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

Interleukin-6 mediates pleiotropic functions in various types of cells through its specific receptor (IL-6-R), the cDNA of which has already been cloned. We report here that an 80 kd single polypeptide chain (IL-6-R) is involved in IL-6 binding and that IL-6 triggers the association of this receptor with a non-ligand-binding membrane glycoprotein, gp130. The association takes place at 37 degrees C within 5 min and is stable for at least 40 min in the presence of IL-6, but does not occur at 0 degree C. Human IL-6-R can associate with a murine gp130 homolog and is functional in murine cells. Mutant IL-6-R lacking the intracytoplasmic portion is functional, suggesting that the two polypeptide chains interact to involve their extracellular portion. In fact, a soluble IL-6-R lacking the transmembrane and intracytoplasmic domains can associate with gp130 in the presence of IL-6 and mediate its function. These findings indicate that the complex of IL-6 and IL-6-R can interact with a non-ligand-binding membrane glycoprotein, gp130, extracellularly and can provide the IL-6 signal.

Pubmed ID: 2788034


  • Taga T
  • Hibi M
  • Hirata Y
  • Yamasaki K
  • Yasukawa K
  • Matsuda T
  • Hirano T
  • Kishimoto T



Publication Data

August 11, 1989

Associated Grants


Mesh Terms

  • Animals
  • Cytoplasm
  • DNA Mutational Analysis
  • Humans
  • In Vitro Techniques
  • Interleukin-6
  • Interleukins
  • Macromolecular Substances
  • Membrane Glycoproteins
  • Mice
  • Molecular Weight
  • Precipitin Tests
  • Protein Binding
  • Receptors, Immunologic
  • Receptors, Interleukin-6
  • Solubility