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• W2071470983 abstract "1. The aims of the present study were to investigate the pharmacological effects of quercetin on wild-type (WT) and mutant (I502A) human (h) Kv1.5 channel currents (I(kur)) and to identify whether mutation in the S6 segment is critical to activation of I(kur) by quercetin. 2. Experiments were performed on WT and site-directed mutant hKv1.5 channels, which were stably expressed in Xenopus oocytes using the two-microelectrode voltage-clamp technique. 3. Quercetin increased WT hKv1.5 channel current in a concentration-, voltage- and time-dependent manner, with an EC(50) of 37.8 micromol/L and a negative shift in the steady state activation and inactivation curves. Quercetin accelerated channel activation and inactivation, significantly decreasing activation and inactivation time constants. However, mutating the I502 residue to Ala abolished the activating effect of quercetin. Quercetin did not modify the activation and inactivation kinetics of I502A channels. As an anti-oxidant, tanshinone IIA (4 micromol/L) inhibited the H(2)O(2)-induced activation of WT hKv1.5 channels. In contrast, quercetin had no significant effect. 4. We conclude that: (i) quercetin preferentially binds to and increases the current amplitude of WT hKv1.5 channels; (ii) Ile502, an aliphatic and neutral amino acid residue residing in the S6 segment, is important in quercetin binding; and (iii) quercetin-induced changes in the properties of WT hKv1.5 channels may be foreign to its own anti-oxidant action." @default.
• W2071470983 created "2016-06-24" @default.
• W2071470983 creator A5006655487 @default.
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• W2071470983 date "2009-01-27" @default.
• W2071470983 modified "2023-10-10" @default.
• W2071470983 title "QUERCETIN ACTIVATES HUMAN Kv1.5 CHANNELS BY A RESIDUE I502 IN THE S6 SEGMENT" @default.
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• W2071470983 doi "https://doi.org/10.1111/j.1440-1681.2008.05061.x" @default.
• W2071470983 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/18986330" @default.
• W2071470983 hasPublicationYear "2009" @default.
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