Highly specific interaction of monomeric S100P protein with interferon beta.

A1 Journal article (refereed)

Internal Authors/Editors

Publication Details

List of Authors: Kazakov AS, Mayorov SA, Deryusheva EI, Avkhacheva NV, Denessiouk KA, Denesyuk AI, Rastrygina VA, Permyakov EA, Permyakov SE.
Publisher: Elsevier
Publication year: 2020
Journal: International Journal of Biological Macromolecules
Journal acronym: Int J Biol.Macromol.
Volume number: 143
Start page: 633
End page: 639


S100 proteins are EF-hand calcium-binding proteins of vertebrates
exerting numerous intra- and extracellular actions and involved into
multiple diseases. Some of S100 proteins serve as extracellular damage
signals via interaction with receptors. Although several S100 proteins
directly bind specific cytokines, this phenomenon remains underexplored.
Using chemical crosslinking, intrinsic fluorescence and surface plasmon
resonance spectroscopies, we show that S100P protein interacts with
interferon beta (IFN-β) depending on calcium level and oligomeric state
of S100P. Dimeric Ca2+-loaded S100P binds IFN-β with equilibrium dissociation constants, Kd, of 0.05-0.6 μM. S100P monomerization favors this interaction decreasing Kd
values down to 0.3-2 nM. Calcium depletion drastically lowers S100P
affinity to IFN-β. Other related EF-hand proteins studied (calmodulin,
α-parvalbumin and S100G) do not bind IFN-β, thereby confirming
selectivity of the S100P - IFN-β interaction. Crystal violet assay
reveals that the S100P binding suppresses IFN-β cytotoxicity to MCF-7
breast cancer cells. Since several cancers (breast, colon, lung, liver,
etc.) exhibit dysregulated functioning of S100P and IFN-β, their
interaction could be relevant to the cancer progression and directed
therapeutic interventions.

Last updated on 2020-26-02 at 03:15