High-affinity interaction between interleukin-11 and S100P protein

Biochem Biophys Res Commun. 2015 Dec 25;468(4):733-8. doi: 10.1016/j.bbrc.2015.11.024. Epub 2015 Nov 6.

Abstract

Interleukin-11 (IL-11) and S100P are oncoproteins co-expressed in numerous cancers, which might favor their interaction during oncogenesis. We have explored the possibility of this interaction by surface plasmon resonance spectroscopy, intrinsic fluorescence, and chemical crosslinking. Recombinant forms of IL-11 and S100P interact with each other under physiological level of calcium ions. IL-11 molecule has at least two S100P-binding sites with dissociation constants of 32 nM and 288 nM, which is 5-13-fold lower than its affinity to extracellular domain of IL-11 receptor subunit α. S100P does not alter IL-11-induced STAT3 activation in HEK293 cells co-expressing IL-11 receptors, but could affect other tumorigenic signaling pathways. The highly specific IL-11 - S100P interaction occurring under physiologically relevant conditions should be taken into consideration upon development of the antineoplastics inhibiting IL-11 signaling.

Keywords: Cancer; Interleukin; Protein–protein interaction; S100 protein; STAT3.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Calcium / chemistry*
  • Calcium / metabolism*
  • Carrier Proteins / chemistry*
  • Carrier Proteins / metabolism*
  • HEK293 Cells
  • Humans
  • Interleukin-11 / chemistry*
  • Interleukin-11 / metabolism*
  • Kinetics
  • Nuclear Proteins / chemistry*
  • Nuclear Proteins / metabolism*
  • Protein Binding

Substances

  • Carrier Proteins
  • IL11 protein, human
  • Interleukin-11
  • Nuclear Proteins
  • S100PBP protein, human
  • Calcium