Molecular cloning and expression of an IL-6 signal transducer, gp130

  title={Molecular cloning and expression of an IL-6 signal transducer, gp130},
  author={Masahiko Hibi and Masaaki Murakami and Mikiyoshi Saito and Toshio Hirano and Tetsuya Taga and Tadamitsu Kishimoto},

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Activation of the signal transducer glycoprotein 130 by both IL-6 and IL-11 requires two distinct binding epitopes.
There is a substantial difference in the mechanism of receptor engagement by cytokines that signal via gp130, suggesting a common mode of recognition of helical cytokines by class I cytokine receptors.
Structure of an Extracellular gp130 Cytokine Receptor Signaling Complex
The cross-reactivity of gp130 is apparently due to a chemical plasticity evident in the amphipathic gp130 cytokine-binding sites, which enhances the complementarity of the viral IL-6–gp130 binding interfaces.
IL-6 receptor and mechanism of signal transduction.
The N-terminus of gp130 is critical for the formation of the high-affinity interleukin-6 receptor complex.
It is demonstrated, using biosensor analysis and size-exclusion chromatography, that modification of the N-terminus of sgp130 interferes with the in vitro in solution formation of the stable hexameric IL-6 receptor complex, and the critical involvement of theN-terminal Ig-like domain of gp130 in tethering the two trimers to form the stablehexamer.
Molecular cloning and expression of the human interleukin 5 receptor
The human IL-5 receptor characterized in this paper is essential for signal transduction, because expression of this molecule in murine IL-3-dependent cell line FDC-P1 allowed these cells to proliferate in response to IL- 5.
Interleukin-6 Family of Cytokines Induced Activation of Different Functional Sites Expressed by gp130 Transducing Protein*
It is indicated that in addition to functional site(s) required by the whole family of IL-6 type cytokines to transduce the signal insight the cell, specific cognate functional sites were recruited by OSM, CNTF, or IL-11.


Interleukin-6 triggers the association of its receptor with a possible signal transducer, gp130
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 IL-6 receptor expression by monoclonal and polyclonal antibodies.
Immunoprecipitation of radiolabeled IL-6R with polyclonal antibodies showed that the Mr of a mature IL- 6R was 80 kDa and its value was reduced to 50K after treatment with O- and N-glycanase and neuraminidase, indicating that IL-7R is a glycoprotein.
Cloning and expression of the human interleukin-6 (BSF-2/IFN beta 2) receptor.
A complementary DNA encoding the human IL-6 receptor (IL-6-R) has now been isolated and consists of 468 amino acids, including a signal peptide of approximately 19 amino acids and a domain of approximately 90 amino acids that is similar to a domain in the immunoglobulin (Ig) superfamily.
cDNA expression cloning of the IL-1 receptor, a member of the immunoglobulin superfamily.
A direct expression strategy was used to clone the receptor for IL-1 from mouse T cells and the product of the cloned complementary DNA binds bothIL-1 alpha and IL-2 beta in a manner indistinguishable from that of the native T cell IL- 1 receptor.
A monoclonal antibody with IL-3-like activity blocks IL-3 binding and stimulates tyrosine phosphorylation.
Evidence is presented that one of these monoclonal antibodies, M7B1-5.1-F9 (F9), interacts with the mouse IL-3 receptor or with part of anIL-3R complex, suggesting that spare receptors may exist.