Direct association of interleukin-6 with a 130-kDa component of the interleukin-6 receptor system

J Biol Chem. 1993 Jan 25;268(3):2149-53.


Affinity cross-linking of membrane bound 125I-interleukin-6 (IL-6) on several cell lines revealed a three-band pattern of IL-6-containing cross-linked complexes with molecular masses of 100, 120, and 150 kDa. To identify the membrane components that were associated with IL-6 in the three complexes, we employed the Denny-Jaffe reagent, a heterobifunctional, cleavable cross-linker that allows the transfer of 125I from the ligand to its receptor. Samples cross-linked with Denny-Jaffe reagent were analyzed by two-dimensional SDS-polyacrylamide gel electrophoresis in which the cross-linker was cleaved prior to the second dimension. This analysis revealed that IL-6 directly associates with a 130-kDa membrane protein thus allowing the formation of the 150-kDa complex. In addition, both the 100- and 120-kDa cross-linked complexes were shown to include an 80-kDa membrane glycoprotein associated with one and two IL-6 molecules, respectively.

MeSH terms

  • Animals
  • Cross-Linking Reagents
  • Electrophoresis, Gel, Two-Dimensional
  • Interleukin-6 / metabolism*
  • Lymphocytes / metabolism
  • Lymphoma, Large B-Cell, Diffuse
  • Macromolecular Substances
  • Membrane Glycoproteins / metabolism
  • Mice
  • Molecular Weight
  • Multiple Myeloma
  • Photochemistry
  • Receptors, Immunologic / metabolism*
  • Receptors, Interleukin-6
  • Recombinant Proteins / metabolism
  • Succinimides
  • Tumor Cells, Cultured


  • Cross-Linking Reagents
  • Interleukin-6
  • Macromolecular Substances
  • Membrane Glycoproteins
  • Receptors, Immunologic
  • Receptors, Interleukin-6
  • Recombinant Proteins
  • Succinimides
  • disuccinimidyl suberate