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High-affinity interaction between interleukin-11 and S100P protein.

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Kazakov AS,Sokolov AS,Rastrygina VA,Solovyev VV,Ismailov RG,Mikhailov RV,Ulitin AB,Yakovenko AR,Mirzabekov TA,Permyakov EA,Permyakov SE

doi

10.1016/j.bbrc.2015.11.024

subject

Has Abstract

pub_date

2015-12-25 00:00:00

pages

733-8

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(15)30894-9

journal_volume

468

pub_type

杂志文章

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