Oncostatin M binds the high-affinity leukemia inhibitory factor receptor

New Biol. 1992 Jan;4(1):61-5.

Abstract

Oncostatin M (OSM) is a glycoprotein cytokine that was recently demonstrated to be structurally and functionally related to the leukemia inhibitory factor (LIF). We have investigated the binding of each cytokine to a variety of cellular receptors including those on solid tumor lines, leukemic cells, endothelial cells, macrophages, and cells transfected with the recently cloned low-affinity LIF receptor, and to a soluble form of the LIF receptor. LIF is incapable of binding either high- or low-affinity OSM receptors, yet OSM is capable of binding the high-affinity but not the low-affinity LIF receptor. Since the presence of high-affinity LIF receptors correlates with the biological activity of LIF on a wide range of target cells, we predict that OSM should have similar effects on LIF-responsive cells.

MeSH terms

  • Animals
  • Cloning, Molecular
  • Cytokines / metabolism*
  • Growth Inhibitors
  • Humans
  • Interleukin-6*
  • Leukemia Inhibitory Factor
  • Leukemia Inhibitory Factor Receptor alpha Subunit
  • Lymphokines
  • Oncostatin M
  • Peptides / metabolism*
  • Receptors, Cytokine*
  • Receptors, Immunologic / genetics
  • Receptors, Immunologic / metabolism*
  • Receptors, OSM-LIF
  • Tumor Cells, Cultured

Substances

  • Cytokines
  • Growth Inhibitors
  • Interleukin-6
  • LIF protein, human
  • LIFR protein, human
  • Leukemia Inhibitory Factor
  • Leukemia Inhibitory Factor Receptor alpha Subunit
  • Lymphokines
  • OSM protein, human
  • Peptides
  • Receptors, Cytokine
  • Receptors, Immunologic
  • Receptors, OSM-LIF
  • Oncostatin M