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

      , , , , , , ,
      Cell
      Elsevier BV

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          Abstract

          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.

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          Author and article information

          Journal
          Cell
          Cell
          Elsevier BV
          00928674
          August 1989
          August 1989
          : 58
          : 3
          : 573-581
          Article
          10.1016/0092-8674(89)90438-8
          2788034
          97e6a2f8-fd2b-446d-84cd-d628ab16fe4c
          © 1989

          https://www.elsevier.com/tdm/userlicense/1.0/

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