Interleukin-6 triggers the association of its receptor with a possible signal transducer, gp130

  title={Interleukin-6 triggers the association of its receptor with a possible signal transducer, gp130},
  author={Tetsuya Taga and Masahiko Hibi and Y. Hirata and Katsuhiko Yamasaki and Kiyoshi Yasukawa and Tadashi Matsuda and Toshio Hirano and Tadamitsu Kishimoto},
The soluble interleukin-6 receptor and related proteins.
  • S. Rose-John
  • Biology
    Best practice & research. Clinical endocrinology & metabolism
  • 2015
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.
Soluble IL-6 receptor potentiates the antagonistic activity of soluble gp130 on IL-6 responses.
SIL-6R of human plasma must be regarded as an antagonistic molecule that enhances the inhibitory activity of sgp130, a promising candidate for the development of IL-6 antagonists.
IL-6 Receptor Independent Stimulation of Human gp130 by Viral IL-61
It is demonstrated that purified recombinant vIL-6 is the first cytokine which directly binds and activates gp130, and points to a possible role of this viral cytokine in the pathophysiology of human herpes virus 8.
IL-6 receptor and mechanism of signal transduction.
The Immunoglobulin-like Module of gp130 Is Required for Signaling by Interleukin-6, but Not by Leukemia Inhibitory Factor*
It is shown that signaling by IL-6, but not LIF, is significantly reduced by mutations in the Ig-like module of gp130, and the binding of125I-labeled IL- 6 or LIF is not affected by these mutations.
Identification of a regulatory domain of the interleukin-6 receptor.
Human interleukin 4 receptor confers biological responsiveness and defines a novel receptor superfamily
In this report, the isolation and functional expression of a human IL-4-R cDNA is described, which encodes a protein that binds humanIL-4 with high affinity and can confer responsiveness to human Il-4.
Interleukin 6 and its receptor: ten years later.
  • T. Hirano
  • Biology
    International reviews of immunology
  • 1998
JAK tyrosine kinase is a key molecule that can initiate multiple signal-transduction pathways by inducing the tyrosinesine-phosphorylation of the cytokine receptor, gp130 in the case of IL-6, on which several signaling molecules are recruited, including STAT, a signal transducer and activator of transcription, and SHP-2, which links to the Ras-MAP kinase pathway.


Demonstration of a non-Tac peptide that binds interleukin 2: a potential participant in a multichain interleukin 2 receptor complex.
An IL-2 binding peptide is identified that does not react with anti-humanIL-2 receptor monoclonal antibodies, including anti-Tac on MLA 144, a gibbon ape T-cell line.
Novel interleukin-2 receptor subunit detected by cross-linking under high-affinity conditions.
The data presented are most consistent with the existence of a 70- to 77-kilodalton glycoprotein subunit (p70) which, upon associating with the 55-kilODalton low-affinity IL-2 receptor (p55), transforms it into a high-Affinity site.
Internalization of interleukin 2 is mediated by the beta chain of the high-affinity interleukin 2 receptor
The beta chain appeared to provide the essential element necessary for ligand internalization by both types of IL-2-R, and each type of receptor targeted the boundIL-2 for intracellular degradation in lysosomes.
Transmembrane signaling of interleukin 2 receptor. Conformation and function of human interleukin 2 receptor (p55)/insulin receptor chimeric molecules
Pressure of the tyrosine kinase activity by IL-2 was not observed in the chimeric receptor with the entire cytoplasmic domain of the Ins-R, and shed light on the structural conformation and functioning of the IL- 2-R complex.
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.
Complementary DNA for a novel human interleukin (BSF-2) that induces B lymphocytes to produce immunoglobulin
The molecular cloning, structural analysis and functional expression of the cDNA encoding human B SF-2 indicated that BSF-2 is functionally and structurally unlike other known proteins.
B-cell-stimulatory factor 2 (beta 2 interferon) functions as a second signal for interleukin 2 production by mature murine T cells.
The experiments demonstrate that either murine TAF or human IL-6 can restore the ability of purified T cells to proliferate in response to Con A or antibodies against the T-cell antigen receptor.
A T3-like protein complex associated with the antigen receptor on murine T cells
A murine T3-like protein complex appears to be more complicated than human T3, containing three monomeric glyco-proteins (21–28K), two of which have N-linked carbohydrate side chains and a novel family of TCR-associated homo- and heterodimers.
Interleukin 2 high-affinity receptor expression requires two distinct binding proteins
Two distinct proteins identical to those already identified on the leukemic cells could be crosslinked covalently to radiolabeled IL-2, both of which are required for high- affinity IL- 2 binding.