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Flavonolignans As a Novel Class of Sodium Pump Inhibitors
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SYSNO ASEP 0462025 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Flavonolignans As a Novel Class of Sodium Pump Inhibitors Tvůrce(i) Kubala, M. (CZ)
Čechová, P. (CZ)
Geletičová, J. (CZ)
Biler, M. (CZ)
Štenclová, T. (CZ)
Trouillas, P. (FR)
Biedermann, David (MBU-M) RID, ORCIDZdroj.dok. Frontiers in Physiology. - : Frontiers Research Foundation - ISSN 1664-042X
Roč. 7, Mar 30 (2016), s. 115Poč.str. 12 s. Jazyk dok. eng - angličtina Země vyd. CH - Švýcarsko Klíč. slova sodium pump ; Na+/K+-ATPase ; flavonolignans Vědní obor RIV CE - Biochemie CEP GA15-03037S GA ČR - Grantová agentura ČR Institucionální podpora MBU-M - RVO:61388971 UT WOS 000372965100001 DOI 10.3389/fphys.2016.00115 Anotace We examined the inhibitory effects of three flavonolignans and their dehydro-derivatives, taxifolin and quercetin on the activity of the Na+/K+-ATPase (NKA). The flavonolignans silychristin, dehydrosilychristin and dehydrosilydianin inhibited NKA with IC50 of 110 +/- 40 mu M, 38 +/- 8 mu M, and 36 +/- 14 mu M, respectively. Using the methods of molecular modeling, we identified several possible binding sites for these species on NKA and proposed the possible mechanisms of inhibition. The binding to the extracellular- or cytoplasmic C-terminal sites can block the transport of cations through the plasma membrane, while the binding on the interface of cytoplasmic domains can inhibit the enzyme allosterically. Fluorescence spectroscopy experiments confirmed the interaction of these three species with the large cytoplasmic segment connecting transmembrane helices 4 and 5 (C45). Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2017
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