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Статья
Interferon beta activity is modulated via binding of specific S100 proteins
2021
Interferon-β (IFN-β) is a pleiotropic cytokine used for therapy of multiple sclerosis, which is also effective in suppression of viral and bacterial infections and cancer. Recently, we reported a highly specific interaction between IFN-β and S100P lowering IFN-β cytotoxicity to cancer cells (Int J Biol Macromol. 2020; 143: 633–639). S100P is a member of large family of multifunctional Ca2+-binding proteins with cytokine-like activities. To probe selectivity of IFN-β—S100 interaction with respect to S100 proteins, we used surface plasmon resonance spectroscopy, chemical crosslinking, and crystal violet assay. Among the thirteen S100 proteins studied S100A1, S100A4, and S100A6 proteins exhibit strictly Ca2+-dependent binding to IFN-β with equilibrium dissociation constants, Kd, of 0.04–1.5 µM for their Ca2+-bound homodimeric forms. Calcium depletion abolishes the S100—IFN-β interactions. Monomerization of S100A1/A4/A6 decreases Kd values down to 0.11–1.0 nM. Interferon-α is unable of binding to the S100 proteins studied. S100A1/A4 proteins inhibit IFN-β-induced suppression of MCF-7 cells viability. The revealed direct influence of specific S100 proteins on IFN-β activity uncovers a novel regulatory role of particular S100 proteins, and opens up novel approaches to enhancement of therapeutic efficacy of IFN-β. © 2020 by the authors. Licensee MDPI, Basel, Switzerland.
Цитирование
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Версии
- 1. Version of Record от 2021-04-27
Метаданные
Название журнала
- International Journal of Molecular Sciences
Том
- 21
Выпуск
- 24
Страницы
- 1-23
Ключевые слова
- alpha2b interferon; beta1a interferon; calcium ion; calcyclin; calgranulin C; calvasculin; crystal violet; homodimer; protein S 100; animal cell; Article; bioinformatics; calcium depletion; cell viability; controlled study; cross linking; dissociation constant; female; human; human cell; MCF-7 cell line; nonhuman; protein protein interaction; surface plasmon resonance
Издатель
- MDPI AG
Тип документа
- journal article
Тип лицензии Creative Commons
- CC
Правовой статус документа
- Свободная лицензия
Источник
- scopus
