Human/mouse interleukin-1 receptor/receptor accessory protein interactions in IL-1beta-induced NFkappaB activation

FEBS Lett. 1998 Jun 16;429(3):307-11. doi: 10.1016/s0014-5793(98)00537-7.

Abstract

We examined whether functional heterologous complexes between human IL-1RI (hIL-1RI) and murine IL-1R accessory protein (mIL-1RAcP) can be formed, utilizing human fibroblast HEK 293 cells and murine fibroblast C127 cells, nontransfected or stably transfected with hIL-1RI (C127-hIL-1RI), respectively. In non-transfected C127 cells, IL-1beta signalled through the mIL-1RI-mIL-1RAcP complex and activated NFkappaB p50/p65 heterodimers. In C127-hIL-1RI cells, IL-1beta signalled through the hIL-1RI and activated both p65/p65 and p50/p65 NFkappaB complexes, where only the activation of NFkappaB p65/p65 was dependent on mIL-1RAcP. Thus, clearly both homologous and heterologous IL-1RI-IL-1RAcP interactions support NFkappaB translocation, but with differences in signalling pattern.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Biological Transport
  • Cell Compartmentation
  • Cell Line
  • Cell Nucleus / metabolism
  • Fibroblasts / cytology
  • Humans
  • Interleukin-1 / pharmacology*
  • Interleukin-1 Receptor Accessory Protein
  • Mice
  • NF-kappa B / metabolism*
  • Protein Binding
  • Proteins / genetics
  • Proteins / metabolism*
  • Receptors, Interleukin-1 / metabolism*
  • Receptors, Interleukin-1 Type I
  • Recombinant Proteins / metabolism
  • Signal Transduction
  • Species Specificity
  • Transfection

Substances

  • IL1RAP protein, human
  • Il1rap protein, mouse
  • Interleukin-1
  • Interleukin-1 Receptor Accessory Protein
  • NF-kappa B
  • Proteins
  • Receptors, Interleukin-1
  • Receptors, Interleukin-1 Type I
  • Recombinant Proteins