNAs corresponding to the human interleukin 13 receptor α chain (IL-13Rα) resulted in substantial binding activity, indicating that both chains are essential components of the IL-13 receptor.

Interleukin 4 receptors on normal human B lymphocytes: Characterization and regulation

IL 4 displays its different biological activities on resting and activated B cells through IL 4R of the same affinity, gross biochemical structure and ability to mediate IL 4 degradation.

An Interleukin (IL)-13 Receptor Lacking the Cytoplasmic Domain Fails to Transduce IL-13-Induced Signals and Inhibits Responses to IL-4*

It is shown here that expression of the IL-13 receptor-α in two factor-dependent cell lines, the premyeloid FD5 and the T lymphoid CT4, conferred the ability to grow continuously in response to IL- 13 and to respond toIL-4 with tyrosine phosphorylation of JAK1, Tyk2, IL-4Rα, IRS-2, and STAT6.

Structure of IL-13 receptor: analysis of subunit composition in cancer and immune cells.

Data from various cancer and normal cell lines are examined for the presence of mRNA for IL-13R alpha and alpha, as well as IL-4R p140 (termed beta chain) and IL-2R gamma c chains, providing a direct support for the model of IL- 13R which consists of three different forms composed of different subunits.

Interleukin-13 is a potent activator of JAK3 and STAT6 in cells expressing interleukin-2 receptor-γ and interleukin-4 receptor-α

IL13 can mimic IL4-induced heterodimerization of IL2Rγ and IL4Rα, with consequent marked activation of JAK3 and the transcription factor STAT6, and it is proposed that IL13 is capable of interacting with multiple receptor subunits in a cell-dependent and combinatorial manner.