High-affinity interaction between interleukin-11 and S100P protein
| Autor: | Sergei E. Permyakov, Tajib Mirzabekov, Andrei S. Sokolov, Roman Mikhailov, Andrey R. Yakovenko, Alexei S. Kazakov, Ramis G. Ismailov, Eugene A. Permyakov, Ulitin Andrei Borisovich, Solovyev Valery Vladimirovich, Victoria A. Rastrygina |
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| Rok vydání: | 2015 |
| Předmět: |
Binding Sites
Chemistry HEK 293 cells Biophysics Nuclear Proteins Cell Biology Plasma protein binding Interleukin-11 Biochemistry Protein–protein interaction Dissociation constant Kinetics HEK293 Cells Extracellular Humans Calcium Signal transduction Binding site Carrier Proteins Receptor Molecular Biology Protein Binding |
| Zdroj: | Biochemical and Biophysical Research Communications. 468:733-738 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/j.bbrc.2015.11.024 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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